|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
32-553 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 1039.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 32 VANEPVLAFTQGSPERDALQKALKDLKGRTEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALA 111
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 112 ARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPS 191
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 192 T-NSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFG 270
Cdd:cd07123 161 VwNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 271 DTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSA 350
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 351 CSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVE 430
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDP-DDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 431 PCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKS 510
Cdd:cd07123 400 PTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1367104953 511 TGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKP 553
Cdd:cd07123 480 TGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
33-563 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 996.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 33 ANEPVLAFTQGSPERDALQKALKDLKGRTEAIPCVVGDEEVWTSDV-QYQVSPFNHGHKVAKFCYADKSLLNKAIEAALA 111
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNErIPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 112 ARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPS 191
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 192 TNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGD 271
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 272 TVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSAC 351
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 352 SRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSSPS-LTILAGGKCDDSVGYFVE 430
Cdd:TIGR01236 321 SRLYVPHSKWPEFKSDLLAELQSVKVGDP-DDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEaLTILYGGKYDDSQGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 431 PCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKS 510
Cdd:TIGR01236 400 PTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKC 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1367104953 511 TGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWSYAYMQ 563
Cdd:TIGR01236 480 TGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
47-551 |
0e+00 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 821.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 47 RDALQKALKDLKG-RTEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRA 125
Cdd:cd07083 1 RRAMREALRRVKEeFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 126 QIFLKAADMLSGPRRAEILAKTMVGqGKTVIQaEIDAAAELIDFFRFNAKYAVELEGQQPI--SVPPSTNSMVYRGLeGF 203
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEvvPYPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 204 VAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGI 282
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 283 NFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWP 362
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 363 QIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSspSLTILAGGKCDDSVGYFVEPCIVESKDPQEP 442
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEEN-GTDLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFVAPTVVEEVPPKAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 443 IMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQdKDVVQEATKVLrnAAGNFYINDKSTGSIVGQQPFGG 522
Cdd:cd07083 395 IAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRK-REHLEEARREF--HVGNLYINRKITGALVGVQPFGG 471
|
490 500
....*....|....*....|....*....
gi 1367104953 523 ARASGTNDKPGGPHYILRWTSPQVIKETH 551
Cdd:cd07083 472 FKLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
103-547 |
3.12e-142 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 417.76 E-value: 3.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTVIQAEIDAAaELIDFFRFNAKYAVELEG 182
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLET-GKPIEEALGEVA-RAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 183 QQPISVPPSTNSMVYRGLEGFVAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQF 261
Cdd:cd07078 79 EVIPSPDPGELAIVRREPLGVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 262 VPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAF 341
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 342 EYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKC 421
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPL-DPDTDMGPLISAAQLDRVLAYIEDAKAEGA-KLLCGGKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 422 DDS-VGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRna 500
Cdd:cd07078 311 LEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE--EEAIELANDTE-YGLAAGVFTRDLERALRVAERLE-- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1367104953 501 AGNFYINDKSTGsIVGQQPFGGARASGTNdKPGGPHYILRWTSPQVI 547
Cdd:cd07078 386 AGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
61-551 |
6.03e-139 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 411.06 E-value: 6.03e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 61 TEAIPCVVGDEEVWTSDVQYQ--VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgp 138
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFdvINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 139 RRAEILAKTMV-GQGKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPISVPPSTNSMVYRglE--GFVAAISPFNFTAI 215
Cdd:COG1012 80 ERREELAALLTlETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETIPSDAPGTRAYVRR--EplGVVGAITPWNFPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 216 GGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHL 294
Cdd:COG1012 157 LAAWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 295 WKQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSR 374
Cdd:COG1012 237 AAAAAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 375 IKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSpSLTILAGGKC-DDSVGYFVEPCIVESKDPQEPIMKEEIFGPVL 453
Cdd:COG1012 311 LKVGDPL-DPGTDMGPLISEAQLERVLAYIEDAVAE-GAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 454 SVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGTNDKpG 533
Cdd:COG1012 389 SVIPFDD--EEEAIALAND-TEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-G 461
|
490
....*....|....*...
gi 1367104953 534 GPHYILRWTSPQVIKETH 551
Cdd:COG1012 462 GREGLEEYTETKTVTIRL 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-549 |
1.42e-134 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 401.22 E-value: 1.42e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 34 NEPVLAFTQGSpERDALQKALKDLK---GRTeaIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAAL 110
Cdd:cd07124 3 NEPFTDFADEE-NRAAFRAALARVReelGRE--YPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 111 AARKEWDLKPIADRAQIFLKAADMLSgPRRAEiLAKTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPISVP 189
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALLR-RRRFE-LAAWMVLEvGKNWAEADADVA-EAIDFLEYYAREMLRLRGFPVEMVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 190 PSTNSMVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPL 268
Cdd:cd07124 157 GEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 269 FGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKC 348
Cdd:cd07124 236 VGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 349 SACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGGKCDDSV--G 426
Cdd:cd07124 316 SACSRVIVHESVYDEFLERLVERTKALKVGDP-EDPEVYMGPVIDKGARDRIRRYIEIGKSEGRL--LLGGEVLELAaeG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 427 YFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYI 506
Cdd:cd07124 393 YFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIAND-TEYGLTGGVFSRSPEHLERARREFE--VGNLYA 467
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1367104953 507 NDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKE 549
Cdd:cd07124 468 NRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTE 510
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
82-547 |
1.20e-125 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 376.49 E-value: 1.20e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQAEI 160
Cdd:pfam00171 12 INPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE--ERKDELAELETlENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 161 DAAaELIDFFRFNAKYAVELEGQqPISVPPSTNSMVYRGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSD 236
Cdd:pfam00171 89 EVD-RAIDVLRYYAGLARRLDGE-TLPSDPGRLAYTRREPLGVVGAITPWNFPL---LLPAwkiAPALAaGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 237 TAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECG 316
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 317 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKS 396
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDP-LDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 397 FARIKKWLEHARSSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsY 476
Cdd:pfam00171 317 LERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDE--EEAIEIANDTE-Y 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1367104953 477 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGqQPFGGARASGTNDKpGGPHYILRWTSPQVI 547
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGRE-GGPYGLEEYTEVKTV 459
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
34-550 |
1.85e-117 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 357.32 E-value: 1.85e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 34 NEPVLAFTQgsPE-RDALQKALKDLK---GRTeaIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAA 109
Cdd:PRK03137 7 HEPFTDFSV--EEnVEAFEEALKKVEkelGQD--YPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 110 LAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAkTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKYAVEL-EGQQPIS 187
Cdd:PRK03137 83 LEAFETWKKWSPEDRARILLRAAAIIR-RRKHEFSA-WLVKEaGKPWAEADADTA-EAIDFLEYYARQMLKLaDGKPVES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 188 VPPSTNSMVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADG 266
Cdd:PRK03137 160 RPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 267 PLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQ 346
Cdd:PRK03137 239 SEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 347 KCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGGKCDDSVG 426
Cdd:PRK03137 319 KCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN--AYMGPVINQASFDKIMSYIEIGKEEGRL--VLGGEGDDSKG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 427 YFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYI 506
Cdd:PRK03137 395 YFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD--FDHALEIANN-TEYGLTGAVISNNREHLEKARREFH--VGNLYF 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1367104953 507 NDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKET 550
Cdd:PRK03137 470 NRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEM 513
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
107-547 |
8.88e-105 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 319.56 E-value: 8.88e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 107 EAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTvIQAEIDAAAELIDFFRFNAKYAVELEGQQPI 186
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLET-GKP-IEEALGEVARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 187 SVPPSTNSMVYRGLEGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPAD 265
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 266 GPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGG 345
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 346 QKCSACSRLYVPHSLWPQIKGRLLeehsrikvgdpaedfgtffsavidaksfarikkwleharsspsltilaggkcddsv 425
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV-------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 426 gyfvepCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFY 505
Cdd:cd06534 257 ------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDE--EEAIALANDTE-YGLTAGVFTRDLNRALRVAERLR--AGTVY 325
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1367104953 506 INDKSTGSiVGQQPFGGARASGTNDKpGGPHYILRWTSPQVI 547
Cdd:cd06534 326 INDSSIGV-GPEAPFGGVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
34-549 |
2.08e-103 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 321.04 E-value: 2.08e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 34 NEPVLAFTQgSPERDALQKAL---KDLKGRTeaIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAAL 110
Cdd:TIGR01237 3 HEPFTDFAD-EENRQAFFKALatvKEQLGKT--YPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 111 AARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPI-SVP 189
Cdd:TIGR01237 80 KAFEAWKKTDPEERAAILFKAAAIVR-RRRHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVnSRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 190 PSTNSMVYRGLeGFVAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPL 268
Cdd:TIGR01237 158 GETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 269 FGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKC 348
Cdd:TIGR01237 237 VGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 349 SACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTIlaGGKCDDSVGYF 428
Cdd:TIGR01237 317 SAGSRAVVHEKVYDEVVERFVEITESLKVGPP-DSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVS--GGCGDDSKGYF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 429 VEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVDSTtSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIND 508
Cdd:TIGR01237 394 IGPTIFADVDRKARLAQEEIFGPVVAFIRASD--FDEALEIANNT-EYGLTGGVISNNRDHINRAKAEFE--VGNLYFNR 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1367104953 509 KSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKE 549
Cdd:TIGR01237 469 NITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTE 509
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
33-540 |
1.23e-96 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 303.73 E-value: 1.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 33 ANEP-VLAFTQGSPERDALQKALKDLK-GRTEAIPCVVGDEEVWTsDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAAL 110
Cdd:cd07125 1 ANSSfVNRIFDLEVPLEALADALKAFDeKEWEAIPIINGEETETG-EGAPVIDPADHERTIGEVSLADAEDVDAALAIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 111 AARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKYAVELEGQQPISVPP 190
Cdd:cd07125 80 AAFAGWSATPVEERAEILEKAADLLEA-NRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 191 S-TNSMVYRGLeGFVAAISPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPAD 265
Cdd:cd07125 158 GeLNGLELHGR-GVFVCISPWNFplaIFTGQIAA---ALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 266 GPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGG 345
Cdd:cd07125 234 GEEIGEALVAHPRIDGVIFTGSTETAKLINRALAE---RDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 346 QKCSACSRLYVPHSLWP----QIKGRLLEehsrIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGGKC 421
Cdd:cd07125 311 QRCSALRLLYLQEEIAErfieMLKGAMAS----LKVGDPW-DLSTDVGPLIDKPAGKLLRAHTELMRGEAWL--IAPAPL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 422 DDSVGYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYPDDKYKETLQLVDStTSYGLTGAVFSQDKDvvqEATKVLRNA- 500
Cdd:cd07125 384 DDGNGYFVAPGIIEIVGIFD--LTTEVFGPILHVIRFKAEDLDEAIEDINA-TGYGLTLGIHSRDER---EIEYWRERVe 457
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1367104953 501 AGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR 540
Cdd:cd07125 458 AGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLR 497
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
44-547 |
1.30e-79 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 270.15 E-value: 1.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 44 SPERDALQKALKDLKGRTEAIPCVVGDeevwTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIAD 123
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 124 RAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAeIDAAAELIDFFRFnakYAVELEGQ--QPISVP-PS--TNSMVYR 198
Cdd:PRK11904 609 RAAILERAADLLEA-NRAELIALCVREAGKTLQDA-IAEVREAVDFCRY---YAAQARRLfgAPEKLPgPTgeSNELRLH 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 199 GLEGFVAaISPFNFT-AIggnLAG--APALM-GNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPLFGDTV 273
Cdd:PRK11904 684 GRGVFVC-ISPWNFPlAI---FLGqvAAALAaGNTVIAKPAEqTPLIAAEAV-KLLHEAGIPKDVLQLLPGDGATVGAAL 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 274 TSSEHLCGINFTGSVptfkhlwkQVAQNLDRfhtfpRLAG----------ECGGKNFHFVHRSADVESVVSGTLRSAFEY 343
Cdd:PRK11904 759 TADPRIAGVAFTGST--------ETARIINR-----TLAArdgpivpliaETGGQNAMIVDSTALPEQVVDDVVTSAFRS 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 344 GGQKCSACSRLYVPHSLWPQ----IKGRLLEehsrIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPslTILAGG 419
Cdd:PRK11904 826 AGQRCSALRVLFVQEDIADRviemLKGAMAE----LKVGDPR-LLSTDVGPVIDAEAKANLDAHIERMKREA--RLLAQL 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 420 KCDDS--VGYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATK 495
Cdd:PRK11904 899 PLPAGteNGHFVAPTAFEIDSISQ--LEREVFGPILHVIRY---KASDLDKVIDAinATGYGLTLGIHSRIEETADRIAD 973
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1367104953 496 VLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 547
Cdd:PRK11904 974 RVR--VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
46-547 |
1.63e-78 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 268.34 E-value: 1.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 46 ERDALQKALKDLKGRT-EAIPCVVGDEEvwTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADR 124
Cdd:COG4230 540 VLAALSAALAAAAEKQwQAAPLIAGEAA--SGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 125 AQIFLKAADMLSGpRRAEILAKTMVGQGKTvIQaeiDAAAEL---IDFFRFnakYAVELEGQQpisvppsTNSMVYRGLe 201
Cdd:COG4230 618 AAILERAADLLEA-HRAELMALLVREAGKT-LP---DAIAEVreaVDFCRY---YAAQARRLF-------AAPTVLRGR- 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 202 GFVAAISPFNFTaiggnLAG-----APALM-GNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPLFGDTVT 274
Cdd:COG4230 682 GVFVCISPWNFP-----LAIftgqvAAALAaGNTVLAKPAEqTPLIAARAV-RLLHEAGVPADVLQLLPGDGETVGAALV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 275 SSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFprLAgECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRL 354
Cdd:COG4230 756 ADPRIAGVAFTGSTETARLINRTLAARDGPIVPL--IA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVL 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 355 YVPHSLWPQ----IKGRLLEehsrIKVGDPAE---DFGtffsAVIDAKSFARIKKWLEHARSSPslTILAGGKCDDSV-- 425
Cdd:COG4230 833 CVQEDIADRvlemLKGAMAE----LRVGDPADlstDVG----PVIDAEARANLEAHIERMRAEG--RLVHQLPLPEECan 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 426 GYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATKVLRnaAGN 503
Cdd:COG4230 903 GTFVAPTLIEIDSISD--LEREVFGPVLHVVRY---KADELDKVIDAinATGYGLTLGVHSRIDETIDRVAARAR--VGN 975
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1367104953 504 FYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 547
Cdd:COG4230 976 VYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTV 1019
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
77-536 |
2.72e-73 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 241.38 E-value: 2.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 77 DVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTV 155
Cdd:cd07097 14 DGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELE--ARKEELARLLTrEEGKTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 156 IQA--EIDAAaelIDFFRFNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNF-TAIGGNLAgAPALM-GNVVL 231
Cdd:cd07097 92 PEArgEVTRA---GQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFpIAIPAWKI-APALAyGNTVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 232 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprl 311
Cdd:cd07097 168 FKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQL---- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 312 agECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 391
Cdd:cd07097 244 --EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE-GVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 392 IDAKSFARIKKWLEHARSSPSlTILAGG---KCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQ 468
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGA-KLVYGGerlKRPDE-GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD--YDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 469 LVDStTSYGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINDKSTGsiVGQQ-PFGGARASGTNDKPGGPH 536
Cdd:cd07097 397 IAND-TEFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEA 460
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
33-544 |
1.56e-71 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 249.01 E-value: 1.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 33 ANEPVLAftqgsperdALQKALKDLKGRT-EAIPCVVGDEevwTSDVQYQV-SPFNHGHKVAKFCYADKSLLNKAIEAAL 110
Cdd:PRK11905 533 SDEATLA---------ALDEALNAFAAKTwHAAPLLAGGD---VDGGTRPVlNPADHDDVVGTVTEASAEDVERALAAAQ 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 111 AARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIqaeiDAAAEL---IDFFRFNAKYAVELEGQQPIs 187
Cdd:PRK11905 601 AAFPEWSATPAAERAAILERAADLMEA-HMPELFALAVREAGKTLA----NAIAEVreaVDFLRYYAAQARRLLNGPGH- 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 188 vppstnsmvyRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPA 264
Cdd:PRK11905 675 ----------KPL-GPVVCISPWNFPlAIfTGQIAAALV-AGNTVLAKPAEqTPLIAARAV-RLLHEAGVPKDALQLLPG 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 265 DGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYG 344
Cdd:PRK11905 742 DGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGP---PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSA 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 345 GQKCSACSRLYVPHSLWPQI----KGRLLEehsrIKVGDPAE---DFGtffsAVIDAKSFARIKKWLEHARSSPSL--TI 415
Cdd:PRK11905 819 GQRCSALRVLCLQEDVADRVltmlKGAMDE----LRIGDPWRlstDVG----PVIDAEAQANIEAHIEAMRAAGRLvhQL 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 416 LAGGKCDDsvGYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEA 493
Cdd:PRK11905 891 PLPAETEK--GTFVAPTLIEIDSISD--LEREVFGPVLHVVRF---KADELDRVIDDinATGYGLTFGLHSRIDETIAHV 963
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1367104953 494 TKvlRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSP 544
Cdd:PRK11905 964 TS--RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
83-528 |
1.65e-68 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 228.25 E-value: 1.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 83 SPFnHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--E 159
Cdd:cd07149 5 SPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE--ERREEFARTIALEaGKPIKDArkE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 160 IDAAaelIDFFRFNAKYAVELEGQQ-PI-SVPPSTNSM--VYRGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVL 231
Cdd:cd07149 82 VDRA---IETLRLSAEEAKRLAGETiPFdASPGGEGRIgfTIREPIGVVAAITPFNFPL---NLVAhkvGPAIAaGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 232 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFPRL 311
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 312 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 391
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDE-DTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 392 IDAKSFARIKKWLEHARSSPSlTILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVD 471
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEGGA-RLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPF--DTLDEAIAMAN 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1367104953 472 StTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGT 528
Cdd:cd07149 381 D-SPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSSTFR-VDHMPYGGVKESGT 433
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
102-543 |
4.17e-68 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 226.64 E-value: 4.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAElIDFFRFNAKYAVEL 180
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE--ERRDEIADWLIREsGSTRPKAAFEVGAA-IAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 181 EGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAVYRILREAGLPPNI 258
Cdd:cd07104 79 EGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 259 IQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESVVSGTLR 338
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKK------VALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 339 SAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSpSLTILAG 418
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDP-DTVIGPLINERQVDRVHAIVEDAVAA-GARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 419 GKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLR 498
Cdd:cd07104 311 GTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDD--EEAVELAND-TEYGLSAAVFTRD---LERAMAFAE 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1367104953 499 NA-AGNFYINDKST--GSIVgqqPFGGARASGTnDKPGGPHYI-----LRWTS 543
Cdd:cd07104 382 RLeTGMVHINDQTVndEPHV---PFGGVKASGG-GRFGGPASLeefteWQWIT 430
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
105-528 |
2.19e-67 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 225.31 E-value: 2.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAAELidfFRFNAKYAVELE 181
Cdd:cd07145 26 AIEVAEKAKDVMSNLPAYKRYKILMKVAELIE--RRKEELAKLLTIEvGKPIKQSrvEVERTIRL---FKLAAEEAKVLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 182 GQQPIS--VPPSTNSMVYRGLE--GFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAVYRILREAG 253
Cdd:cd07145 101 GETIPVdaYEYNERRIAFTVREpiGVVGAITPFNFPA---NLFAhkiAPAIaVGNSVVVKPSSNTPLTAIELAKILEEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 254 LPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVV 333
Cdd:cd07145 178 LPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGG------TGKKVALELGGSDPMIVLKDADLERAV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSl 413
Cdd:cd07145 252 SIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDE-STDLGPLISPEAVERMENLVNDAVEKGG- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 414 TILAGGKCDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQEA 493
Cdd:cd07145 330 KILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDD--EEAVEIANS-TEYGLQASVFTND---INRA 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 1367104953 494 TKVLRN-AAGNFYINDKSTGSIvGQQPFGGARASGT 528
Cdd:cd07145 402 LKVARElEAGGVVINDSTRFRW-DNLPFGGFKKSGI 436
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
88-507 |
2.24e-66 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 222.91 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQA--EIDAAA 164
Cdd:cd07088 23 GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR--ENADELAKLIVEeQGKTLSLArvEVEFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 165 eliDFFRFNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKPSDTAML 240
Cdd:cd07088 101 ---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFF---LIArklAPALVtGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 241 ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNF 320
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI----TKVSL--ELGGKAP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 321 HFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARI 400
Cdd:cd07088 249 AIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA-ATDMGPLVNEAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 401 KKWLEHARSSPSlTILAGGKCDDS-VGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDStTSYGLT 479
Cdd:cd07088 328 EEMVERAVEAGA-TLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELAND-SEYGLT 403
|
410 420
....*....|....*....|....*...
gi 1367104953 480 GAVFSQDKDVVQEATKVLRnaAGNFYIN 507
Cdd:cd07088 404 SYIYTENLNTAMRATNELE--FGETYIN 429
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
25-545 |
1.10e-65 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 222.09 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 25 KHTSSLKVANEPVLAFTQGSPERDALQKalkdlkgrTEAIPcVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNK 104
Cdd:TIGR01238 8 KNSLGIDLDNESELKPLEAQIHAWADKT--------WQAAP-IIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKYAVELEGQQ 184
Cdd:TIGR01238 79 AIDSAQQAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDVLGEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 185 piSVPPstnsmvyrglEGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQF 261
Cdd:TIGR01238 157 --SVES----------RGVFVCISPWNFPlAIfTGQISAALA-AGNTVIAKPAEqTSLIAYRAV-ELMQEAGFPAGTIQL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 262 VPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfHTFPRLAgECGGKNFHFVHRSADVESVVSGTLRSAF 341
Cdd:TIGR01238 223 LPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED--APVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 342 EYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEdFGTFFSAVIDAKSFARIKKWLEH----ARSSPSLTILA 417
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHL-LTTDVGPVIDAEAKQNLLAHIEHmsqtQKKIAQLTLDD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 418 GGKCDDsvGYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYpddKYKETLQLVD--STTSYGLTGAVFSQDKDVVQEATK 495
Cdd:TIGR01238 379 SRACQH--GTFVAPTLFELDDIAE--LSEEVFGPVLHVVRY---KARELDQIVDqiNQTGYGLTMGVHSRIETTYRWIEK 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1367104953 496 VLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQ 545
Cdd:TIGR01238 452 HAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
103-543 |
3.53e-65 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 219.51 E-value: 3.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEG 182
Cdd:cd07150 24 ERAIAAAYDAFPAWAATTPSERERILLKAAEIME--RRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 183 QQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQF 261
Cdd:cd07150 102 ETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 262 VPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAF 341
Cdd:cd07150 182 VTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 342 EYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKC 421
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPR-DPDTVIGPLISPRQVERIKRQVEDAVAKGA-KLLTGGKY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 422 DdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSvyVYPDDKYKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA- 500
Cdd:cd07150 334 D---GNFYQPTVLTDVTPDMRIFREETFGPVTS--VIPAKDAEEALELAND-TEYGLSAAILTND---LQRAFKLAERLe 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1367104953 501 AGNFYINDkSTGSIVGQQPFGGARASGTNdKPGGPHYI-----LRWTS 543
Cdd:cd07150 405 SGMVHIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
91-542 |
6.96e-65 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 219.53 E-value: 6.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 91 VAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAaELIDF 169
Cdd:cd07131 28 VGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLK--KRKEELARLVTREmGKPLAEGRGDVQ-EAIDM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 170 FRFNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRI 248
Cdd:cd07131 105 AQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFpVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVEL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSAD 328
Cdd:cd07131 185 FAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCAR------PNKRVALEMGGKNPIIVMDDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHAR 408
Cdd:cd07131 259 LDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE-ETDMGPLINEAQLEKVLNYNEIGK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 409 SSpSLTILAGG----KCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSvyVYPDDKYKETLQLVDStTSYGLTGAVFS 484
Cdd:cd07131 338 EE-GATLLLGGerltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVA--LIEVSSLEEAIEIAND-TEYGLSSAIYT 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367104953 485 QDkdvVQEATKVLRNA-AGNFYINDKSTGSIVgQQPFGGARASGTNDKPGGPHYILRWT 542
Cdd:cd07131 414 ED---VNKAFRARRDLeAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFT 468
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
88-527 |
2.29e-64 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 217.30 E-value: 2.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQA--EIDAAA 164
Cdd:cd07103 7 GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIR--ERAEDLARLLTlEQGKPLAEArgEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 165 eliDFFRFNAKYAVELEGQqpiSVPPSTNS---MVYRGLEGFVAAISPFNFTAigGNLA--GAPAL-MGNVVLWKPSDTA 238
Cdd:cd07103 85 ---SFLEWFAEEARRIYGR---TIPSPAPGkriLVIKQPVGVVAAITPWNFPA--AMITrkIAPALaAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 239 MLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfpRLAGECGGk 318
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK------RVSLELGG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 319 NFHF-VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSF 397
Cdd:cd07103 230 NAPFiVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDE-GTDMGPLINERAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 398 ARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYG 477
Cdd:cd07103 309 EKVEALVEDAVAKGA-KVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTE--DEVIARAND-TPYG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1367104953 478 LTGAVFSQDKDVVQEATKVLRnaAGNFYINdksTGSIVG-QQPFGGARASG 527
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALE--AGMVGIN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
97-547 |
2.84e-64 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 216.63 E-value: 2.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLS--GPRRAEILAKTmvgQGKTVIQA--EIDAAAeliDFFRF 172
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEanAEELARLLTLE---QGKPLAEAqfEVGGAV---AWLRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 173 NAKYAVELEGQQpiSVPPSTNSMVYRGLeGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKPSDTAMLASYAVYRI 248
Cdd:cd07106 90 TASLDLPDEVIE--DDDTRRVELRRKPL-GVVAAIVPWNFPLL---LAAwkiAPALLaGNTVVLKPSPFTPLCTLKLGEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 249 LREAgLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSAD 328
Cdd:cd07106 164 AQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKR------VTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHAR 408
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDP-GTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 409 SSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkd 488
Cdd:cd07106 315 AK-GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDE--DEVIARAND-SEYGLGASVWSSD-- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367104953 489 vVQEATKV-LRNAAGNFYINdkSTGSIVGQQPFGGARASGTndkpG---GPHYILRWTSPQVI 547
Cdd:cd07106 389 -LERAEAVaRRLEAGTVWIN--THGALDPDAPFGGHKQSGI----GvefGIEGLKEYTQTQVI 444
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
67-527 |
9.17e-64 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 216.28 E-value: 9.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 67 VVGDEEVWTSdvqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK 146
Cdd:cd07086 8 VGSGGETFTS-----RNPAN-GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALR--KKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 147 TM---VGQGKTVIQAEIDaaaELIDFfrfnAKYAVELEGQQPISVPPSTNS-----MVYRGLeGFVAAISPFNF-TAIGG 217
Cdd:cd07086 80 LVsleMGKILPEGLGEVQ---EMIDI----CDYAVGLSRMLYGLTIPSERPghrlmEQWNPL-GVVGVITAFNFpVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 218 -NLAgaPALM-GNVVLWKPSDTAMLASYAVYRILREA----GLPPNIIQFVPADGPlFGDTVTSSEHLCGINFTGSVPTf 291
Cdd:cd07086 152 wNAA--IALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEV- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 292 khlWKQVAQNLDRfhTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEE 371
Cdd:cd07086 228 ---GRRVGETVAR--RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 372 HSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSpSLTILAGGKC--DDSVGYFVEPCIVESKDPQEPIMKEEIF 449
Cdd:cd07086 303 YKQVRIGDPLDE-GTLVGPLINQAAVEKYLNAIEIAKSQ-GGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 450 GPVLsvYVYPDDKYKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA---AGNFYINDKSTGSIVGqQPFGGARAS 526
Cdd:cd07086 381 APIL--YVIKFDSLEEAIAINND-VPQGLSSSIFTED---LREAFRWLGPKgsdCGIVNVNIPTSGAEIG-GAFGGEKET 453
|
.
gi 1367104953 527 G 527
Cdd:cd07086 454 G 454
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
82-528 |
4.57e-63 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 213.97 E-value: 4.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQA--- 158
Cdd:cd07093 2 FNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEA-RADELALLESLDTGKPITLArtr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 EIDAAAElidFFRFNAKYAVELEGQqpiSVPPSTNSMVY--RGLEGFVAAISPFNFTAIggnLAG---APAL-MGNVVLW 232
Cdd:cd07093 80 DIPRAAA---NFRFFADYILQLDGE---SYPQDGGALNYvlRQPVGVAGLITPWNLPLM---LLTwkiAPALaFGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 233 KPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprla 312
Cdd:cd07093 151 KPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSL----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 313 gECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVI 392
Cdd:cd07093 226 -ELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDP-LDPDTEVGPLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 393 DAKSFARIKKWLEHARSSPSlTILAGGKCDDSV----GYFVEPCIVESKDPQEPIMKEEIFGPVLSvyVYPDDKYKETLQ 468
Cdd:cd07093 304 SKEHLEKVLGYVELARAEGA-TILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVT--VIPFDDEEEAIE 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1367104953 469 LVDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN-----DKSTgsivgqqPFGGARASGT 528
Cdd:cd07093 381 LANDTP-YGLAAYVWTRDLGRAHRVARRLE--AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
82-527 |
5.69e-63 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 214.48 E-value: 5.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-TMVGQGKTVIQA 158
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIR--EDAEELARlETLNTGKTLRES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 EIDAAaELIDFFRFNAKYAVELEGQQpISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:cd07119 95 EIDID-DVANCFRYYAGLATKETGEV-YDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 238 AMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGG 317
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALELGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 318 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSF 397
Cdd:cd07119 247 KNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNG-LDADTEMGPLVSAEHR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 398 ARIKKWLEHARSSPSlTILAGGK------CDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVD 471
Cdd:cd07119 326 EKVLSYIQLGKEEGA-RLVCGGKrptgdeLAK--GYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE--EEAIRLAN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367104953 472 STTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDksTGSIVGQQPFGGARASG 527
Cdd:cd07119 401 DTP-YGLAGAVWTKDIARANRVARRLR--AGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
74-527 |
1.09e-61 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 210.62 E-value: 1.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 74 WTSDVQyqvSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGK 153
Cdd:cd07151 10 RTIDVL---NPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILE-ERRDEIVEWLIRESGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 154 TVIQAEIDAAAElIDFFRFNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNV 229
Cdd:cd07151 85 TRIKANIEWGAA-MAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPL---HLSMrsvAPALaLGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 230 VLWKP-SDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtf 308
Cdd:cd07151 161 VVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 309 pRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFF 388
Cdd:cd07151 236 -KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP-DTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 389 SAVIDAKSFARIKKWLEHARSSpSLTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQ 468
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEE-GATLLVGGEAEGNV---LEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE--EEALE 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367104953 469 LVDStTSYGLTGAVFSQDkdvVQEATKV-LRNAAGNFYINDKStgsiVGQQP---FGGARASG 527
Cdd:cd07151 388 LAND-TEYGLSGAVFTSD---LERGVQFaRRIDAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
88-527 |
1.80e-61 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 209.85 E-value: 1.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTV--IQAEIDAAAE 165
Cdd:cd07090 7 GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLR-ERNDEIARLETIDNGKPIeeARVDIDSSAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 166 LIDFFrfnAKYAVELEGQQpisVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:cd07090 86 CLEYY---AGLAPTLSGEH---VPLPGGSFAYTRREplGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 243 YAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHF 322
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH------VTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 323 VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKK 402
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPL-DEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 403 WLEHARSSPSlTILAGG-------KCDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDSTTs 475
Cdd:cd07090 312 YIESAKQEGA-KVLCGGervvpedGLEN--GFYVSPCVLTDCTDDMTIVREEIFGPVMSILPF--DTEEEVIRRANDTT- 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1367104953 476 YGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSIvgQQPFGGARASG 527
Cdd:cd07090 386 YGLAAGVFTRD---LQRAHRVIAQlQAGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
82-527 |
4.65e-61 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 208.44 E-value: 4.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA-- 158
Cdd:cd07094 4 HNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLK--KRAEEFAKIIACEgGKPIKDArv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 EIDAAaelIDFFRFNAKYAVELEGQQpISVPPSTNSMVYRGLE-----GFVAAISPFNFTAiggNLAG---APAL-MGNV 229
Cdd:cd07094 81 EVDRA---IDTLRLAAEEAERIRGEE-IPLDATQGSDNRLAWTirepvGVVLAITPFNFPL---NLVAhklAPAIaTGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 230 VLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFP 309
Cdd:cd07094 154 VVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 310 RLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFS 389
Cdd:cd07094 226 RIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDE-DTDVG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 390 AVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQL 469
Cdd:cd07094 305 PLISEEAAERVERWVEEAVEAGA-RLLCGGERDGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRY--DDFEEAIRI 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367104953 470 VDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDkSTGSIVGQQPFGGARASG 527
Cdd:cd07094 379 ANS-TDYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
88-527 |
8.28e-61 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 207.68 E-value: 8.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAELI 167
Cdd:cd07115 7 GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDVPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 168 DFFRFNAKYAVELEGQqpiSVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYA 244
Cdd:cd07115 86 DTFRYYAGWADKIEGE---VIPVRGPFLNYTVREpvGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 245 VYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVH 324
Cdd:cd07115 163 IAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKR------VSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 325 RSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWL 404
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL-DPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 405 EHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFS 484
Cdd:cd07115 316 DVGREEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDE--EEALRIANGTE-YGLAAGVWT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1367104953 485 QDKDVVQEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 527
Cdd:cd07115 392 RDLGRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
87-527 |
1.92e-59 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 204.32 E-value: 1.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 87 HGHKVAKFCYADKSLLNKAIEAALAA--RKEW-DLKPIAdRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTViqAEIDA 162
Cdd:cd07114 6 TGEPWARVPEASAADVDRAVAAARAAfeGGAWrKLTPTE-RGKLLRRLADLIE--ANAEELAELETRDnGKLI--RETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 163 -AAELIDFFRFNAKYAVELEGQ-QPISVPPSTNSMVYRGLeGFVAAISPFN----FTAiggnLAGAPAL-MGNVVLWKPS 235
Cdd:cd07114 81 qVRYLAEWYRYYAGLADKIEGAvIPVDKGDYLNFTRREPL-GVVAAITPWNspllLLA----KKLAPALaAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 236 DTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGEC 315
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 316 GGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAK 395
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDP-ETQMGPLATER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 396 SFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVD 471
Cdd:cd07114 309 QLEKVERYVARAREEGA-RVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDE--EEAIALAN 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367104953 472 StTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVgqQPFGGARASG 527
Cdd:cd07114 386 D-SEYGLAAGIWTRDLARAHRVARAIE--AGTVWVNTYRALSPS--SPFGGFKDSG 436
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
82-527 |
3.80e-59 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 203.36 E-value: 3.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGprRAEILAKTMVGQ-GKTV-IQAE 159
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLALEtGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 160 IDAAAeLIDFFRFNAKYAVELEGQqpiSVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSD 236
Cdd:cd07108 79 PEAAV-LADLFRYFGGLAGELKGE---TLPFGPDVLTYTVREplGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 237 TAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtfPRLAG--- 313
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 314 ECGGKNFHFVHRSADVESVVSGTLRSA-FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AEDFGtffs 389
Cdd:cd07108 225 ELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPldeATDIG---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 390 AVIDAKSFARIKKWLEHARSSPSLTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKE 465
Cdd:cd07108 301 AIISEKQFAKVCGYIDLGLSTSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKD--EDE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1367104953 466 TLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKstgsiVGQQP---FGGARASG 527
Cdd:cd07108 379 VIAMANDSH-YGLAAYVWTRDLGRALRAAHALE--AGWVQVNQG-----GGQQPgqsYGGFKQSG 435
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
82-527 |
8.18e-59 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 202.57 E-value: 8.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPfNHGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA 158
Cdd:cd07118 2 RSP-AHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIR--ARRERLALIETLEsGKPISQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 --EIDAAAELidfFRFNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTA--IGGNLAGAPAlMGNVVLWKP 234
Cdd:cd07118 79 rgEIEGAADL---WRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 235 SD-----TAMLAsyavyRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfp 309
Cdd:cd07118 155 SEftsgtTLMLA-----ELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKK----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 310 rLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFS 389
Cdd:cd07118 225 -VSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDP-ETKVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 390 AVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQL 469
Cdd:cd07118 303 AIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIAL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367104953 470 VDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgQQPFGGARASG 527
Cdd:cd07118 381 AND-TVYGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
88-545 |
1.91e-58 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 202.29 E-value: 1.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAA-RKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAEL 166
Cdd:cd07113 25 EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQ-HGEELAQLETLCSGKSIHLSRAFEVGQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 167 IDFFRFNAKYAVELEGQqpiSVPPSTNSM--------VYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:cd07113 104 ANFLRYFAGWATKINGE---TLAPSIPSMqgerytafTRREPVGVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 238 AMLASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGG 317
Cdd:cd07113 181 TPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL------ELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 318 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSF 397
Cdd:cd07113 254 KNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE-SVMFGPLANQPHF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 398 ARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYG 477
Cdd:cd07113 333 DKVCSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE--EELIQLIND-TPFG 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367104953 478 LTGAVFSQDkdvvqeATKVLRNA----AGNFYIN-----DKSTgsivgqqPFGGARASGTNdKPGGPHYILRWTSPQ 545
Cdd:cd07113 409 LTASVWTNN------LSKALRYIprieAGTVWVNmhtflDPAV-------PFGGMKQSGIG-REFGSAFIDDYTELK 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
105-528 |
2.14e-58 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 201.45 E-value: 2.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQA---EIDAAAELIDFFrfnAKYAVELE 181
Cdd:cd07107 24 AVAAARAAFPEWRATTPLERARMLRELATRLR--EHAEELALIDALDCGNPVSAmlgDVMVAAALLDYF---AGLVTELK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 182 GQqpiSVPPSTNSMVYRGLE--GFVAAISPFN----FTAigGNLAgAPALMGNVVLWKPSDTAMLASYAVYRILREAgLP 255
Cdd:cd07107 99 GE---TIPVGGRNLHYTLREpyGVVARIVAFNhplmFAA--AKIA-APLAAGNTVVVKPPEQAPLSALRLAELAREV-LP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 256 PNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVVSG 335
Cdd:cd07107 172 PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAE------GIKHVTLELGGKNALIVFPDADPEAAADA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 336 TLRSA-FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSLT 414
Cdd:cd07107 246 AVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDP-ATTMGPLVSRQQYDRVMHYIDSAKREGARL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 415 ILAGGKCDDSV---GYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQ 491
Cdd:cd07107 325 VTGGGRPEGPAlegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDE--AEMVAQANG-VEYGLTAAIWTND---IS 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1367104953 492 EATKVLRNA-AGNFYINDKST---GSivgqqPFGGARASGT 528
Cdd:cd07107 399 QAHRTARRVeAGYVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
83-549 |
5.22e-58 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 200.23 E-value: 5.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 83 SPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQA--EI 160
Cdd:cd07101 2 APFT-GEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHAfeEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 161 DAAAELIDFFRFNAKYAVELEGQQPiSVPPSTNSMVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKPSD 236
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRG-AIPVLTRTTVNRRPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 237 TAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTssEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECG 316
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGC------SLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 317 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSAVIDAKS 396
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLG-AALDYGPDMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 397 FARIKKWLEHARSSPSlTILAGGKCDDSVG-YFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTS 475
Cdd:cd07101 307 LDRVTAHVDDAVAKGA-TVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADD--DEAIELAND-TD 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367104953 476 YGLTGAVFSQDKDVVQEATKVLRnaAGNFYIND---KSTGSIvgQQPFGGARASGTNDKpGGPHYILRWTSPQVIKE 549
Cdd:cd07101 383 YGLNASVWTRDGARGRRIAARLR--AGTVNVNEgyaAAWASI--DAPMGGMKDSGLGRR-HGAEGLLKYTETQTVAV 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
97-527 |
5.42e-58 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 200.55 E-value: 5.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 97 ADKSLLNKAIEAALAARKEWDLK-PIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNA 174
Cdd:cd07089 16 AGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALE--ARKEELRALLVAEvGAPVMTARAMQVDGPIGHLRYFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 175 KYAVELEGQQPISVPPS----TNSMVYRGLEGFVAAISPFNFtAIGGNLAG-APAL-MGNVVLWKPSDTAMLASYAVYRI 248
Cdd:cd07089 94 DLADSFPWEFDLPVPALrggpGRRVVRREPVGVVAAITPWNF-PFFLNLAKlAPALaAGNTVVLKPAPDTPLSALLLGEI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSAD 328
Cdd:cd07089 173 IAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLL------ELGGKSANIVLDDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHAR 408
Cdd:cd07089 247 LAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA-DPGTVMGPLISAAQRDRVEGYIARGR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 409 SSPSlTILAGGKCDDS--VGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQD 486
Cdd:cd07089 326 DEGA-RLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDD--DEAVRIAND-SDYGLSGGVWSAD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1367104953 487 KDVVQEATKVLRnaAGNFYINDKSTGSIVGqqPFGGARASG 527
Cdd:cd07089 402 VDRAYRVARRIR--TGSVGINGGGGYGPDA--PFGGYKQSG 438
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
82-527 |
3.47e-57 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 198.24 E-value: 3.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEI 160
Cdd:cd07147 4 TNPYT-GEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE--ERFEELAETIVLEaGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 161 DAAaELIDFFRFNAKYAVELEGQ-QPISVPPSTN---SMVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNVVLW 232
Cdd:cd07147 81 EVA-RAIDTFRIAAEEATRIYGEvLPLDISARGEgrqGLVRRFPIGPVSAITPFNFPL---NLVAhkvAPAIaAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 233 KPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtfpRLA 312
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--------KVV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 313 GECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVI 392
Cdd:cd07147 228 LELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDD-ATDVGPMI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 393 DAKSFARIKKWLEHARSSPSlTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDS 472
Cdd:cd07147 307 SESEAERVEGWVNEAVDAGA-KLLTGGKRDGAL---LEPTILEDVPPDMEVNCEEVFGPVVTVEPY--DDFDEALAAVND 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1367104953 473 tTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASG 527
Cdd:cd07147 381 -SKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
104-555 |
3.47e-56 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 197.02 E-value: 3.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILaktmvgqgkTVIQAEI-----DAAAELIDFF---RFNAK 175
Cdd:PRK09407 58 AAFARARAAQRAWAATPVRERAAVLLRFHDLVLE-NREELL---------DLVQLETgkarrHAFEEVLDVAltaRYYAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 176 YAVELEGQQPIS--VPPSTNSMVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKP-SDTAMLASYAVyRI 248
Cdd:PRK09407 128 RAPKLLAPRRRAgaLPVLTKTTELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTPLTALAAV-EL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 249 LREAGLPPNIIQFVPADGPLFGDTVT-SSEHLCginFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVHRSA 327
Cdd:PRK09407 204 LYEAGLPRDLWQVVTGPGPVVGTALVdNADYLM---FTGSTATGRVLAEQAGRRLIGF------SLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 328 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSAVIDAKSFARIKKWLEHA 407
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG-AGYDYSADMGSLISEAQLETVSAHVDDA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 408 RSSPSlTILAGGKCDDSVG-YFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQD 486
Cdd:PRK09407 354 VAKGA-TVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV--DEAVERANDTP-YGLNASVWTGD 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367104953 487 KDVVQEATKVLRnaAGNFYINDKST---GSIvgQQPFGGARASGTNDKpGGPHYILRWTSPQVIKETHK-PLG 555
Cdd:PRK09407 430 TARGRAIAARIR--AGTVNVNEGYAaawGSV--DAPMGGMKDSGLGRR-HGAEGLLKYTESQTIATQRVlPLA 497
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
88-527 |
8.64e-56 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 195.12 E-value: 8.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPI--ADRAQIFLKAADMLSgpRRAEILAK--TMVGqGKTV-IQAEIDA 162
Cdd:cd07091 29 EEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIE--RDRDELAAleSLDN-GKPLeESAKGDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 163 AaELIDFFRFNAKYAVELEGQqpiSVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAM 239
Cdd:cd07091 106 A-LSIKCLRYYAGWADKIQGK---TIPIDGNFLAYTRREpiGVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 240 LASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRFhTFprlagECGGK 318
Cdd:cd07091 182 LSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKV-TL-----ELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 319 NFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFA 398
Cdd:cd07091 256 SPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP-DTFQGPQVSKAQFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 399 RIKKWLEHARSSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYvypddKYKETLQLVD--STTSY 476
Cdd:cd07091 335 KILSYIESGKKE-GATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTIL-----KFKTEDEVIEraNDTEY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1367104953 477 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINdksTGSIVGQQ-PFGGARASG 527
Cdd:cd07091 409 GLAAGVFTKDINKALRVSRALK--AGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
88-527 |
4.15e-55 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 192.45 E-value: 4.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPiADRAQIFLKAADMLSgpRRAEILAKTM-VGQGKTVIQAEIDAAA 164
Cdd:cd07109 7 GEVFARIARGGAADVDRAVQAARRAfeSGWLRLSP-AERGRLLLRIARLIR--EHADELARLEsLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 165 eLIDFFRFNAKYAVELEGQqpiSVPPSTNSMVYRGLE--GFVAAISPFNFTA-IGGNLAgAPAL-MGNVVLWKPSDTAML 240
Cdd:cd07109 84 -AARYFEYYGGAADKLHGE---TIPLGPGYFVYTVREphGVTGHIIPWNYPLqITGRSV-APALaAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 241 ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGGKNF 320
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN------VVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 321 HFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGtfFSAVIDAKSFARI 400
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD--LGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 401 KKWLEHARSSpSLTILAGG---KCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYG 477
Cdd:cd07109 311 EGFVARARAR-GARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDE--AEAIALANG-TDYG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1367104953 478 LTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVgQQPFGGARASG 527
Cdd:cd07109 387 LVAGVWTRDGDRALRVARRLR--AGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
105-540 |
3.05e-54 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 198.66 E-value: 3.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSGprRAEILAKTMVGQ-GKTVIQAeIDAAAELIDFFRFnakYAVElegq 183
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLMEA--QMQTLMGLLVREaGKTFSNA-IAEVREAVDFLRY---YAGQ---- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 184 qpisVPPSTNSMVYRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQ 260
Cdd:PRK11809 757 ----VRDDFDNDTHRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPAEqTPLIAAQAV-RILLEAGVPAGVVQ 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 261 FVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLD-RFHTFPRLAgECGGKNFHFVHRSADVESVVSGTLRS 339
Cdd:PRK11809 830 LLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQGRPIPLIA-ETGGQNAMIVDSSALTEQVVADVLAS 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 340 AFEYGGQKCSACSRLYVP-----HSLwPQIKGRLLEehsrIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSS--PS 412
Cdd:PRK11809 909 AFDSAGQRCSALRVLCLQddvadRTL-KMLRGAMAE----CRMGNP-DRLSTDIGPVIDAEAKANIERHIQAMRAKgrPV 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 413 LTILAGGKCDDSVGYFVEPCIVESKDPQEpiMKEEIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVV 490
Cdd:PRK11809 983 FQAARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRY---NRNQLDELIEQinASGYGLTLGVHTRIDETI 1057
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1367104953 491 QEATKvlRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR 540
Cdd:PRK11809 1058 AQVTG--SAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
103-527 |
8.93e-54 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 189.35 E-value: 8.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 103 NKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKT-MVGQGKTVIQAEIDAAAELIDFFRFNAKYAVE 179
Cdd:cd07112 27 DRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIE--AHRDELALLeTLDMGKPISDALAVDVPSAANTFRWYAEAIDK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 180 LEGQQPiSVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNI 258
Cdd:cd07112 105 VYGEVA-PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 259 IQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRFHTfprlagECGGKNFHFV-HRSADVESVVSGT 336
Cdd:cd07112 184 LNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWL------ECGGKSPNIVfADAPDLDAAAEAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 337 LRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSpSLTIL 416
Cdd:cd07112 258 AAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRMGALVSEAHFDKVLGYIESGKAE-GARLV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 417 AGGKCD--DSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVdSTTSYGLTGAVFSQDKDVVQEAT 494
Cdd:cd07112 336 AGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE--EEAVALA-NDSVYGLAASVWTSDLSRAHRVA 412
|
410 420 430
....*....|....*....|....*....|...
gi 1367104953 495 KVLRnaAGNFYINDKSTGSIvgQQPFGGARASG 527
Cdd:cd07112 413 RRLR--AGTVWVNCFDEGDI--TTPFGGFKQSG 441
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
105-534 |
1.35e-53 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 187.86 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTVIQAEIDAAAELIDFfrfNAKYAVELE 181
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLK--ANKEELARLIsreTGKPLWEAQTEVAAMAGKIDI---SIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 182 GQQPISVPPSTNSMVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQ 260
Cdd:cd07095 80 GERATPMAQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 261 FVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprLAGECGGKNFHFVHRSADVESVVSGTLRSA 340
Cdd:cd07095 159 LVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 341 FEYGGQKCSACSRLYVPHSLWPQ-IKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGG 419
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAE-PPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 420 KCDDSvGYFVEPCIVESKDPQEPiMKEEIFGPVLSVYVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRn 499
Cdd:cd07095 312 RLVAG-TAFLSPGIIDVTDAADV-PDEEIFGPLLQVYRY--DDFDEAIALANA-TRFGLSAGLLSDDEALFERFLARIR- 385
|
410 420 430
....*....|....*....|....*....|....*
gi 1367104953 500 aAGNFYINDKSTGSiVGQQPFGGARASGtNDKPGG 534
Cdd:cd07095 386 -AGIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPSA 417
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
95-527 |
1.88e-52 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 185.62 E-value: 1.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 95 CYAD--KSLLNKAIEAALAARKE--WDLKPiADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQA--EIDAAaelI 167
Cdd:cd07120 12 TYADggVAEAEAAIAAARRAFDEtdWAHDP-RLRARVLLELADAFE--ANAERLARLLAlENGKILGEArfEISGA---I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 168 DFFRFNAKYAVELEGQQpISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP-SDTAMLASyAV 245
Cdd:cd07120 86 SELRYYAGLARTEAGRM-IEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKPaGQTAQINA-AI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 246 YRILREA-GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVH 324
Cdd:cd07120 164 IRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRL------GLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 325 RSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG---DPAEDFGtffsAVIDAKSFARIK 401
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGpglDPASDMG----PLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 402 KWLEHARSSPSLTILAGGKCDD--SVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLT 479
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDE--AEAVALAND-TDYGLA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1367104953 480 GAVFSQDkdvVQEATKVLRN-AAGNFYINDKstGSIVGQQPFGGARASG 527
Cdd:cd07120 391 ASVWTRD---LARAMRVARAiRAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
96-535 |
2.30e-52 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 184.80 E-value: 2.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 96 YADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVI---QAEIDAAAElidFFRF 172
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE--EHADEIADWIVRESGSIRpkaGFEVGAAIG---ELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 173 NAKYAVELEGQQPISVPPSTnSMVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAVYRILR 250
Cdd:cd07152 84 AAGLPTQPQGEILPSAPGRL-SLARRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 251 EAGLPPNIIQFVPAdGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSADVE 330
Cdd:cd07152 163 EAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL------ELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSS 410
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATG-QVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 411 PSlTILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 490
Cdd:cd07152 315 GA-RLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSD--EEAVALAND-TEYGLSAGIISRDVGRA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1367104953 491 QEATKVLRnaAGNFYINDKSTGSIVgQQPFGGARASGTNDKPGGP 535
Cdd:cd07152 388 MALADRLR--TGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
103-527 |
9.30e-52 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 183.86 E-value: 9.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTV---IQAE-----IDAAAELIDFFR 171
Cdd:cd07138 39 DRAVAAARRAFPAWSATSVEERAALLERIAEAYE--ARADELAQAItleMGAPITLaraAQVGlgighLRAAADALKDFE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 172 FnakyaVELEGqqpisvppstNSMVYRGLEGFVAAISPFNFTA--IGGNLAgaPALM-GNVVLWKPSDTAMLASYAVYRI 248
Cdd:cd07138 117 F-----EERRG----------NSLVVREPIGVCGLITPWNWPLnqIVLKVA--PALAaGCTVVLKPSEVAPLSAIILAEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTfkhlWKQVAQNLDRfhTFPRLAGECGGKNFHFVHRSAD 328
Cdd:cd07138 180 LDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA----GKRVAEAAAD--TVKRVALELGGKSANIILDDAD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWL---- 404
Cdd:cd07138 254 LEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP-ATTLGPLASAAQFDRVQGYIqkgi 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 405 -EHARsspsltILAGG--KCDD-SVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTG 480
Cdd:cd07138 333 eEGAR------LVAGGpgRPEGlERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE--DEAIAIAND-TPYGLAG 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1367104953 481 AVFSQDKDVVQEATKVLRnaAGNFYINDkstGSIVGQQPFGGARASG 527
Cdd:cd07138 404 YVWSADPERARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
88-528 |
9.45e-52 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 183.30 E-value: 9.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAEL 166
Cdd:cd07092 7 GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE--ENAEELAALESRNtGKPLHLVRDDELPGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 167 IDFFRFNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAV 245
Cdd:cd07092 85 VDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 246 YRILREaGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHR 325
Cdd:cd07092 165 AELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHL------ELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 326 SADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLE 405
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDE-DTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 406 HARSspSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQ 485
Cdd:cd07092 317 RAPA--HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE--DEAIELAND-VEYGLASSVWTR 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1367104953 486 DKDVVQEATKVLRnaAGNFYINDKstGSIVGQQPFGGARASGT 528
Cdd:cd07092 392 DVGRAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
103-527 |
1.58e-51 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 183.54 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 103 NKAIEAALAA-RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTVIQAEIDAAAELIDFFRFNAKyav 178
Cdd:cd07082 41 LEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK--ENKEEVANLLmweIGKTLKDALKEVDRTIDYIRDTIEELK--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 179 ELEGQ--QPISVPPSTNS--MVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAVYRILR 250
Cdd:cd07082 116 RLDGDslPGDWFPGTKGKiaQVRREPLGVVLAIGPFNYPL---NLTVsklIPALiMGNTVVFKPATQGVLLGIPLAEAFH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 251 EAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQvaqnldrfHTFPRLAGECGGKNFHFVHRSADVE 330
Cdd:cd07082 193 DAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ--------HPMKRLVLELGGKDPAIVLPDADLE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSS 410
Cdd:cd07082 265 LAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN-GVDITPLIDPKSADFVEGLIDDAVAK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 411 PSlTILAGGKCDdsVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 490
Cdd:cd07082 344 GA-TVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI--EEAIELANK-SNYGLQASIFTKDINKA 417
|
410 420 430
....*....|....*....|....*....|....*..
gi 1367104953 491 QEATKVLRnaAGNFYINDKSTGSIvGQQPFGGARASG 527
Cdd:cd07082 418 RKLADALE--VGTVNINSKCQRGP-DHFPFLGRKDSG 451
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
88-527 |
6.85e-51 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 181.65 E-value: 6.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GK---TVIQAEIDAA 163
Cdd:PRK13473 27 GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIE--ENADEFARLESLNcGKplhLALNDEIPAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 164 aelIDFFRFNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:PRK13473 105 ---VDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 243 YAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHF 322
Cdd:PRK13473 182 LKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHL------ELGGKAPVI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 323 VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSFARIKK 402
Cdd:PRK13473 255 VFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP-DDEDTELGPLISAAHRDRVAG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 403 WLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDsTTSYGLTGAV 482
Cdd:PRK13473 334 FVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE--DQAVRWAN-DSDYGLASSV 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1367104953 483 FSQDKDVVQEATKVLRnaAGNFYINDKstGSIVGQQPFGGARASG 527
Cdd:PRK13473 411 WTRDVGRAHRVSARLQ--YGCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
82-527 |
8.04e-51 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 181.57 E-value: 8.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAA-RKEWDLK-PIADRAQIFLKAADMLSgpRRAEILAKT-MVGQGKTVIQA 158
Cdd:cd07143 27 YNPST-GKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLME--RNLDYLASIeALDNGKTFGTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 EIDAAAELIDFFRFNAKYAVELEGQqpiSVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPS 235
Cdd:cd07143 104 KRVDVQASADTFRYYGGWADKIHGQ---VIETDIKKLTYTRHEpiGVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 236 DTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhTFPRLAGEC 315
Cdd:cd07143 181 ELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKKVTLEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 316 GGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAK 395
Cdd:cd07143 256 GGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAE-DTFQGPQVSQI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 396 SFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTs 475
Cdd:cd07143 335 QYERIMSYIESGKAEGA-TVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE--EEAIKRANDST- 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1367104953 476 YGLTGAVFSQDkdvVQEATKVlRNA--AGNFYINDKSTgsIVGQQPFGGARASG 527
Cdd:cd07143 411 YGLAAAVFTNN---INNAIRV-ANAlkAGTVWVNCYNL--LHHQVPFGGYKQSG 458
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
97-527 |
2.34e-50 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 179.85 E-value: 2.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKY 176
Cdd:cd07110 16 ATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRE-RREELAELEARDNGKPLDEAAWDVD-DVAGCFEYYADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 177 AVELEGQQPISVP---PSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREA 252
Cdd:cd07110 94 AEQLDAKAERAVPlpsEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 253 GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESV 332
Cdd:cd07110 174 GLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKP------VSLELGGKSPIIVFDDADLEKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 333 VSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSpS 412
Cdd:cd07110 248 VEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEE-GVRLGPLVSQAQYEKVLSFIARGKEE-G 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 413 LTILAGGKCDDSV--GYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 490
Cdd:cd07110 326 ARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATE--DEAIALAND-SEYGLAAAVISRDAERC 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 1367104953 491 QEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 527
Cdd:cd07110 403 DRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
103-527 |
1.84e-49 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 176.61 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAeLIDFFRFNAKYAVELEG 182
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLES-RRDEFIEAMMEETGATAAWAGFNVDL-AAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 183 QQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQF 261
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 262 V---PADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPRLAgECGGKNFHFVHRSADVESVVSGTLR 338
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLK-----PVLL-ELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 339 SAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEdfgtffSAVIDAKSFARIKKWLEHARSSPSlTILAG 418
Cdd:cd07105 235 GAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL------GSLVSAAAADRVKELVDDALSKGA-KLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 419 GKCDDSV-GYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvvqeATKVL 497
Cdd:cd07105 308 GLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDE--EEAVRIAND-SEYGLSAAVFTRD------LARAL 378
|
410 420 430
....*....|....*....|....*....|....*..
gi 1367104953 498 RNA----AGNFYINdkstGSIVG---QQPFGGARASG 527
Cdd:cd07105 379 AVAkrieSGAVHIN----GMTVHdepTLPHGGVKSSG 411
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
88-547 |
2.67e-49 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 176.64 E-value: 2.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQA--EIDAAAE 165
Cdd:cd07099 6 GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALAD-HADELAELLHAETGKPRADAglEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 166 LIDFFrfnAKYAVELEGQQPISVPPST----NSMVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAML 240
Cdd:cd07099 85 AIDWA---ARNAPRVLAPRKVPTGLLMpnkkATVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 241 ASYAVYRILREAGLPPNIIQFVPADGPlfgdtvtSSEHLCG-----INFTGSVPTFKHLWKQVAQNLdrfhtFPRLAgEC 315
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGA-------TGAALIDagvdkVAFTGSVATGRKVMAAAAERL-----IPVVL-EL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 316 GGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTfFSAVIDAK 395
Cdd:cd07099 228 GGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDAD-IGPMTTAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 396 SFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTs 475
Cdd:cd07099 307 QLDIVRRHVDDAVAKGA-KALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADE--DEAIALANDSR- 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367104953 476 YGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKpGGPHYILRWTSPQVI 547
Cdd:cd07099 383 YGLSASVFSRDLARAEAIARRLE--AGAVSINDVLLTAGIPALPFGGVKDSGGGRR-HGAEGLREFCRPKAI 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
88-527 |
1.03e-48 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 176.06 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLK-PIADRAQIFLKAADMLSgpRRAEILA--KTMvGQGKTVIQAEIDAAA 164
Cdd:cd07144 33 GEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVE--KNRDLLAaiEAL-DSGKPYHSNALGDLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 165 ELIDFFRFNAKYAVELEGQqpiSVPPSTNSMVYRGLE--GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTA 238
Cdd:cd07144 110 EIIAVIRYYAGWADKIQGK---TIPTSPNKLAYTLHEpyGVCGQIIPWNYPL---AMAAwklAPALAaGNTVVIKPAENT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 239 MLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfpRLAGECGGK 318
Cdd:cd07144 184 PLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLK------AVTLECGGK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 319 NFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEE-HSRIKVGDPAEDfGTFFSAVIDAKSF 397
Cdd:cd07144 258 SPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHvKQNYKVGSPFDD-DTVVGPQVSKTQY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 398 ARIKKWLEHARSSPSLTILAGGK--CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVDSTTs 475
Cdd:cd07144 337 DRVLSYIEKGKKEGAKLVYGGEKapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT--YEEAIKKANDTT- 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1367104953 476 YGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSIvgQQPFGGARASG 527
Cdd:cd07144 414 YGLAAAVFTKD---IRRAHRVARElEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
82-507 |
1.30e-48 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 175.13 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA-- 158
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLA--ANTDEIAEELTWQmGRPIAQAgg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 EIDAAAELIDFFRFNAKYAVelegqQPISVPPSTN---SMVYRGLeGFVAAISPFN---FTAIGgnlAGAPALM-GNVVL 231
Cdd:cd07102 78 EIRGMLERARYMISIAEEAL-----ADIRVPEKDGferYIRREPL-GVVLIIAPWNypyLTAVN---AVIPALLaGNAVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 232 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRL 311
Cdd:cd07102 149 LKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGR------FIKV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 312 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 391
Cdd:cd07102 222 GLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDP-STTLGPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 392 IDAKSFARIKKWLEHARSSPSlTILAGGK---CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQ 468
Cdd:cd07102 301 VSARAADFVRAQIADAIAKGA-RALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSD--AEAIA 377
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1367104953 469 LV-DSTtsYGLTGAVFSQDKDVVQE-ATKVlrnAAGNFYIN 507
Cdd:cd07102 378 LMnDSE--YGLTASVWTKDIARAEAlGEQL---ETGTVFMN 413
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
105-527 |
1.45e-48 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 176.08 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 105 AIEAALAA-----RKEWDLKPIADRAQiFLKA-ADMLSgpRRAEILAKT-MVGQGKTVIQAE--IDAAAELIDFFrfnAK 175
Cdd:PLN02467 50 AVEAARKAfkrnkGKDWARTTGAVRAK-YLRAiAAKIT--ERKSELAKLeTLDCGKPLDEAAwdMDDVAGCFEYY---AD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 176 YAVELEGQQ--PISVPPST-NSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILRE 251
Cdd:PLN02467 124 LAEALDAKQkaPVSLPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 252 AGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPrLAGECGGKNFHFVHRSADVES 331
Cdd:PLN02467 204 VGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVFDDVDLDK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 332 VVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSp 411
Cdd:PLN02467 278 AVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE-GCRLGPVVSEGQYEKVLKFISTAKSE- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 412 SLTILAGGKCDD--SVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDV 489
Cdd:PLN02467 356 GATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE--DEAIELANDSH-YGLAGAVISNDLER 432
|
410 420 430
....*....|....*....|....*....|....*...
gi 1367104953 490 VQEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 527
Cdd:PLN02467 433 CERVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
103-538 |
1.45e-45 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 167.56 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQA--EIDAAAELIDFFrfnAKYAVE 179
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLII--ANKEDLAQLMTLeQGKPLKEAigEVAYGASFLEYF---AEEAKR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 180 LEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTaiggnLA-----GAPALM-GNVVLWKPSDTAMLASYAVYRILREAG 253
Cdd:PLN02278 140 VYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFP-----LAmitrkVGPALAaGCTVVVKPSELTPLTALAAAELALQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 254 LPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVV 333
Cdd:PLN02278 215 IPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA------TVKRVSLELGGNAPFIVFDDADLDVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSl 413
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE-GVTQGPLINEAAVQKVESHVQDAVSKGA- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 414 TILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDkdvVQEA 493
Cdd:PLN02278 367 KVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE--EEAIAIANDTE-AGLAAYIFTRD---LQRA 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1367104953 494 TKVlrNAAGNFYINDKSTGSIVGQQ-PFGGARASGTNdKPGGPHYI 538
Cdd:PLN02278 441 WRV--SEALEYGIVGVNEGLISTEVaPFGGVKQSGLG-REGSKYGI 483
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
102-527 |
1.51e-45 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 166.10 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAAELIDFFrfnAKYAV 178
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLR--ERKDELARLITLEmGKPIAEAraEVEKCAWICRYY---AENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 179 ELEGQQPISVPPSTNSMVYRGLeGFVAAISPFNFT-------AiggnlagAPALM-GNVVLWKPSDTAMLASYAVYRILR 250
Cdd:cd07100 76 AFLADEPIETDAGKAYVRYEPL-GVVLGIMPWNFPfwqvfrfA-------APNLMaGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 251 EAGLPPNIIQFVPADGPLFgDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVHRSADVE 330
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKS------VLELGGSDPFIVLDDADLD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFS--AVIDAKSfaRIKKWLEHAR 408
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDE-DTDLGplARKDLRD--ELHEQVEEAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 409 SSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKD 488
Cdd:cd07100 298 AA-GATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDE--EEAIALAND-SPFGLGGSVFTTDLE 373
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1367104953 489 vvqEATKVLRN-AAGNFYIND--KSTGSIvgqqPFGGARASG 527
Cdd:cd07100 374 ---RAERVARRlEAGMVFINGmvKSDPRL----PFGGVKRSG 408
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
104-527 |
9.57e-45 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 164.67 E-value: 9.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 104 KAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNAKYAVEL 180
Cdd:cd07139 40 AAVAAARRAfdNGPWPRLSPAERAAVLRRLADALE--ARADELARLWTAEnGMPISWSRRAQGPGPAALLRYYAALARDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 181 EGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNII 259
Cdd:cd07139 118 PFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 260 QFVPADgplfgdtVTSSEHLCG------INFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSADVESVV 333
Cdd:cd07139 198 NVVPAD-------REVGEYLVRhpgvdkVSFTGSTAAGRRIAAVCGERLARVTL------ELGGKSAAIVLDDADLDAAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSL 413
Cdd:cd07139 265 PGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP-ATQIGPLASARQRERVEGYIAKGRAEGAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 414 TILAGGKCDD-SVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQE 492
Cdd:cd07139 344 LVTGGGRPAGlDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE--DDAVRIAND-SDYGLSGSVWTAD---VER 417
|
410 420 430
....*....|....*....|....*....|....*.
gi 1367104953 493 ATKVLRNA-AGNFYINDKSTGSivgQQPFGGARASG 527
Cdd:cd07139 418 GLAVARRIrTGTVGVNGFRLDF---GAPFGGFKQSG 450
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
97-527 |
1.05e-44 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 165.05 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTvIQ----AEIDAAAELIDFFr 171
Cdd:PRK13252 41 ATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR--ERNDELAALETlDTGKP-IQetsvVDIVTGADVLEYY- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 172 fnAKYAVELEGQQpisVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRI 248
Cdd:PRK13252 117 --AGLAPALEGEQ---IPLRGGSFVYTRREplGVCAGIGAWNYPIQIACWKSAPALaAGNAMIFKPSEVTPLTALKLAEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 249 LREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSAD 328
Cdd:PRK13252 192 YTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKE------VTMELGGKSPLIVFDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHAR 408
Cdd:PRK13252 265 LDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP-MDPATNFGPLVSFAHRDKVLGYIEKGK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 409 SSPSlTILAGGKC----DDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFS 484
Cdd:PRK13252 344 AEGA-RLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE--DEVIARANDTE-YGLAAGVFT 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1367104953 485 QDkdvVQEATKVL-RNAAGNFYINdkSTGSIVGQQPFGGARASG 527
Cdd:PRK13252 420 AD---LSRAHRVIhQLEAGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
140-527 |
2.20e-44 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 162.21 E-value: 2.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 140 RAEILAKTMVG-QGKTVIQAEIDAAAElIDFFRFNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFT--AIG 216
Cdd:PRK10090 11 RASEISALIVEeGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPffLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 217 GNLAgaPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLW 295
Cdd:PRK10090 90 RKMA--PALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 296 KQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRI 375
Cdd:PRK10090 168 AAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 376 KVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSV 455
Cdd:PRK10090 242 QFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367104953 456 YVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgqQPF-GGARASG 527
Cdd:PRK10090 321 VAF--DTLEEAIAMAND-SDYGLTSSIYTQNLNVAMKAIKGLK--FGETYINRENFEAM---QGFhAGWRKSG 385
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
102-533 |
4.12e-44 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 162.53 E-value: 4.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 102 LNKAIEAALAARKEwdLKPiADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAaelIDFFRFNAKYAV 178
Cdd:cd07146 23 LREALALAASYRST--LTR-YQRSAILNKAAALLE--ARREEFARLITLEsGLCLKDTryEVGRA---ADVLRFAAAEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 179 ELEGQQpISVPPSTNSMVYRGLE-----GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTAMLASYAVYRIL 249
Cdd:cd07146 95 RDDGES-FSCDLTANGKARKIFTlreplGVVLAITPFNHPL---NQVAhkiAPAIAaNNRIVLKPSEKTPLSAIYLADLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 250 REAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFPRLAGECGGKNFHFVHRSADV 329
Cdd:cd07146 171 YEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 330 ESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARS 409
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDP-ATDMGTVIDEEAAIQIENRVEEAIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 410 SPSLTILAGGKcddsVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDV 489
Cdd:cd07146 322 QGARVLLGNQR----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDL--DEAIAISNS-TAYGLSSGVCTNDLDT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1367104953 490 VQEATKVLRNAAGNfyINDkSTGSIVGQQPFGGARASGTNDKPG 533
Cdd:cd07146 395 IKRLVERLDVGTVN--VNE-VPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
82-528 |
6.12e-44 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 162.90 E-value: 6.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARK---EWDLKPIADRAQIFLKAADMLSgpRRAEILA--KTMVGqGKTVI 156
Cdd:cd07141 27 INPAT-GEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIE--RDRAYLAslETLDN-GKPFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 157 QAEIDAAAELIDFFRFNAKYAVELEGQqpiSVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWK 233
Cdd:cd07141 103 KSYLVDLPGAIKVLRYYAGWADKIHGK---TIPMDGDFFTYTRHEpvGVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 234 PSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTfKHLWKQVA--QNLDrfhtfpRL 311
Cdd:cd07141 180 PAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAgkSNLK------RV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 312 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 391
Cdd:cd07141 253 TLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP-KTEQGPQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 392 IDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYvypddKYKETLQLVD 471
Cdd:cd07141 332 IDEEQFKKILELIESGKKEGA-KLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIF-----KFKTIDEVIE 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367104953 472 --STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgQQPFGGARASGT 528
Cdd:cd07141 406 raNNTTYGLAAAVFTKDIDKAITFSNALR--AGTVWVNCYNVVSP--QAPFGGYKMSGN 460
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
84-527 |
1.51e-43 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 161.47 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 84 PFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK--TMvGQGKTVIQ---A 158
Cdd:cd07117 23 PAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIID--ENKELLAMveTL-DNGKPIREtraV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 EIDAAAeliDFFRFNAKyAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:cd07117 99 DIPLAA---DHFRYFAG-VIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 238 AMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtFPRLAgECGG 317
Cdd:cd07117 175 TSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 318 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSF 397
Cdd:cd07117 248 KSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP-DTQMGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 398 ARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDSt 473
Cdd:cd07117 327 DKILSYVDIAKEEGA-KILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE--DEVIDMAND- 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1367104953 474 TSYGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINdkSTGSIVGQQPFGGARASG 527
Cdd:cd07117 403 SEYGLGGGVFTKD---INRALRVARAVeTGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
88-533 |
2.59e-43 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 161.12 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKE--WDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAEIDAAAE 165
Cdd:cd07142 29 GEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKPYEQARYAEVPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 166 LIDFFRFNAKYAVELEGqqpISVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:cd07142 108 AARLFRYYAGWADKIHG---MTLPADGPHHVYTLHEpiGVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 243 YAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDrfhtfpRLAGECGGKNFH 321
Cdd:cd07142 185 LLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLK------PVTLELGGKSPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 322 FVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaedfgtFFSAV-----IDAKS 396
Cdd:cd07142 259 IVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP------FRKGVeqgpqVDKEQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 397 FARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVDStTSY 476
Cdd:cd07142 333 FEKILSYIEHGKEEGA-TLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT--VDEVIKRANN-SKY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367104953 477 GLTGAVFSQDKDVVQEATKVLRnaAGNFYIN--DKSTGSIvgqqPFGGARASGTNDKPG 533
Cdd:cd07142 409 GLAAGVFSKNIDTANTLSRALK--AGTVWVNcyDVFDASI----PFGGYKMSGIGREKG 461
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
82-486 |
3.43e-43 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 160.45 E-value: 3.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPiadraqiflkaadmlsGPRRAEIL---------AKTMVGQ- 151
Cdd:cd07130 17 ISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVP----------------APKRGEIVrqigdalrkKKEALGKl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 152 -----GKTVIQA--EIDaaaELIDFfrfnAKYAVELEGQQPISVPPSTNSMvYRGLE-----GFVAAISPFNF-TAIGG- 217
Cdd:cd07130 80 vslemGKILPEGlgEVQ---EMIDI----CDFAVGLSRQLYGLTIPSERPG-HRMMEqwnplGVVGVITAFNFpVAVWGw 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 218 NLAGApALMGNVVLWKPSDTAMLASYAVYRI----LREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVptfkH 293
Cdd:cd07130 152 NAAIA-LVCGNVVVWKPSPTTPLTAIAVTKIvarvLEKNGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGST----A 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 294 LWKQVAQNLDRfhTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHS 373
Cdd:cd07130 226 VGRQVGQAVAA--RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 374 RIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKdPQEPIMKEEIFGPVL 453
Cdd:cd07130 304 QVRIGDPLDD-GTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPIL 380
|
410 420 430
....*....|....*....|....*....|...
gi 1367104953 454 svYVYPDDKYKETLQLVDStTSYGLTGAVFSQD 486
Cdd:cd07130 381 --YVLKFDTLEEAIAWNNE-VPQGLSSSIFTTD 410
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
82-527 |
2.07e-42 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 158.66 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK--TMvGQGKTV---I 156
Cdd:cd07559 21 YNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIE--ENLELLAVaeTL-DNGKPIretL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 157 QAEIDAAaelIDFFRFNAKYAVELEGQqpIS-VPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP 234
Cdd:cd07559 97 AADIPLA---IDHFRYFAGVIRAQEGS--LSeIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 235 SDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtFPrLAGE 314
Cdd:cd07559 172 ASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL-----IP-VTLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 315 CGGK--NFHFvhrsADVES--------VVSGTLRSAFEYGgQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDf 384
Cdd:cd07559 245 LGGKspNIFF----DDAMDadddfddkAEEGQLGFAFNQG-EVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 385 GTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD 460
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGA-EVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367104953 461 DkyKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINdkSTGSIVGQQPFGGARASG 527
Cdd:cd07559 398 E--EEAIAIAND-TEYGLGGGVWTRD---INRALRVARGiQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
87-526 |
7.50e-42 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 156.91 E-value: 7.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 87 HGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQA--EIDAA 163
Cdd:cd07085 25 TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE--ENLDELARLITlEHGKTLADArgDVLRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 164 AELIDFfrfNAKYAVELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSD 236
Cdd:cd07085 103 LEVVEF---ACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAM------IPLWMfpmaiacGNTFVLKPSE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 237 TAMLASYAVYRILREAGLPPNIIQFVPADGplfgDTVtssEHLC------GINFTGSVPTFKHLWKQVAQNLDRFHTFpr 310
Cdd:cd07085 174 RVPGAAMRLAELLQEAGLPDGVLNVVHGGK----EAV---NALLdhpdikAVSFVGSTPVGEYIYERAAANGKRVQAL-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 311 lageCGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSA 390
Cdd:cd07085 245 ----GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG-AGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 391 VIDAKSFARIKKWLEHArsspsltILAGGKC-----DDSV-----GYFVEPCIVESKDPQEPIMKEEIFGPVLSVyVYPD 460
Cdd:cd07085 320 VISPAAKERIEGLIESG-------VEEGAKLvldgrGVKVpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSI-VRVD 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367104953 461 DkYKETLQLVDStTSYGLTGAVFSQDKDVvqeATKVLRNA-AGNFYINdkstgsI-----VGQQPFGGARAS 526
Cdd:cd07085 392 T-LDEAIAIINA-NPYGNGAAIFTRSGAA---ARKFQREVdAGMVGIN------VpipvpLAFFSFGGWKGS 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
88-536 |
3.23e-41 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 155.25 E-value: 3.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTVIQ---AEIDAAA 164
Cdd:cd07111 47 GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN-GKPIREsrdCDIPLVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 165 ELidfFRFNAKYA----VELEGQQPIsvppstnsmvyrgleGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAM 239
Cdd:cd07111 126 RH---FYHHAGWAqlldTELAGWKPV---------------GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 240 LASYAVYRILREAGLPPNIIQFVPADGPlFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKN 319
Cdd:cd07111 188 LTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAG------TGKKLSLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 320 FHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AEDFGtffsAVIDAKS 396
Cdd:cd07111 261 PFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPldkAIDMG----AIVDPAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 397 FARIKKWLEHARSSPSLTILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSvyVYPDDKYKETLQLVDStTSY 476
Cdd:cd07111 337 LKRIRELVEEGRAEGADVFQPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLV--VLTFRTAKEAVALANN-TPY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 477 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASGTNdKPGGPH 536
Cdd:cd07111 413 GLAASVWSENLSLALEVALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGFG-REGGKE 467
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
104-535 |
1.52e-40 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 152.84 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-TMVGQGKTVIQA---EIDAAAELIDFFRFNAKYAVe 179
Cdd:cd07098 22 EAIAAARAAQREWAKTSFAERRKVLRSLLKYIL--ENQEEICRvACRDTGKTMVDAslgEILVTCEKIRWTLKHGEKAL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 180 legqQPISVPPSTNsMVYRGLE------GFVAAISPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAMLASYAVYRIL 249
Cdd:cd07098 99 ----RPESRPGGLL-MFYKRARveyeplGVVGAIVSWNYpfhNLLGPIIA---ALFaGNAIVVKVSEQVAWSSGFFLSII 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 250 REA----GLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPRLAgECGGKNFHFVHR 325
Cdd:cd07098 171 REClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKDPAIVLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 326 SADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---DFGtffsAVIDAKSFARIKK 402
Cdd:cd07098 244 DADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDgdvDVG----AMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 403 WLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGL 478
Cdd:cd07098 320 LVADAVEKGA-RLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD--EEAVEIANS-TEYGL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1367104953 479 TGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTnDKPGGP 535
Cdd:cd07098 396 GASVFGKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGE 449
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
97-532 |
5.11e-38 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 146.26 E-value: 5.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAkTMVGQ--GKTVIQAEIDAAAELidffrfnA 174
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLE--ENKEELA-EVIARetGKPLWEAATEVTAMI-------N 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 175 KYAV------ELEGQQPISVPPSTNSMVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYR 247
Cdd:PRK09457 104 KIAIsiqayhERTGEKRSEMADGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 248 ILREAGLPPNIIQFVPAdGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprLAGECGGKNFHFVHRSA 327
Cdd:PRK09457 183 LWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDEVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 328 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQ-IKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEH 406
Cdd:PRK09457 257 DIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 407 ARSSPSLTILAGGKCDDSVGyFVEPCIVESKDPQEPImKEEIFGPVLSVYVYPDdkYKETLQLVDStTSYGLTGAVFSQD 486
Cdd:PRK09457 337 LLALGGKSLLEMTQLQAGTG-LLTPGIIDVTGVAELP-DEEYFGPLLQVVRYDD--FDEAIRLANN-TRFGLSAGLLSDD 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1367104953 487 KDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGtNDKP 532
Cdd:PRK09457 412 REDYDQFLLEIR--AGIVNWNKPLTGA-SSAAPFGGVGASG-NHRP 453
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
82-529 |
2.79e-37 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 143.71 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNHGHkVAKFCYADKSLLNKAIEAALAA---RKEWdlKPIADRAQIFLKAADMLSGprRAEILAKTMVGQG-KTVIQ 157
Cdd:cd07148 4 VNPFDLKP-IGEVPTVDWAAIDKALDTAHALfldRNNW--LPAHERIAILERLADLMEE--RADELALLIAREGgKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 158 A--EIDAAaelIDFFRFNAKYAVELEGQQ-PISV-PPSTNSMVYRGLE--GFVAAISPFNFTAiggNLA---GAPAL-MG 227
Cdd:cd07148 79 AkvEVTRA---IDGVELAADELGQLGGREiPMGLtPASAGRIAFTTREpiGVVVAISAFNHPL---NLIvhqVAPAIaAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 228 NVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQNldrfht 307
Cdd:cd07148 153 CPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLRSKLAPG------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 308 fPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTF 387
Cdd:cd07148 226 -TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPT-DPDTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 388 FSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYfvEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETL 467
Cdd:cd07148 304 VGPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSY--DDLDEAI 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367104953 468 QLVDStTSYGLTGAVFSQDKDVVQEATKVLrnAAGNFYINDKsTGSIVGQQPFGGARASGTN 529
Cdd:cd07148 379 AQANS-LPVAFQAAVFTKDLDVALKAVRRL--DATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
88-533 |
2.05e-36 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 142.64 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKE--WDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAeidAAAE 165
Cdd:PLN02466 83 GEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQS---AKAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 166 L---IDFFRFNAKYAVELEGqqpISVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAM 239
Cdd:PLN02466 159 LpmfARLFRYYAGWADKIHG---LTVPADGPHHVQTLHEpiGVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 240 LASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFprlagECGGKN 319
Cdd:PLN02466 236 LSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL-----ELGGKS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 320 FHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQI----KGRLLeehsRIKVGDPaedfgtFFSAV---- 391
Cdd:PLN02466 311 PFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFvekaKARAL----KRVVGDP------FKKGVeqgp 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 392 -IDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYvypddKYKETLQLV 470
Cdd:PLN02466 381 qIDSEQFEKILRYIKSGVESGA-TLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSIL-----KFKDLDEVI 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367104953 471 D--STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN--DKSTGSIvgqqPFGGARASGTNDKPG 533
Cdd:PLN02466 455 RraNNTRYGLAAGVFTQNLDTANTLSRALR--VGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
88-527 |
3.17e-36 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 141.50 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-------TMVGQGKTViqa 158
Cdd:PLN02766 46 GEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIE--EHIEELAAldtidagKLFALGKAV--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 EIDAAAELidfFRFNAKYAVELEGQQpISVPPSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:PLN02766 121 DIPAAAGL---LRYYAGAADKIHGET-LKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 238 AMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRfhtfprLAGECG 316
Cdd:PLN02766 197 TPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQ------VSLELG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 317 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKS 396
Cdd:PLN02766 271 GKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF-DPRARQGPQVDKQQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 397 FARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYvypddKYK---ETLQLVDSt 473
Cdd:PLN02766 350 FEKILSYIEHGKREGA-TLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLM-----KFKtveEAIKKANN- 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367104953 474 TSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN-----DKSTgsivgqqPFGGARASG 527
Cdd:PLN02766 423 TKYGLAAGIVTKDLDVANTVSRSIR--AGTIWVNcyfafDPDC-------PFGGYKMSG 472
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
104-527 |
5.42e-36 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 140.43 E-value: 5.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM-VGQGKTVIQA--EIDAAAELIDFFRFNAK--YAV 178
Cdd:PRK11241 52 AAIDAANRALPAWRALTAKERANILRRWFNLMM--EHQDDLARLMtLEQGKPLAEAkgEISYAASFIEWFAEEGKriYGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 179 ELEGQQPisvppSTNSMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPN 257
Cdd:PRK11241 130 TIPGHQA-----DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 258 IIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESVVSGTL 337
Cdd:PRK11241 205 VFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK------VSLELGGNAPFIVFDDADLDKAVEGAL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 338 RSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSlTILA 417
Cdd:PRK11241 279 ASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK-GVTIGPLIDEKAVAKVEEHIADALEKGA-RVVC 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 418 GGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvvqeATKVL 497
Cdd:PRK11241 357 GGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE--ADVIAQAND-TEFGLAAYFYARD------LSRVF 427
|
410 420 430
....*....|....*....|....*....|..
gi 1367104953 498 RNA-AGNFYINDKSTGSIVGQ-QPFGGARASG 527
Cdd:PRK11241 428 RVGeALEYGIVGINTGIISNEvAPFGGIKASG 459
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
88-527 |
1.15e-34 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 136.86 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILA---------------KTMVG 150
Cdd:cd07140 31 GSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLME--EHQEELAtiesldsgavytlalKTHVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 151 QGktviqaeidaaaelIDFFRFNAKYAVELEGQQ-PISVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM- 226
Cdd:cd07140 109 MS--------------IQTFRYFAGWCDKIQGKTiPINQARPNRNLTLTKREpiGVCGIVIPWNYPLMMLAWKMAACLAa 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 227 GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVA-QNLDRf 305
Cdd:cd07140 175 GNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKK- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 306 htfprLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AE 382
Cdd:cd07140 254 -----VSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPldrST 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 383 DFGTffsavidAKSFARIKKWLEHARSS--PSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD 460
Cdd:cd07140 329 DHGP-------QNHKAHLDKLVEYCERGvkEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1367104953 461 DKYKETLQLVDsTTSYGLTGAVFSQDkdvvqeATKVLRNA----AGNFYINDKSTGSIVGqqPFGGARASG 527
Cdd:cd07140 402 GDVDGVLQRAN-DTEYGLASGVFTKD------INKALYVSdkleAGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
102-547 |
2.07e-32 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 129.67 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAEiDAAAELIDFFRFNAKYAVELE 181
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 182 GQQPISVPPSTNSMVYRGLE---GFVAAISPFNF--TAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAG-LP 255
Cdd:cd07084 79 PHEPGNHLGQGLKQQSHGYRwpyGPVLVIGAFNFplWIPLLQLAGALA-MGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 256 PNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVptfkhlwkQVAQNLDRFHTFPRLAGECGGKNFHFVHRSAD-VESVVS 334
Cdd:cd07084 158 PEDVTLINGDGKT-MQALLLHPNPKMVLFTGSS--------RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 335 GTLRSAFEYGGQKCSACSRLYVPH--SLWPQIKgRLLEEHSRIKVGDpaedfgTFFSAVIDAKSFARIkkwlEHARSSPS 412
Cdd:cd07084 229 QCVQDMTACSGQKCTAQSMLFVPEnwSKTPLVE-KLKALLARRKLED------LLLGPVQTFTTLAMI----AHMENLLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 413 LTILAGGK--CDDSVGYFVEPCI-------VESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYgLTGAVF 483
Cdd:cd07084 298 SVLLFSGKelKNHSIPSIYGACVasalfvpIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGS-LTAAIY 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367104953 484 SQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 547
Cdd:cd07084 377 SNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
102-547 |
4.28e-32 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 129.63 E-value: 4.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 102 LNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMvGQGKTV---IQAEIDAAAELIdffRFNAKY 176
Cdd:PRK09847 59 IDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL-DTGKPIrhsLRDDIPGAARAI---RWYAEA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 177 AVELEGQqpisVPPSTN---SMVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREA 252
Cdd:PRK09847 135 IDKVYGE----VATTSShelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 253 GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhTFPRLAGECGGKNFHFVHRSA-DVES 331
Cdd:PRK09847 211 GLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpDLQQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 332 VVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSP 411
Cdd:PRK09847 286 AASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPATTMGTLIDCAHADSVHSFIREGESKG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 412 SLtiLAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVVQ 491
Cdd:PRK09847 365 QL--LLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE--EQALQLAND-SQYGLGAAVWTRDLSRAH 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367104953 492 EATKVLRnaAGNFYINDKSTGSIVgqQPFGGARASGtNDKPGGPHYILRWTSPQVI 547
Cdd:PRK09847 439 RMSRRLK--AGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
88-527 |
8.61e-31 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 125.24 E-value: 8.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAeiLAKTMVGQ-GKTVIQAEIDAAaEL 166
Cdd:PRK09406 11 GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQ--VAALMTLEmGKTLASAKAEAL-KC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 167 IDFFRFNAKYAVELEGQQPISVPPSTNS---MVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWK-PSDTAMLA 241
Cdd:PRK09406 88 AKGFRYYAEHAEALLADEPADAAAVGASrayVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKhASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 242 SYaVYRILREAGLPPNIIQ--FVPADGPlfgDTVTSSEHLCGINFTGSVPTfkhlWKQVAQnldrfhtfprLAG------ 313
Cdd:PRK09406 167 LY-LADLFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPA----GRAVAA----------IAGdeikkt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 314 --ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 391
Cdd:PRK09406 229 vlELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDP-DTDVGPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 392 IDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdkYKETLQLVD 471
Cdd:PRK09406 308 ATEQGRDEVEKQVDDAVAAGA-TILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD--IDEAIEIAN 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1367104953 472 STTsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSivGQQPFGGARASG 527
Cdd:PRK09406 385 ATT-FGLGSNAWTRD---EAEQERFIDDlEAGQVFINGMTVSY--PELPFGGVKRSG 435
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
104-533 |
1.01e-30 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 125.72 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQAEIDAAAELIDFfrfnAKYAVELEGQ 183
Cdd:PLN02315 60 EGLRACEEAAKIWMQVPAPKRGEIVRQIGDALR--AKLDYLGRLVSLEMGKILAEGIGEVQEIIDM----CDFAVGLSRQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 184 QPISVPPST--NSM---VYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRI----LREAG 253
Cdd:PLN02315 134 LNGSIIPSErpNHMmmeVWNPL-GIVGVITAFNFpCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLvaevLEKNN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 254 LPPNIIQFVpADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGGKNFHFVHRSADVESVV 333
Cdd:PLN02315 213 LPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR------FGKCLLELSGNNAIIVMDDADIQLAV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSl 413
Cdd:PLN02315 286 RSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK-GTLLGPLHTPESKKNFEKGIEIIKSQGG- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 414 TILAGGKCDDSVGYFVEPCIVESKdPQEPIMKEEIFGPVLsvYVYPDDKYKETLQLVDSTTSyGLTGAVFSQDKDVVQEA 493
Cdd:PLN02315 364 KILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVL--YVMKFKTLEEAIEINNSVPQ-GLSSSIFTRNPETIFKW 439
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1367104953 494 TKVLRNAAGNFYINDKSTGSIVGQQpFGGARASGTNDKPG 533
Cdd:PLN02315 440 IGPLGSDCGIVNVNIPTNGAEIGGA-FGGEKATGGGREAG 478
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
154-527 |
4.88e-27 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 113.78 E-value: 4.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 154 TVIQAEIDAAAELIDffrfnaKYAVELEGQQPISVPPSTNSMVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVV 230
Cdd:cd07087 61 AVVLGEIDHALKHLK------KWMKPRRVSVPLLLQPAKAYVIPEPL-GVVLIIGPWNYplqLALA-PLIGAIA-AGNTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 231 LWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPlfgdtVTS---SEHLCGINFTGSVPTFKHLWKQVAQNLdrfhT 307
Cdd:cd07087 132 VLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-----VATallAEPFDHIFFTGSPAVGKIVMEAAAKHL----T 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 308 FPRLagECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSlwpqIKGRLLEEHSR-IKV---GDPAE- 382
Cdd:cd07087 202 PVTL--ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES----IKDELIEELKKaIKEfygEDPKEs 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 383 -DFGtffsAVIDAKSFARIKKWLEHArsspslTILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDd 461
Cdd:cd07087 276 pDYG----RIINERHFDRLASLLDDG------KVVIGGQVDKE-ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDD- 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367104953 462 kYKETLQLVDStTSYGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSIVGQQPFGGARASG 527
Cdd:cd07087 344 -LDEAIEFINS-RPKPLALYLFSEDKAVQE---RVLAEtSSGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
74-527 |
8.58e-27 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 113.70 E-value: 8.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 74 WTSDV--QY--QVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTmV 149
Cdd:cd07116 9 WVAPVkgEYfdNITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET-W 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 150 GQGKTV---IQAEIDAAaelIDFFRFnakYAVELEGQQPISVPPSTNSMVYRGLE--GFVAAISPFNFTAIGGNLAGAPA 224
Cdd:cd07116 87 DNGKPVretLAADIPLA---IDHFRY---FAGCIRAQEGSISEIDENTVAYHFHEplGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 225 LM-GNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLd 303
Cdd:cd07116 161 LAaGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 304 rfhtFPrLAGECGGK--NFHF----VHRSADVESVVSGTLRSAFEYGgQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKV 377
Cdd:cd07116 239 ----IP-VTLELGGKspNIFFadvmDADDAFFDKALEGFVMFALNQG-EVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 378 GDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVEsKDPQEPIMKEEIFGPVL 453
Cdd:cd07116 313 GNPL-DTETMIGAQASLEQLEKILSYIDIGKEEGA-EVLTGGErnelGGLLGGGYYVPTTFK-GGNKMRIFQEEIFGPVL 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1367104953 454 SVYVYPDdkYKETLQLVDSTTsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINdkSTGSIVGQQPFGGARASG 527
Cdd:cd07116 390 AVTTFKD--EEEALEIANDTL-YGLGAGVWTRD---GNTAYRMGRGiQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
184-527 |
9.16e-25 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 106.93 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 184 QPISVPPS-----TNSMVYRGLEGFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAglp 255
Cdd:cd07134 79 KPKRVRTPlllfgTKSKIRYEPKGVCLIISPWNYpfnLAFG-PLVSAIA-AGNTAILKPSELTPHTSAVIAKIIREA--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 256 pniiqFVPADGPLF-GDTVTSSE-------HlcgINFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSA 327
Cdd:cd07134 154 -----FDEDEVAVFeGDAEVAQAllelpfdH---IFFTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 328 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHA 407
Cdd:cd07134 220 DLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 408 RSSPSlTILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPD-DkyketlQLVDSTTSYG--LTGAVFS 484
Cdd:cd07134 300 VAKGA-KVEFGGQFDAA-QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDlD------EVIEYINAKPkpLALYVFS 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1367104953 485 QDKDVVQeatKVLRN-AAGNFYINDkstgSIV----GQQPFGGARASG 527
Cdd:cd07134 372 KDKANVN---KVLARtSSGGVVVND----VVLhflnPNLPFGGVNNSG 412
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
82-527 |
6.10e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 104.94 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQiflKAADMLSGPR-RAEILAKTMVGQ-GKTVIQA- 158
Cdd:PRK13968 12 VNPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQ---KLRDIGKALRaRSEEMAQMITREmGKPINQAr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 159 -EIDAAAELIDFFrfnAKYAVELEGQQPISVPPSTNSMVYRGLeGFVAAISPFNFtAIGGNLAGA-PALM-GNVVLWKPS 235
Cdd:PRK13968 88 aEVAKSANLCDWY---AEHGPAMLKAEPTLVENQQAVIEYRPL-GTILAIMPWNF-PLWQVMRGAvPILLaGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 236 DTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGEC 315
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALKK------CVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 316 GGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGtffsaviDAK 395
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEEN-------ALG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 396 SFARIKKWLE-HARSSPSL----TILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYkeTLQLV 470
Cdd:PRK13968 309 PMARFDLRDElHHQVEATLaegaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEH--ALELA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1367104953 471 DStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSivGQQPFGGARASG 527
Cdd:PRK13968 387 ND-SEFGLSATIFTTDETQARQMAARLE--CGGVFINGYCASD--ARVAFGGVKKSG 438
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
202-528 |
7.37e-24 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 104.22 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 202 GFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSS-E 277
Cdd:cd07135 110 GVVLIIGPWNYpvlLALS-PLVGAIA-AGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKfD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 278 HlcgINFTGSVPTFKHLWKQVAQNLDrfhtfPrLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVP 357
Cdd:cd07135 187 K---IFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 358 HSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSspslTILAGGKCDDSVgYFVEPCIVESK 437
Cdd:cd07135 258 PSVYDEFVEELKKVLDEFYPGGANAS--PDYTRIVNPRHFNRLKSLLDTTKG----KVVIGGEMDEAT-RFIPPTIVSDV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 438 DPQEPIMKEEIFGPVLSVYVYPD-DKYKETLQLVDSTtsygLTGAVFSQDKDVVQeatKVL-RNAAGNFYINDKSTGSIV 515
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDlDEAIKVINSRDTP----LALYIFTDDKSEID---HILtRTRSGGVVINDTLIHVGV 403
|
330
....*....|...
gi 1367104953 516 GQQPFGGARASGT 528
Cdd:cd07135 404 DNAPFGGVGDSGY 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
75-488 |
7.01e-23 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 102.14 E-value: 7.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 75 TSDVQYQVSPfnhghkvakfCYADKslLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRR--AEILAKTMVGQG 152
Cdd:PLN00412 40 TRKTQYKVQA----------CTQEE--VNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKApiAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 153 KTVIqAEIDAAAELIDFfrfNAKYAVEL--EGQQPISVPPSTNS-----MVYRGLEGFVAAISPFNFTAiggNLAG---A 222
Cdd:PLN00412 108 KDAV-TEVVRSGDLISY---TAEEGVRIlgEGKFLVSDSFPGNErnkycLTSKIPLGVVLAIPPFNYPV---NLAVskiA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 223 PALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSvptfkhlwkqvaqn 301
Cdd:PLN00412 181 PALIaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 302 lDRFHTFPRLAG------ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRI 375
Cdd:PLN00412 247 -DTGIAISKKAGmvplqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 376 KVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLSV 455
Cdd:PLN00412 326 TVGPPEDD--CDITPVVSESSANFIEGLVMDAKEKGA-TFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPV 399
|
410 420 430
....*....|....*....|....*....|...
gi 1367104953 456 YVYPDDkyKETLQLVDStTSYGLTGAVFSQDKD 488
Cdd:PLN00412 400 IRINSV--EEGIHHCNA-SNFGLQGCVFTRDIN 429
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
155-527 |
1.75e-22 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 100.87 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 155 VIQAEIDAAAELIDffrfnaKYAVELEGQQPISVPPSTNSMVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVVL 231
Cdd:PTZ00381 71 LTVAEIEHLLKHLD------EYLKPEKVDTVGVFGPGKSYIIPEPL-GVVLVIGAWNYplnLTLI-PLAGAIA-AGNTVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 232 WKPSDTAMLASYAVYRILREAgLPPNIIQFVPADgplfgdtVTSSEHLCG-----INFTGSVPTFKHLWKQVAQNLdrfh 306
Cdd:PTZ00381 142 LKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGG-------VEVTTELLKepfdhIFFTGSPRVGKLVMQAAAENL---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 307 TFPRLagECGGKNFHFVHRSADV----ESVVSGTLRSAfeygGQKCSACSRLYVPHSlwpqIKGRLLEE--HSRIKV--G 378
Cdd:PTZ00381 210 TPCTL--ELGGKSPVIVDKSCNLkvaaRRIAWGKFLNA----GQTCVAPDYVLVHRS----IKDKFIEAlkEAIKEFfgE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 379 DP--AEDFgtffSAVIDAKSFARIKKWLEHARSspslTILAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLSVY 456
Cdd:PTZ00381 280 DPkkSEDY----SRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPIL 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367104953 457 VYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSIVGQQPFGGARASG 527
Cdd:PTZ00381 351 TYEN--IDEVLEFINS-RPKPLALYYFGEDKRHKE---LVLENtSSGAVVINDCVFHLLNPNLPFGGVGNSG 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
184-527 |
2.23e-21 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 96.80 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 184 QPISVPPS-----TNSMVYRGLEGFVAAISPFN--FTAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPP 256
Cdd:cd07136 79 KPKRVKTPllnfpSKSYIYYEPYGVVLIIAPWNypFQLALAPLIGAIA-AGNTAVLKPSELTPNTSKVIAKIIEET-FDE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 257 NIIQFVPadgplfGDTVTSSEHLCG----INFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSADVE-- 330
Cdd:cd07136 157 EYVAVVE------GGVEENQELLDQkfdyIFFTGSVRVGKIVMEAAAKHL----TPVTL--ELGGKSPCIVDEDANLKla 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 331 --SVVSGTLRSAfeygGQKCSACSRLYVPHSlwpqIKGRLLEE---HSRIKVGDPA---EDFGTffsaVIDAKSFARIKK 402
Cdd:cd07136 225 akRIVWGKFLNA----GQTCVAPDYVLVHES----VKEKFIKElkeEIKKFYGEDPlesPDYGR----IINEKHFDRLAG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 403 WLEHArsspslTILAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDStTSYGLTGAV 482
Cdd:cd07136 293 LLDNG------KIVFGGNTDRETLY-IEPTILDNVTWDDPVMQEEIFGPILPVLTY--DTLDEAIEIIKS-RPKPLALYL 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1367104953 483 FSQDKDVvqeATKVLRNAA-GNFYINDKSTGSIVGQQPFGGARASG 527
Cdd:cd07136 363 FSEDKKV---EKKVLENLSfGGGCINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
190-527 |
1.74e-19 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 91.01 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 190 PSTNSMVYRGLeGFVAAISPFNF---TAIGGnLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFV---P 263
Cdd:cd07133 92 PAKAEVEYQPL-GVVGIIVPWNYplyLALGP-LIAALA-AGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVtggA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 264 ADGPLFgdtvtSS---EHLCginFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSADVESVVSGTLRSA 340
Cdd:cd07133 168 DVAAAF-----SSlpfDHLL---FTGSTAVGRHVMRAAAENL----TPVTL--ELGGKSPAIIAPDADLAKAAERIAFGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 341 FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIkvgdpaedFGTF-----FSAVIDAKSFARIKKWLEHARSSPS-LT 414
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM--------YPTLadnpdYTSIINERHYARLQGLLEDARAKGArVI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 415 ILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDSTTS----YgltgaVFSQDKdvv 490
Cdd:cd07133 306 ELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTY--DSLDEAIDYINARPRplalY-----YFGEDK--- 375
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1367104953 491 QEATKVLRN-AAGNFYINDksTGSIVGQ--QPFGGARASG 527
Cdd:cd07133 376 AEQDRVLRRtHSGGVTIND--TLLHVAQddLPFGGVGASG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
103-484 |
3.33e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 88.26 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 103 NKAIEAALAARKE----WDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQAEIDAAAELiDFFRFNAKYA 177
Cdd:PLN02419 150 NEEFKAAVSAAKQafplWRNTPITTRQRVMLKFQELIR--KNMDKLAMNITTeQGKTLKDSHGDIFRGL-EVVEHACGMA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 178 VELEGQQPISVPPSTNSMVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSDTAMLASYAVYRILR 250
Cdd:PLN02419 227 TLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAM------IPLWMfpvavtcGNTFILKPSEKDPGASVILAELAM 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 251 EAGLPPNIIQFVPADGplfgDTVTS---SEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSA 327
Cdd:PLN02419 301 EAGLPDGVLNIVHGTN----DTVNAicdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS------NMGAKNHGLVLPDA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 328 DVESVVSGTLRSAFEYGGQKCSACSRLYV--PHSLWpqiKGRLLEEHSRIKV---GDPAEDFGtffsAVIDAKSFARIKK 402
Cdd:PLN02419 371 NIDATLNALLAAGFGAAGQRCMALSTVVFvgDAKSW---EDKLVERAKALKVtcgSEPDADLG----PVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 403 WLEHARSSPSLTILAGgkcDDSV------GYFVEPCIVESKDPQEPIMKEEIFGPVLsvYVYPDDKYKETLQLVDStTSY 476
Cdd:PLN02419 444 LIQSGVDDGAKLLLDG---RDIVvpgyekGNFIGPTILSGVTPDMECYKEEIFGPVL--VCMQANSFDEAISIINK-NKY 517
|
....*...
gi 1367104953 477 GLTGAVFS 484
Cdd:PLN02419 518 GNGAAIFT 525
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
314-527 |
1.43e-16 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 82.27 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 314 ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSA-----CSrlyvphslwPQIKGRLLEE-HSRIKV---GDPAE-- 382
Cdd:cd07132 206 ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyvlCT---------PEVQEKFVEAlKKTLKEfygEDPKEsp 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 383 DFGTffsaVIDAKSFARIKKWLEharsspSLTILAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDdk 462
Cdd:cd07132 277 DYGR----IINDRHFQRLKKLLS------GGKVAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNN-- 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367104953 463 YKETLQLVDSTTSyGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSIVGQQPFGGARASG 527
Cdd:cd07132 344 LDEAIEFINSREK-PLALYVFSNNKKVIN---KILSNtSSGGVCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
200-512 |
4.23e-12 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 68.45 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 200 LEGFVAAISPFNFTAIGGNLAGAPALMGNV-VLWKP-SDTAMLAsYAVYRILREAG-LPPNIIQFVPAD-GPLFgDTVTS 275
Cdd:cd07128 144 RRGVAVHINAFNFPVWGMLEKFAPALLAGVpVIVKPaTATAYLT-EAVVKDIVESGlLPEGALQLICGSvGDLL-DHLGE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 276 SEHlcgINFTGSVPTFKHLwkQVAQNLDRFHTfpRLAGECGGKNFHFVhrSADVES-------VVSGTLRSAFEYGGQKC 348
Cdd:cd07128 222 QDV---VAFTGSAATAAKL--RAHPNIVARSI--RFNAEADSLNAAIL--GPDATPgtpefdlFVKEVAREMTVKAGQKC 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 349 SACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPslTILAGGK-------C 421
Cdd:cd07128 293 TAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLE-GVRMGPLVSREQREDVRAAVATLLAEA--EVVFGGPdrfevvgA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 422 DDSVGYFVEPCIVESKDPQEP--IMKEEIFGPVLSVYVYpdDKYKETLQLVdsttSYG---LTGAVFSQDKDvvqEATKV 496
Cdd:cd07128 370 DAEKGAFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPY--DSLAEAIELA----ARGrgsLVASVVTNDPA---FAREL 440
|
330 340
....*....|....*....|....
gi 1367104953 497 LRNAA---GNFYINDK-----STG 512
Cdd:cd07128 441 VLGAApyhGRLLVLNRdsakeSTG 464
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
185-528 |
1.05e-11 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 67.05 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 185 PISVPPSTNSMVYRGLeGFVAAISPFNFtAIGGNL---AGAPAlMGNVVLWKPSDTAMLASYAVYRILrEAGLPPNIIQF 261
Cdd:cd07137 87 PLTTFPAKAEIVSEPL-GVVLVISAWNF-PFLLSLepvIGAIA-AGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 262 VPAdgplfgdTVTSSEHLC-----GINFTGSVPTFKHLWKQVAQNLDrfhtfPrLAGECGGKNFHFVHRSADVESVVSGT 336
Cdd:cd07137 163 IEG-------GVPETTALLeqkwdKIFFTGSPRVGRIIMAAAAKHLT-----P-VTLELGGKCPVIVDSTVDLKVAVRRI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 337 LrsAFEYG---GQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPSl 413
Cdd:cd07137 230 A--GGKWGcnnGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKES--KDLSRIVNSHHFQRLSRLLDDPSVADK- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 414 tILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVdSTTSYGLTGAVFSQDKDVvqEA 493
Cdd:cd07137 305 -IVHGGERDEK-NLYIEPTILLDPPLDSSIMTEEIFGPLLPIITV--KKIEESIEII-NSRPKPLAAYVFTKNKEL--KR 377
|
330 340 350
....*....|....*....|....*....|....*
gi 1367104953 494 TKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGT 528
Cdd:cd07137 378 RIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
82-543 |
1.83e-10 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 63.28 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIA--DRAQ----IFLKAADMLSGPRRAEILAK-TMVGQGKT 154
Cdd:cd07126 17 LDPLN-GDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKnpERYLlygdVSHRVAHELRKPEVEDFFARlIQRVAPKS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 155 VIQA--EIDAAAELIDFF-----RFNAK-YAV--ELEGQQpisvppstnSMVYRGLEGFVAAISPFNFT----AIggNLA 220
Cdd:cd07126 96 DAQAlgEVVVTRKFLENFagdqvRFLARsFNVpgDHQGQQ---------SSGYRWPYGPVAIITPFNFPleipAL--QLM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 221 GApALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCgINFTGSvptfkhlwKQVAQ 300
Cdd:cd07126 165 GA-LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRM-TLFTGS--------SKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 301 NLDRfHTFPRLAGECGGKNFHFVHRS-ADVESVVSGTLRSAFEYGGQKCSACSRLYVpHSLWPQ--IKGRLLEEHSRIKV 377
Cdd:cd07126 235 RLAL-ELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFA-HENWVQagILDKLKALAEQRKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 378 GD----PAEDFGTffsavidaksfARIKKWLEHARSSPSLTILAGGK-----CDDSVGYFVEPC-----IVESKDPQE-P 442
Cdd:cd07126 313 EDltigPVLTWTT-----------ERILDHVDKLLAIPGAKVLFGGKpltnhSIPSIYGAYEPTavfvpLEEIAIEENfE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 443 IMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYgLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQ--QPF 520
Cdd:cd07126 382 LVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAH-LTAAVVSNDIRFLQEVLANTVNGTTYAGIRARTTGAPQNHwfGPA 460
|
490 500
....*....|....*....|....
gi 1367104953 521 GGARASGTndkpGGPHYI-LRWTS 543
Cdd:cd07126 461 GDPRGAGI----GTPEAIrLVWSC 480
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
198-460 |
4.82e-10 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 62.03 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 198 RGLEGFVAAispFNFTAIGGNLAGAPALMGNV-VLWKP-SDTAMLASYAVyRILREAG-LPPNIIQFV---PAD-----G 266
Cdd:PRK11903 149 RGVALFINA---FNFPAWGLWEKAAPALLAGVpVIVKPaTATAWLTQRMV-KDVVAAGiLPAGALSVVcgsSAGlldhlQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 267 PlfGDTVTssehlcginFTGSVPTFKHLwkqvaqnldRFHtfPRLAGecggknfHFVHRSADVESVVSGTL-------RS 339
Cdd:PRK11903 225 P--FDVVS---------FTGSAETAAVL---------RSH--PAVVQ-------RSVRVNVEADSLNSALLgpdaapgSE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 340 AFEY------------GGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAED---FGTFFSAVIDAKSFARIKKWL 404
Cdd:PRK11903 276 AFDLfvkevvremtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDgvrMGPLVSRAQLAAVRAGLAALR 355
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367104953 405 EHArsspslTILAGGK------CDDSVGYFVEPCIVESKDPQEP--IMKEEIFGPVLSVYVYPD 460
Cdd:PRK11903 356 AQA------EVLFDGGgfalvdADPAVAACVGPTLLGASDPDAAtaVHDVEVFGPVATLLPYRD 413
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
190-527 |
8.43e-06 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 48.50 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 190 PSTNSMVYRGLeGFVAAISPFNFTAIGG--NLAGAPAlMGNVVLWKPSDTAMlASYAVYRILREAGLPPNIIQFVpaDGP 267
Cdd:PLN02174 103 PASAEIVSEPL-GVVLVISAWNYPFLLSidPVIGAIS-AGNAVVLKPSELAP-ASSALLAKLLEQYLDSSAVRVV--EGA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 268 LFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESVVSGTLrsAFEYG--- 344
Cdd:PLN02174 178 VTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTP------VVLELGGKSPVVVDSDTDLKVTVRRII--AGKWGcnn 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 345 GQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPSltILAGGKcDDS 424
Cdd:PLN02174 250 GQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMES--KDMSRIVNSTHFDRLSKLLDEKEVSDK--IVYGGE-KDR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 425 VGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDSTTSyGLTGAVFSQDKDVVQE-ATKVlrnAAGN 503
Cdd:PLN02174 325 ENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTL--NNLEESFDVIRSRPK-PLAAYLFTHNKKLKERfAATV---SAGG 398
|
330 340
....*....|....*....|....
gi 1367104953 504 FYINDKSTGSIVGQQPFGGARASG 527
Cdd:PLN02174 399 IVVNDIAVHLALHTLPFGGVGESG 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
175-527 |
2.78e-05 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 46.64 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 175 KYAVELEGQQPISVPPSTNSMVYRGLeGFVAAISPFNFtAIGGNL---AGAPAlMGNVVLWKPSDtamlasyavyrilre 251
Cdd:PLN02203 84 KWMAPKKAKLPLVAFPATAEVVPEPL-GVVLIFSSWNF-PIGLSLeplIGAIA-AGNAVVLKPSE--------------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 252 agLPPNIIQFVPADGPLFGDT---------VTSSEHLC-----GINFTGSVPTFKHLWKQVAQnldrfHTFPrLAGECGG 317
Cdd:PLN02203 146 --LAPATSAFLAANIPKYLDSkavkvieggPAVGEQLLqhkwdKIFFTGSPRVGRIIMTAAAK-----HLTP-VALELGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 318 KN---FHFVHRSADVESVVSGTLRSAFEY-GGQKCSACSRLYVPHSLWPqIKGRLLEEHSRIKVGDPAEDFGTFfSAVID 393
Cdd:PLN02203 218 KCpciVDSLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAP-ILIELLKSTIKKFFGENPRESKSM-ARILN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 394 AKSFARIKKWLEHARSSPSltILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYpdDKYKETLQLVDST 473
Cdd:PLN02203 296 KKHFQRLSNLLKDPRVAAS--IVHGGSIDEK-KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITV--KKIEDSIAFINSK 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1367104953 474 TSyGLTGAVFSQDKDVVQEAtkVLRNAAGNFYINDKSTGSIVGQQPFGGARASG 527
Cdd:PLN02203 371 PK-PLAIYAFTNNEKLKRRI--LSETSSGSVTFNDAIIQYACDSLPFGGVGESG 421
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
227-507 |
5.12e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 45.93 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 227 GNVVLWKPSDTAMLASYAVYRILR----EAGLPPNIIQFV--PADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQ 300
Cdd:cd07127 221 GNPVIVKPHPAAILPLAITVQVARevlaEAGFDPNLVTLAadTPEEPIAQTLATRPE-VRIIDFTGSNAFGDWLEANARQ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 301 NLdrfhtfprLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVP---------HSLWPQIKGRLLEE 371
Cdd:cd07127 300 AQ--------VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPrdgiqtddgRKSFDEVAADLAAA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367104953 372 HSRIkVGDPAEDFGtFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYfvEPCIVESKDPQEPIMKEEIFGP 451
Cdd:cd07127 372 IDGL-LADPARAAA-LLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGP 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367104953 452 VLsvYVYPDDKYKETLQLVDST--TSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYIN 507
Cdd:cd07127 448 IA--FVVATDSTDHSIELARESvrEHGAMTVGVYSTDPEVVERVQEAALDAGVALSIN 503
|
|
| |
