|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
6-397 |
0e+00 |
|
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: 746.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 6 SAFESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNC 85
Cdd:cd07132 51 PKFEAVLSEILLVKNEIKYAISNLPEWMKPEPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNC 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 86 VVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGK 165
Cdd:cd07132 131 VVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 166 NPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERL 245
Cdd:cd07132 211 SPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 246 QGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVV 325
Cdd:cd07132 291 KKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVI 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958654670 326 TQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLLSSPGMEKLNDLRYPPY 397
Cdd:cd07132 371 NKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPY 442
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
6-380 |
0e+00 |
|
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: 631.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 6 SAFESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNC 85
Cdd:cd07087 51 PPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 86 VVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGK 165
Cdd:cd07087 131 VVLKPSELAPATSALLAKLIPKYFDPEAVAVVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 166 NPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERL 245
Cdd:cd07087 211 SPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 246 QGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVV 325
Cdd:cd07087 291 ASLLDDGKVVIGGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958654670 326 TQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACL 380
Cdd:cd07087 371 ERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
6-405 |
0e+00 |
|
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: 583.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 6 SAFESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNC 85
Cdd:cd07136 51 SEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 86 VVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGK 165
Cdd:cd07136 131 AVLKPSELTPNTSKVIAKIIEETFDEEYVAVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 166 NPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERL 245
Cdd:cd07136 211 SPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 246 QGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVV 325
Cdd:cd07136 291 AGLLDNGKIVFGGNTDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVE 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 326 TQMLEctsSGSFGG---NDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLLSSPGMEklNDLRYPPYGTWDQ 402
Cdd:cd07136 371 KKVLE---NLSFGGgciNDTIMHLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYKGKKK 445
|
...
gi 1958654670 403 QLI 405
Cdd:cd07136 446 KLK 448
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
5-411 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 576.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 5 QSAFESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGN 84
Cdd:PTZ00381 59 RHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 85 CVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGG 164
Cdd:PTZ00381 139 TVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 165 KNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFER 244
Cdd:PTZ00381 219 KSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 245 LQGLLGC--GRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNG 322
Cdd:PTZ00381 299 LAELIKDhgGKVVYGGEVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 323 QVVTQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLLSSPGMEKLNDLRYPPYGTWDQ 402
Cdd:PTZ00381 379 RHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKS 458
|
....*....
gi 1958654670 403 QLISWAMGS 411
Cdd:PTZ00381 459 WVLSFLLKL 467
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
6-378 |
0e+00 |
|
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: 527.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 6 SAFESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLT-KFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGN 84
Cdd:cd07135 58 PPFETLLTEVSGVKNDILHMLKNLKKWAKDEKVKDGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 85 CVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGG 164
Cdd:cd07135 138 TVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 165 KNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFER 244
Cdd:cd07135 218 KSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 245 LQGLLGC--GRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNG 322
Cdd:cd07135 298 LKSLLDTtkGKVVIGGEMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDK 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958654670 323 QVVTQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07135 378 SEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
9-380 |
8.90e-170 |
|
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: 482.50 E-value: 8.90e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 9 ESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVL 88
Cdd:cd07134 54 EVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAIL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 89 KPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPC 168
Cdd:cd07134 134 KPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 169 YVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQT--SPNLGRIINQKHFERLQ 246
Cdd:cd07134 214 IVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARkaSPDLARIVNDRHFDRLK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 247 GLL-----GCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN 321
Cdd:cd07134 294 GLLddavaKGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958654670 322 GQVVTQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACL 380
Cdd:cd07134 374 KANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
5-380 |
4.13e-164 |
|
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: 468.04 E-value: 4.13e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 5 QSAFESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGN 84
Cdd:cd07137 51 KPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 85 CVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGG 164
Cdd:cd07137 131 AVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 165 KNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFE 243
Cdd:cd07137 211 KCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 244 RLQGLLGCGRVAI----GGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFS 319
Cdd:cd07137 291 RLSRLLDDPSVADkivhGGERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFT 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958654670 320 NNGQVVTQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACL 380
Cdd:cd07137 371 KNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
6-378 |
4.22e-162 |
|
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: 462.72 E-value: 4.22e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 6 SAFESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNC 85
Cdd:cd07133 52 SRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 86 VVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGK 165
Cdd:cd07133 132 VMIKPSEFTPRTSALLAELLAEYFDEDEVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 166 NPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDnPQTSPNLGRIINQKHFERL 245
Cdd:cd07133 212 SPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPT-LADNPDYTSIINERHYARL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 246 QGLL------GCGRVAIG--GQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYA 317
Cdd:cd07133 291 QGLLedarakGARVIELNpaGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYY 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958654670 318 FSNNGQVVTQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07133 371 FGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
9-401 |
1.22e-141 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 412.97 E-value: 1.22e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 9 ESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVL 88
Cdd:PLN02203 62 EAYRDEVGVLTKSANLALSNLKKWMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 89 KPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPC 168
Cdd:PLN02203 142 KPSELAPATSAFLAANIPKYLDSKAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPC 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 169 YVD---DNCDPQTVANRVAWFRYFN-AGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFER 244
Cdd:PLN02203 222 IVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 245 LQGLLGCGRVAI----GGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSN 320
Cdd:PLN02203 302 LSNLLKDPRVAAsivhGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTN 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 321 NGQVVTQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLLSSPGMEKLndLRYPPygtW 400
Cdd:PLN02203 382 NEKLKRRILSETSSGSVTFNDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEFE--FRYPP---W 456
|
.
gi 1958654670 401 D 401
Cdd:PLN02203 457 N 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
14-381 |
3.03e-122 |
|
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: 361.53 E-value: 3.03e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 14 EIILCQNEVDLALKNLQTWMKDESVSTNfltKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEM 93
Cdd:cd07078 58 EVARAADTFRYYAGLARRLHGEVIPSPD---PGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 94 SKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ-LLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYV 170
Cdd:cd07078 135 TPLTALLLAELLAEAgLPPGVLNVVTGDGDEVGAaLASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 171 DDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFERLQGLL 249
Cdd:cd07078 215 FDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPlDPDTDMGPLISAAQLDRVLAYI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 250 -----GCGRVAIGGQSDEGE--RYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNG 322
Cdd:cd07078 295 edakaEGAKLLCGGKRLEGGkgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDL 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958654670 323 QVVTQMLECTSSGSFGGNDGFLYLTlPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLL 381
Cdd:cd07078 375 ERALRVAERLEAGTVWINDYSVGAE-PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
8-397 |
1.42e-119 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 356.66 E-value: 1.42e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 8 FESDMSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVV 87
Cdd:PLN02174 65 LESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 88 LKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNP 167
Cdd:PLN02174 145 LKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 168 CYVDDNCDPQTVANRVAWFRY-FNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQ 246
Cdd:PLN02174 225 VVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 247 GLLG----CGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNG 322
Cdd:PLN02174 305 KLLDekevSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNK 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958654670 323 QVVTQMLECTSSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLLSSpgMEKLNDLRYPPY 397
Cdd:PLN02174 385 KLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRS--LFGDSAVRYPPY 457
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
13-381 |
6.73e-98 |
|
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: 296.83 E-value: 6.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 13 SEIILCQNEVDLALKNLQTWMKDESVSTNfltKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSE 92
Cdd:cd06534 53 GEVARAIDTFRYAAGLADKLGGPELPSPD---PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 93 MSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ-LLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCY 169
Cdd:cd06534 130 LTPLTALALAELLQEAgLPPGVVNVVPGGGDEVGAaLLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 170 VDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVpalqnaitrfygdnpqtspnlgriinqkhfERLQgll 249
Cdd:cd06534 210 VDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFV------------------------------EKLV--- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 250 gcgrvaiggqsdegeryiapTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQML 329
Cdd:cd06534 257 --------------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958654670 330 ECTSSGSFGGNDGFLYLTlPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLL 381
Cdd:cd06534 317 ERLRAGTVYINDSSIGVG-PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
49-378 |
1.75e-97 |
|
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: 299.73 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ- 126
Cdd:COG1012 135 AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAa 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:COG1012 215 LVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQSDEGER--YIAPTVLVDVQE 277
Cdd:COG1012 295 SIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRRPDGEGgyFVEPTVLADVTP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 278 TEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYlTLPALPLGGVG 357
Cdd:COG1012 375 DMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTG-AVPQAPFGGVK 453
|
330 340
....*....|....*....|.
gi 1958654670 358 NSGMGRYHGKFSFDTFSHQRA 378
Cdd:COG1012 454 QSGIGREGGREGLEEYTETKT 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
49-378 |
4.26e-86 |
|
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: 269.79 E-value: 4.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ- 126
Cdd:pfam00171 120 AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEa 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:pfam00171 200 LVEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGE-RYIAPTVLVDVQET 278
Cdd:pfam00171 280 SIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYFVEPTVLANVTPD 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 279 EPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYlTLPALPLGGVGN 358
Cdd:pfam00171 360 MRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTG-DADGLPFGGFKQ 438
|
330 340
....*....|....*....|
gi 1958654670 359 SGMGRYHGKFSFDTFSHQRA 378
Cdd:pfam00171 439 SGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
14-378 |
2.57e-85 |
|
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: 267.55 E-value: 2.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 14 EIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEM 93
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 94 SKNTEKVLAELLPQY-LDQSCFAVVLGGpEETGQ-LLKHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVD 171
Cdd:cd07099 158 TPLVGELLAEAWAAAgPPQGVLQVVTGD-GATGAaLIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 172 DNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPAL--------QNAITRFYGD-NPQTSPNLGRIInQKHF 242
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLvakaralrPGADDIGDADiGPMTTARQLDIV-RRHV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 243 ErlQGLLGCGRVAIGG-QSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN 321
Cdd:cd07099 316 D--DAVAKGAKALTGGaRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 322 ---GQVVTQMLEctsSGSFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07099 394 larAEAIARRLE---AGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
48-374 |
1.32e-67 |
|
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: 221.43 E-value: 1.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 48 SAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQL 127
Cdd:cd07092 111 TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 L--KHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07092 191 LvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL----GCGRVAIGGQSDEGERY-IAPTVLVDVQETE 279
Cdd:cd07092 271 SVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTVVAGVAQDD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 280 PVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYltLPALPLGGVGNS 359
Cdd:cd07092 351 EIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPL--AAEMPHGGFKQS 428
|
330
....*....|....*
gi 1958654670 360 GMGRYHGKFSFDTFS 374
Cdd:cd07092 429 GYGKDLSIYALEDYT 443
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
50-373 |
2.24e-66 |
|
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: 218.07 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ-L 127
Cdd:cd07103 112 LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEaL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LKH----KfdyIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC 203
Cdd:cd07103 192 CASprvrK---ISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 SQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGL----LGCG-RVAIGGQ-SDEGERYIAPTVLVDVQ 276
Cdd:cd07103 269 HESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALvedaVAKGaKVLTGGKrLGLGGYFYEPTVLTDVT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 277 ETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFlyLTLPALPLGGV 356
Cdd:cd07103 349 DDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL--ISDAEAPFGGV 426
|
330
....*....|....*..
gi 1958654670 357 GNSGMGRYHGKFSFDTF 373
Cdd:cd07103 427 KESGLGREGGKEGLEEY 443
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
12-367 |
4.21e-65 |
|
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: 215.24 E-value: 4.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 12 MSEIILCQNEVDLALKNLQTWMKDESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPS 91
Cdd:cd07098 77 LGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 92 EMSKNTEKVLAELLPQYLdQSCFA------VVLGGPEETGQLLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGG 164
Cdd:cd07098 157 EQVAWSSGFFLSIIRECL-AACGHdpdlvqLVTCLPETAEALTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 165 KNPCYVDDNCDPQTVANrvAWFR--YFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNP-QTSPNLGRIINQKH 241
Cdd:cd07098 236 KDPAIVLDDADLDQIAS--IIMRgtFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPlDGDVDVGAMISPAR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 242 FERLQGLLG----------CGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREK 311
Cdd:cd07098 314 FDRLEELVAdavekgarllAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 312 PLALYAFSNN---GQVVTQMLECtssGSFGGND-GFLYLTLpALPLGGVGNSGMGRYHGK 367
Cdd:cd07098 394 GLGASVFGKDikrARRIASQLET---GMVAINDfGVNYYVQ-QLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
49-374 |
2.43e-63 |
|
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: 210.55 E-value: 2.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ- 126
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGAa 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07109 191 LVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGER----YIAPTVLVDVQ 276
Cdd:cd07109 271 SIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRIAEGAPaggyFVAPTLLDDVP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 277 ETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFlyltlPA----LP 352
Cdd:cd07109 351 PDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYG-----AGggieLP 425
|
330 340
....*....|....*....|..
gi 1958654670 353 LGGVGNSGMGRYHGKFSFDTFS 374
Cdd:cd07109 426 FGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
51-377 |
1.96e-62 |
|
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: 207.38 E-value: 1.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 51 IRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVL-AEL-----LPQYLdqscFAVVLGGPEET 124
Cdd:cd07104 94 VRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIfeeagLPKGV----LNVVPGGGSEI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 125 GQ-LLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL 202
Cdd:cd07104 170 GDaLVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRIL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 203 CSQEMQERLVPALQNAITRF-YGD--NPQTSpnLGRIINQKHFERLQGLL------GcGRVAIGGQSDegERYIAPTVLV 273
Cdd:cd07104 250 VHESVYDEFVEKLVAKAKALpVGDprDPDTV--IGPLINERQVDRVHAIVedavaaG-ARLLTGGTYE--GLFYQPTVLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 274 DVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGflylTL---PA 350
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ----TVndePH 400
|
330 340
....*....|....*....|....*..
gi 1958654670 351 LPLGGVGNSGMGRYHGKFSFDTFSHQR 377
Cdd:cd07104 401 VPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
36-378 |
2.52e-62 |
|
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: 207.57 E-value: 2.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 36 ESVSTNFLTKFSSAFirKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCF 114
Cdd:cd07150 102 ETLPSDSPGTVSMSV--RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVF 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 115 AVVLGGPEETGQLL--KHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 192
Cdd:cd07150 180 NVVTGGGAEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 193 QTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSDeGER 265
Cdd:cd07150 260 QICMSASRIIVEEPVYDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVedavakG-AKLLTGGKYD-GNF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 266 YiAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLY 345
Cdd:cd07150 338 Y-QPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTIL 416
|
330 340 350
....*....|....*....|....*....|...
gi 1958654670 346 lTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07150 417 -DEAHVPFGGVKASGFGREGGEWSMEEFTELKW 448
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
49-381 |
2.96e-62 |
|
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: 207.58 E-value: 2.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQL 127
Cdd:cd07118 113 GLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 L--KHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07118 193 MteHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQnAITRF--YGD--NPQTspNLGRIINQKHFERLQGLLGCGR-----VAIGGQSDEGE--RYIAPTVLVD 274
Cdd:cd07118 273 SIADAFVAAVV-ARSRKvrVGDplDPET--KVGAIINEAQLAKITDYVDAGRaegatLLLGGERLASAagLFYQPTIFTD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 275 VQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGN---DGFlyltlPAL 351
Cdd:cd07118 350 VTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNtflDGS-----PEL 424
|
330 340 350
....*....|....*....|....*....|
gi 1958654670 352 PLGGVGNSGMGRYHGKFSFDTFSHQRACLL 381
Cdd:cd07118 425 PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
51-367 |
4.31e-62 |
|
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: 207.00 E-value: 4.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 51 IRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGpEETGQLL-K 129
Cdd:cd07106 110 LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGG-DELGPALtS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 130 H-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ 208
Cdd:cd07106 189 HpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 209 ERLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGERY-IAPTVLVDVQETEPV 281
Cdd:cd07106 269 DEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 282 MQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLECtssGSFGGNdGFLYLTlPALPLGGVGN 358
Cdd:cd07106 349 VDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDlerAEAVARRLEA---GTVWIN-THGALD-PDAPFGGHKQ 423
|
....*....
gi 1958654670 359 SGMGRYHGK 367
Cdd:cd07106 424 SGIGVEFGI 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
50-375 |
1.75e-60 |
|
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: 202.86 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-----LPQYLdqscFAVVLGGPEET 124
Cdd:cd07102 111 YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAfaeagLPEGV----FQVLHLSHETS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 125 GQLLK-HKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC 203
Cdd:cd07102 187 AALIAdPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 SQEMQERLVPALQnAITRFY--GDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQ----SDEGERYIAPTV 271
Cdd:cd07102 267 HESIYDAFVEAFV-AVVKGYklGDPLDPSTTLGPVVSARAADFVRAQIadaiakG-ARALIDGAlfpeDKAGGAYLAPTV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 272 LVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGN--DgflYLTlP 349
Cdd:cd07102 345 LTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcD---YLD-P 420
|
330 340
....*....|....*....|....*.
gi 1958654670 350 ALPLGGVGNSGMGRYHGKFSFDTFSH 375
Cdd:cd07102 421 ALAWTGVKDSGRGVTLSRLGYDQLTR 446
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
47-378 |
9.45e-60 |
|
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: 200.93 E-value: 9.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 47 SSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-----LPqyldQSCFAVVLGGP 121
Cdd:cd07089 115 GRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaetdLP----AGVVNVVTGSD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 122 EETGQLL--KHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 199
Cdd:cd07089 191 NAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 200 YVLCSQEMQERLVPALQNAITRF-YGD--NPQTspNLGRIINQKHFERLQGLLGCGR------VAIGGQSDEGER--YIA 268
Cdd:cd07089 271 RLLVPRSRYDEVVEALAAAFEALpVGDpaDPGT--VMGPLISAAQRDRVEGYIARGRdegarlVTGGGRPAGLDKgfYVE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 269 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYltL 348
Cdd:cd07089 349 PTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGY--G 426
|
330 340 350
....*....|....*....|....*....|
gi 1958654670 349 PALPLGGVGNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07089 427 PDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
51-363 |
1.06e-59 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 201.29 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 51 IRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQ-LLK 129
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDaLVG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 130 H-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ 208
Cdd:PRK13473 214 HpKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 209 ERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGL------LGCGRVAIGGQSDEGE-RYIAPTVLVDVQETEP 280
Cdd:PRK13473 294 DDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFverakaLGHIRVVTGGEAPDGKgYYYEPTLLAGARQDDE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 281 VMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLECtssGSFGGNDGFLYLTlpALPLGGVG 357
Cdd:PRK13473 374 IVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDvgrAHRVSARLQY---GCTWVNTHFMLVS--EMPHGGQK 448
|
....*.
gi 1958654670 358 NSGMGR 363
Cdd:PRK13473 449 QSGYGK 454
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
54-378 |
5.23e-59 |
|
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: 198.94 E-value: 5.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQLL-KHK 131
Cdd:cd07093 116 QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGFGPEAGAALvAHP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 132 -FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQER 210
Cdd:cd07093 196 dVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 211 LVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQSDEGER-----YIAPTVLVDVQETE 279
Cdd:cd07093 276 FLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVELARaegatILTGGGRPELPDleggyFVEPTVITGLDNDS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 280 PVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNG---QVVTQMLEctsSGSFGGNDgFLYLTLPAlPLGGV 356
Cdd:cd07093 356 RVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLgraHRVARRLE---AGTVWVNC-WLVRDLRT-PFGGV 430
|
330 340
....*....|....*....|..
gi 1958654670 357 GNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07093 431 KASGIGREGGDYSLEFYTELKN 452
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
49-363 |
6.34e-58 |
|
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: 196.42 E-value: 6.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETG-Q 126
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGdE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSDEGErYIAPTVLVDVQET 278
Cdd:cd07145 277 EVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndavekG-GKILYGGKRDEGS-FFPPTVLENDTPD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 279 EPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNgqvVTQMLECTSSGSFGG---NDGFLyLTLPALPLGG 355
Cdd:cd07145 355 MIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND---INRALKVARELEAGGvviNDSTR-FRWDNLPFGG 430
|
....*...
gi 1958654670 356 VGNSGMGR 363
Cdd:cd07145 431 FKKSGIGR 438
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
48-321 |
2.88e-57 |
|
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: 194.79 E-value: 2.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 48 SAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-----LPQYLdqscFAVVLGGPE 122
Cdd:cd07088 126 NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagLPAGV----LNIVTGRGS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 123 ETGQLL-KH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD- 199
Cdd:cd07088 202 VVGDALvAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAEr 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 200 -YVLCS--QEMQERLVPALQNAItrfYGDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSDEGER--YIA 268
Cdd:cd07088 282 vYVHEDiyDEFMEKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVEEMVeraveaG-ATLLTGGKRPEGEKgyFYE 357
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958654670 269 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN 321
Cdd:cd07088 358 PTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTEN 410
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-382 |
5.56e-57 |
|
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: 193.81 E-value: 5.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 38 VSTNFLTkfssaFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAV 116
Cdd:cd07115 105 VRGPFLN-----YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 117 VLGGPEETGQ-LLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 194
Cdd:cd07115 180 VTGFGEVAGAaLVEHPdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQM 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 195 CVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQSDeGER--Y 266
Cdd:cd07115 260 CTAGSRLLVHESIYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGreegaRLLTGGKRP-GARgfF 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 267 IAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNdgfLY- 345
Cdd:cd07115 339 VEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN---TYn 415
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958654670 346 LTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLLS 382
Cdd:cd07115 416 RFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
49-371 |
7.28e-57 |
|
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: 193.35 E-value: 7.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQ-L 127
Cdd:cd07108 111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAaL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYV--DDNCDpQTVANRVAWFRYFNAGQTCVAPDYVLCS 204
Cdd:cd07108 191 VDHpDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQGQSCTAGSRLFVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 205 QEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG------RVAIGGQSDEGER-----YIAPTVL 272
Cdd:cd07108 270 EDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPladgfFVQPTIF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 273 VDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFlyLTLPALP 352
Cdd:cd07108 350 SGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGG--GQQPGQS 427
|
330
....*....|....*....
gi 1958654670 353 LGGVGNSGMGRyhgKFSFD 371
Cdd:cd07108 428 YGGFKQSGLGR---EASLE 443
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
42-373 |
3.13e-56 |
|
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: 191.95 E-value: 3.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 42 FLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-----LPqyldQSCFAV 116
Cdd:cd07138 117 FEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEIldeagLP----AGVFNL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 117 VLGGPEETGQLL-KH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCD-----PQTVANrvawfRYF 189
Cdd:cd07138 193 VNGDGPVVGEALsAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADlekavPRGVAA-----CFA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 190 NAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGG-QSDE 262
Cdd:cd07138 268 NSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGGpGRPE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 263 G-ER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLEctsSGS 336
Cdd:cd07138 348 GlERgyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADperARAVARRLR---AGQ 424
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958654670 337 FGGNDGFLYltlPALPLGGVGNSGMGRYHGKFSFDTF 373
Cdd:cd07138 425 VHINGAAFN---PGAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
48-377 |
2.44e-55 |
|
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: 189.48 E-value: 2.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 48 SAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-----LPqyldQSCFAVVLGGPE 122
Cdd:cd07110 113 KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLP----PGVLNVVTGTGD 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 123 ETGQLLKH--KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 200
Cdd:cd07110 189 EAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 201 VLCSQEMQERLVPALQNAITRFYGDNPQTSP-NLGRIINQKHFERLQGLLGCG-----RVAIGGQSDEGER---YIAPTV 271
Cdd:cd07110 269 LLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARGkeegaRLLCGGRRPAHLEkgyFIAPTV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 272 LVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGflYLTLPAL 351
Cdd:cd07110 349 FADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCS--QPCFPQA 426
|
330 340
....*....|....*....|....*.
gi 1958654670 352 PLGGVGNSGMGRYHGKFSFDTFSHQR 377
Cdd:cd07110 427 PWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
47-374 |
3.49e-55 |
|
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: 188.17 E-value: 3.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 47 SSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEE-- 123
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLNVVTHSPEDap 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 124 --TGQLLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 200
Cdd:cd07105 170 evVEALIAHPaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 201 VLCSQEMQERLVPALQNAITRFYGDNPQtspnLGRIINQKHFERLQGL----LGCG-RVAIGGQSDEGER--YIAPTVLV 273
Cdd:cd07105 250 IIVHESIADEFVEKLKAAAEKLFAGPVV----LGSLVSAAAADRVKELvddaLSKGaKLVVGGLADESPSgtSMPPTILD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 274 DVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLEctsSGSFGGNDGFLYlTLPA 350
Cdd:cd07105 326 NVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlarALAVAKRIE---SGAVHINGMTVH-DEPT 401
|
330 340
....*....|....*....|....
gi 1958654670 351 LPLGGVGNSGMGRYHGKFSFDTFS 374
Cdd:cd07105 402 LPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
49-374 |
4.63e-55 |
|
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: 188.97 E-value: 4.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-----LPqyldQSCFAVVLGGPEE 123
Cdd:cd07112 118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLP----AGVLNVVPGFGHT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 124 TGQLL-KHK-FDYIFFTGSPRVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPD 199
Cdd:cd07112 194 AGEALgLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 200 YVLCSQEMQERLVPALQNAITRFY-GD--NPQTSpnLGRIINQKHFERLQGLLGCG-----RVAIGGQS---DEGERYIA 268
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKpGDplDPATR--MGALVSEAHFDKVLGYIESGkaegaRLVAGGKRvltETGGFFVE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 269 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFS---NNGQVVTQMLEC--TSSGSFGGNDgf 343
Cdd:cd07112 352 PTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTsdlSRAHRVARRLRAgtVWVNCFDEGD-- 429
|
330 340 350
....*....|....*....|....*....|.
gi 1958654670 344 lyltlPALPLGGVGNSGMGRYHGKFSFDTFS 374
Cdd:cd07112 430 -----ITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
50-373 |
1.49e-54 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 188.36 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLNlMIMPLVG-AIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQL 127
Cdd:PLN02278 155 LVLKQPVGVVGAITPWNFPLA-MITRKVGpALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 L--KHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:PLN02278 234 LlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQG------------LLGCGRVAIGGQsdegerYIAPTVL 272
Cdd:PLN02278 314 GIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVEShvqdavskgakvLLGGKRHSLGGT------FYEPTVL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 273 VDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGfLYLTLPAlP 352
Cdd:PLN02278 388 GDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEG-LISTEVA-P 465
|
330 340
....*....|....*....|.
gi 1958654670 353 LGGVGNSGMGRYHGKFSFDTF 373
Cdd:PLN02278 466 FGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
47-373 |
8.09e-53 |
|
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: 183.16 E-value: 8.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 47 SSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETG 125
Cdd:cd07139 129 GHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADREVGE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 126 QLLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 204
Cdd:cd07139 209 YLVRHPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 205 QEMQERLVPALQNAITRF-YGD--NPQTSpnLGRIINQKHFERLQGLLGCG-----RVAIGGQSDEG-ER--YIAPTVLV 273
Cdd:cd07139 289 RSRYDEVVEALAAAVAALkVGDplDPATQ--IGPLASARQRERVEGYIAKGraegaRLVTGGGRPAGlDRgwFVEPTLFA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 274 DVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQ----VVTQMlectSSGSFGGNdgflYLTL- 348
Cdd:cd07139 367 DVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVErglaVARRI----RTGTVGVN----GFRLd 438
|
330 340
....*....|....*....|....*
gi 1958654670 349 PALPLGGVGNSGMGRYHGKFSFDTF 373
Cdd:cd07139 439 FGAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
49-363 |
3.40e-52 |
|
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: 180.87 E-value: 3.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQ-YLDQSCFAVVLGGPEETG-Q 126
Cdd:cd07149 117 GFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVGdA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKHK-FDYIFFTGSPRVGKIVMAAAAkhLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07149 197 LVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGD--NPQTspNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEgeRYIAPTVLVDVQE 277
Cdd:cd07149 275 DIYDEFLERFVAATKKLvVGDplDEDT--DVGPMISEAEAERIEEWVeeaveGGARLLTGGKRDG--AILEPTVLTDVPP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 278 TEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVtqmLECTSSGSFGG---NDGFLYlTLPALPLG 354
Cdd:cd07149 351 DMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKA---LKAARELEVGGvmiNDSSTF-RVDHMPYG 426
|
....*....
gi 1958654670 355 GVGNSGMGR 363
Cdd:cd07149 427 GVKESGTGR 435
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
55-367 |
4.92e-52 |
|
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: 180.58 E-value: 4.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQLLKHKFD 133
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDNAD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 134 YIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVAnRVAWFRYF-NAGQTCVAPD--YVLCS--QEMQ 208
Cdd:cd07101 198 YVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAA-AGAVRACFsNAGQLCVSIEriYVHESvyDEFV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 209 ERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQS--DEGERYIAPTVLVDVQETEPV 281
Cdd:cd07101 277 RRFVARTRALRL---GAALDYGPDMGSLISQAQLDRVTAHVDDAVakgatVLAGGRArpDLGPYFYEPTVLTGVTEDMEL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 282 MQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLECtssGSFGGNDGFL--YLTLPAlPLGGV 356
Cdd:cd07101 354 FAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDgarGRRIAARLRA---GTVNVNEGYAaaWASIDA-PMGGM 429
|
330
....*....|.
gi 1958654670 357 GNSGMGRYHGK 367
Cdd:cd07101 430 KDSGLGRRHGA 440
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
51-374 |
7.78e-52 |
|
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: 180.58 E-value: 7.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 51 IRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQLL- 128
Cdd:cd07119 130 TVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELa 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 129 -KHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEM 207
Cdd:cd07119 210 eSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 208 QERLVPAL---QNAITRFYGDNPQTspNLGRIINQKHFERLQGLLGCG-----RVAIGGQSDEGER-----YIAPTVLVD 274
Cdd:cd07119 290 HDKFVAALaerAKKIKLGNGLDADT--EMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKRPTGDElakgyFVEPTIFDD 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 275 VQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDgfLYLTLPALPLG 354
Cdd:cd07119 368 VDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWG 445
|
330 340
....*....|....*....|
gi 1958654670 355 GVGNSGMGRYHGKFSFDTFS 374
Cdd:cd07119 446 GYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
49-378 |
3.63e-51 |
|
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: 178.51 E-value: 3.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-----LPQYLdqscFAVVLGGPEE 123
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV----VNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 124 TGQLL-KH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 201
Cdd:cd07114 189 TGEALvEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 202 LCSQEMQERLVPALQnAITRF--YGD--NPQTspNLGRIINQKHFERLQGLLGC-----GRVAIGGQSDEGER-----YI 267
Cdd:cd07114 269 LVQRSIYDEFVERLV-ARARAirVGDplDPET--QMGPLATERQLEKVERYVARareegARVLTGGERPSGADlgagyFF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 268 APTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN-GQV--VTQMLEctsSGSFGGNDgfl 344
Cdd:cd07114 346 EPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDlARAhrVARAIE---AGTVWVNT--- 419
|
330 340 350
....*....|....*....|....*....|....*
gi 1958654670 345 YLTL-PALPLGGVGNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07114 420 YRALsPSSPFGGFKDSGIGRENGIEAIREYTQTKS 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
47-374 |
4.82e-51 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 178.46 E-value: 4.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 47 SSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETG 125
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 126 QLL-KHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC 203
Cdd:TIGR01804 205 PLLvNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 SQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQSDEGER-----YIAPTVL 272
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEKGkaegaTLATGGGRPENVGlqngfFVEPTVF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 273 VDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLEctsSGSFGGNDGFLYltlP 349
Cdd:TIGR01804 365 ADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADlgrAHRVADQLE---AGTVWINTYNLY---P 438
|
330 340
....*....|....*....|....*.
gi 1958654670 350 A-LPLGGVGNSGMGRYHGKFSFDTFS 374
Cdd:TIGR01804 439 AeAPFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
49-362 |
5.24e-51 |
|
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: 177.94 E-value: 5.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQL 127
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LKH--KFDYIFFTGSPRVGKIVMAAAAkhLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07146 194 LIThpDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQK---HFE-RLQGLLGCG-RVAIGGQSDeGERYiAPTVLVDVQETE 279
Cdd:cd07146 272 SVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDEEaaiQIEnRVEEAIAQGaRVLLGNQRQ-GALY-APTVLDHVPPDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 280 PVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYlTLPALPLGGVGNS 359
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGF-RSELSPFGGVKDS 428
|
...
gi 1958654670 360 GMG 362
Cdd:cd07146 429 GLG 431
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
49-363 |
7.52e-51 |
|
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: 177.79 E-value: 7.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLG-GPEETGQ 126
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGfGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKH-KFDYIFFTGSPRVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANrVAWFR-YFNAGQTCVAPDYVLC 203
Cdd:cd07091 215 ISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVE-WAAFGiFFNQGQCCCAGSRIFV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 SQEMQERLVPAL-QNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQ--SDEGeRYIAPTVLVDV 275
Cdd:cd07091 294 QESIYDEFVEKFkARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGkkegaTLLTGGErhGSKG-YFIQPTVFTDV 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 276 QETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLEctsSGSFGGNDgflYLTL-PAL 351
Cdd:cd07091 373 KDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDinkALRVSRALK---AGTVWVNT---YNVFdAAV 446
|
330
....*....|..
gi 1958654670 352 PLGGVGNSGMGR 363
Cdd:cd07091 447 PFGGFKQSGFGR 458
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
33-378 |
1.11e-50 |
|
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: 177.60 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 33 MKDESVSTNFlTKFssAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQ 111
Cdd:cd07144 125 IQGKTIPTSP-NKL--AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 112 SCFAVVLGGPEETGQ-LLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYF 189
Cdd:cd07144 202 GVVNIIPGYGAVAGSaLAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMY 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 190 NAGQTCVAPDYVLCSQEMQERLVPALQNAITRFY--GDNPQTSPNLGRIINQKHFERLQGLLGCGR------VAIGGQSD 261
Cdd:cd07144 282 NSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKkegaklVYGGEKAP 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 262 EGER---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSF- 337
Cdd:cd07144 362 EGLGkgyFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVw 441
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958654670 338 --GGNDGFlyltlPALPLGGVGNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07144 442 inSSNDSD-----VGVPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
49-382 |
2.63e-50 |
|
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: 176.77 E-value: 2.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLL 128
Cdd:cd07559 130 SYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 129 KH--KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNP-------CYVDDNCDPQTVANRVAWFryFNAGQTCVAPD 199
Cdd:cd07559 210 AShpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPniffddaMDADDDFDDKAEEGQLGFA--FNQGEVCTCPS 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 200 YVLCSQEMQERLVPALQNAITRFYGDNPQ-TSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQ-----SDEGERYIA 268
Cdd:cd07559 288 RALVQESIYDEFIERAVERFEAIKVGNPLdPETMMGAQVSKDQLEKILSYVDIGKeegaeVLTGGErltlgGLDKGYFYE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 269 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNdgfLYLTL 348
Cdd:cd07559 368 PTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN---CYHQY 444
|
330 340 350
....*....|....*....|....*....|....*
gi 1958654670 349 PA-LPLGGVGNSGMGRYHGKFSFDTFSHQRACLLS 382
Cdd:cd07559 445 PAhAPFGGYKKSGIGRETHKMMLDHYQQTKNILVS 479
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
49-374 |
2.80e-50 |
|
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: 176.08 E-value: 2.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELL-PQYLDQSCFAVVLGGPEETGQL 127
Cdd:cd07094 117 AWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTGEREVLGDA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 L--KHKFDYIFFTGSPRVGKIVMAAAAKhlTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07094 197 FaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFERLQ-----GLLGCGRVAIGGQSDegERYIAPTVLVDVQETE 279
Cdd:cd07094 275 ELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVErwveeAVEAGARLLCGGERD--GALFKPTVLEDVPRDT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 280 PVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYLTlPALPLGGVGNS 359
Cdd:cd07094 353 KLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRT-DWMPFGGVKES 431
|
330
....*....|....*
gi 1958654670 360 GMGRYHGKFSFDTFS 374
Cdd:cd07094 432 GVGREGVPYAMEEMT 446
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
52-377 |
3.09e-50 |
|
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: 175.56 E-value: 3.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 52 RKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEK-VLAELLPQY-LDQSCFAVVLGGPEETGQLLK 129
Cdd:cd07152 107 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGvVIARLFEEAgLPAGVLHVLPGGADAGEALVE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 130 H-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ 208
Cdd:cd07152 187 DpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 209 ERLVPALQNAITRFYGDNPQTSP-NLGRIINQKHFERLQGL------LGcGRVAIGGQSDegERYIAPTVLVDVQETEPV 281
Cdd:cd07152 267 DAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIvddsvaAG-ARLEAGGTYD--GLFYRPTVLSGVKPGMPA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 282 MQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLEctsSGSFGGNDGflylTL---PALPLGG 355
Cdd:cd07152 344 FDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDvgrAMALADRLR---TGMLHINDQ----TVndePHNPFGG 416
|
330 340
....*....|....*....|...
gi 1958654670 356 VGNSGMG-RYHGKFSFDTFSHQR 377
Cdd:cd07152 417 MGASGNGsRFGGPANWEEFTQWQ 439
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
33-378 |
6.28e-50 |
|
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: 175.61 E-value: 6.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 33 MKDESVSTNFLTKFssAFIRKEPFGLVLIIAPWNYPLNL---MIMPlvgAIAAGNCVVLKPSEMSKNTEKVLAELLPQY- 108
Cdd:cd07131 115 LFGETVPSELPNKD--AMTRRQPIGVVALITPWNFPVAIpswKIFP---ALVCGNTVVFKPAEDTPACALKLVELFAEAg 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 109 LDQSCFAVVLGGPEETGQ-LLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWF 186
Cdd:cd07131 190 LPPGVVNVVHGRGEEVGEaLVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 187 RYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFERLQG-----------LLGCGRV 254
Cdd:cd07131 270 AFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDmGPLINEAQLEKVLNyneigkeegatLLLGGER 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 255 AIGGQSDEGeRYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPL--ALYAFSNNgQVVTQMLECT 332
Cdd:cd07131 350 LTGGGYEKG-YFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLssAIYTEDVN-KAFRARRDLE 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958654670 333 SsgsfggndGFLYLTLPA------LPLGGVGNSGMG-RYHGKFSFDTFSHQRA 378
Cdd:cd07131 428 A--------GITYVNAPTigaevhLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
48-363 |
1.72e-48 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 171.72 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 48 SAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQL 127
Cdd:TIGR03374 130 TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGKTVGDP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LK--HKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:TIGR03374 210 LTghEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAACRIYAQR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGL------LGCGRVAIGGQSDEGE-RYIAPTVLVDVQE 277
Cdd:TIGR03374 290 GIYDTLVEKLGAAVATLkSGAPDDESTELGPLSSLAHLERVMKAveeakaLGHIKVITGGEKRKGNgYYFAPTLLAGAKQ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 278 TEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYLTlpALPLGGVG 357
Cdd:TIGR03374 370 DDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFMLVS--EMPHGGQK 447
|
....*.
gi 1958654670 358 NSGMGR 363
Cdd:TIGR03374 448 LSGYGK 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
55-366 |
3.75e-48 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 171.60 E-value: 3.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQLLKHKFD 133
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDNAD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 134 YIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVP 213
Cdd:PRK09407 234 YLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 214 ALQNAITRF-----YGDNPQtspnLGRIINQKHFERLQGLLGCGR-----VAIGGQS--DEGERYIAPTVLVDVQETEPV 281
Cdd:PRK09407 314 AFVAAVRAMrlgagYDYSAD----MGSLISEAQLETVSAHVDDAVakgatVLAGGKArpDLGPLFYEPTVLTGVTPDMEL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 282 MQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLECtssGSFGGNDGFL--YLTLPAlPLGGV 356
Cdd:PRK09407 390 AREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDtarGRAIAARIRA---GTVNVNEGYAaaWGSVDA-PMGGM 465
|
330
....*....|
gi 1958654670 357 GNSGMGRYHG 366
Cdd:PRK09407 466 KDSGLGRRHG 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
48-366 |
1.31e-47 |
|
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: 169.16 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 48 SAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ 126
Cdd:cd07113 135 TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGAVGAQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07113 215 LISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQSDEGERY-IAPTVLVDVQET 278
Cdd:cd07113 295 SKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLDDARaegdeIVRGGEALAGEGYfVQPTLVLARSAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 279 EPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGN-DGFLYltlPALPLGGVG 357
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLD---PAVPFGGMK 451
|
....*....
gi 1958654670 358 NSGMGRYHG 366
Cdd:cd07113 452 QSGIGREFG 460
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
50-377 |
3.60e-47 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 168.76 E-value: 3.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLG-GPEETGQL 127
Cdd:PLN02467 146 YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGlGTEAGAPL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDpqtVANRVAW--FRYF-NAGQTCVAPDYVLC 203
Cdd:PLN02467 226 ASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVD---LDKAVEWamFGCFwTNGQICSATSRLLV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 SQ----EMQERLVPALQNaITrfYGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQSDEGER---YIAPTV 271
Cdd:PLN02467 303 HEriasEFLEKLVKWAKN-IK--ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKsegatILCGGKRPEHLKkgfFIEPTI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 272 LVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN---GQVVTQMLECtssgsfggndGFLYL-- 346
Cdd:PLN02467 380 ITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDlerCERVSEAFQA----------GIVWInc 449
|
330 340 350
....*....|....*....|....*....|....
gi 1958654670 347 ---TLPALPLGGVGNSGMGRYHGKFSFDTFSHQR 377
Cdd:PLN02467 450 sqpCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
50-321 |
3.74e-47 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 166.45 E-value: 3.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQLL 128
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 129 --KHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQE 206
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 207 MQERLVPALQNAITRFYGDNP--QTSPNLGRIINQKHFERLQGLLG-----CGRVAIGGQSDEGERYI-APTVLVDVQET 278
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFGNPaeRNDIAMGPLINAAALERVEQKVAraveeGARVALGGKAVEGKGYYyPPTLLLDVRQE 305
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958654670 279 EPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN 321
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQN 348
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
27-373 |
4.29e-47 |
|
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: 166.87 E-value: 4.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 27 KNLQTWMKDESVSTnfltKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSE----MSKNTEKVLA 102
Cdd:cd07100 72 ENAEAFLADEPIET----DAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASnvpgCALAIEELFR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 103 EL-LPQYldqsCFAVVLGGPEETGQLLKHkfDYI---FFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQT 178
Cdd:cd07100 148 EAgFPEG----VFQNLLIDSDQVEAIIAD--PRVrgvTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 179 VANRVAWFRYFNAGQTCVAP------DYVLcsQEMQERLVPALQNAITrfyGD--NPQTspNLGRIINQKHFERLQGLL- 249
Cdd:cd07100 222 AVKTAVKGRLQNAGQSCIAAkrfivhEDVY--DEFLEKFVEAMAALKV---GDpmDEDT--DLGPLARKDLRDELHEQVe 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 250 -----GCgRVAIGGQSDEGER-YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN-- 321
Cdd:cd07100 295 eavaaGA-TLLLGGKRPDGPGaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDle 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958654670 322 -GQVVTQMLEC--TSSGSFGGNDgflyltlPALPLGGVGNSGMGRYHGKFSFDTF 373
Cdd:cd07100 374 rAERVARRLEAgmVFINGMVKSD-------PRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
49-378 |
9.78e-47 |
|
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: 166.94 E-value: 9.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQL 127
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LK-H-KFDYIFFTGSPRVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 204
Cdd:cd07143 218 ISsHmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 205 QEMQERLVPALQNAITRFYGDNPqTSPNL--GRIINQKHFERLQGLLGCGR-----VAIGGQSDEGERY-IAPTVLVDVQ 276
Cdd:cd07143 298 EGIYDKFVKRFKEKAKKLKVGDP-FAEDTfqGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFTDVT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 277 ETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDgflYLTL-PALPLGG 355
Cdd:cd07143 377 EDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNC---YNLLhHQVPFGG 453
|
330 340
....*....|....*....|...
gi 1958654670 356 VGNSGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07143 454 YKQSGIGRELGEYALENYTQIKA 476
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
50-374 |
3.76e-46 |
|
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: 165.11 E-value: 3.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ-L 127
Cdd:cd07097 130 ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQaL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQE 206
Cdd:cd07097 210 VEHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 207 MQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERL-----QGLLGCGRVAIGGQSDEGER---YIAPTVLVDVQE 277
Cdd:cd07097 290 IHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDlryieIARSEGAKLVYGGERLKRPDegyYLAPALFAGVTN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 278 TEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLAL--------YA--FSNNGQVVTQMLECTSSGsfggndgflylT 347
Cdd:cd07097 370 DMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAgivttslkHAthFKRRVEAGVVMVNLPTAG-----------V 438
|
330 340
....*....|....*....|....*...
gi 1958654670 348 LPALPLGGVGNSGMG-RYHGKFSFDTFS 374
Cdd:cd07097 439 DYHVPFGGRKGSSYGpREQGEAALEFYT 466
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
36-374 |
4.11e-46 |
|
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: 165.32 E-value: 4.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 36 ESVSTNFLTKFSSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFA 115
Cdd:cd07117 117 EEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 116 VVLGGPEETGQLLKHK--FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 193
Cdd:cd07117 197 IVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 194 TCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQT-SPNLGRIINQKHFERLQGLLGCG-----RVAIGGQS------D 261
Cdd:cd07117 277 VCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDpDTQMGAQVNKDQLDKILSYVDIAkeegaKILTGGHRltenglD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 262 EGErYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNd 341
Cdd:cd07117 357 KGF-FIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN- 434
|
330 340 350
....*....|....*....|....*....|....
gi 1958654670 342 gfLYLTLPA-LPLGGVGNSGMGRYHGKFSFDTFS 374
Cdd:cd07117 435 --TYNQIPAgAPFGGYKKSGIGRETHKSMLDAYT 466
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
47-375 |
2.82e-45 |
|
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: 162.47 E-value: 2.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 47 SSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGpEETG 125
Cdd:cd07090 108 SFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 126 QLLKHKFDY--IFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL- 202
Cdd:cd07090 187 QLLCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFv 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 203 ---CSQEMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQSD------EGERYIA 268
Cdd:cd07090 267 qrsIKDEFTERLVERTKKIRI---GDPLDEDTQMGALISEEHLEKVLGYIESAkqegaKVLCGGERVvpedglENGFYVS 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 269 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQ----VVTQMlectSSGSFGGNDgfl 344
Cdd:cd07090 344 PCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQrahrVIAQL----QAGTCWINT--- 416
|
330 340 350
....*....|....*....|....*....|..
gi 1958654670 345 YLTLPA-LPLGGVGNSGMGRYHGKFSFDTFSH 375
Cdd:cd07090 417 YNISPVeVPFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
53-378 |
6.33e-45 |
|
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: 162.28 E-value: 6.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 53 KEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLG-GPEETGQLLKH 130
Cdd:cd07142 139 HEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGfGPTAGAAIASH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 131 K-FDYIFFTGSPRVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ 208
Cdd:cd07142 219 MdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIY 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 209 ERLVP-ALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQS--DEGeRYIAPTVLVDVQETEP 280
Cdd:cd07142 299 DEFVEkAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGkeegaTLITGGDRigSKG-YYIQPTIFSDVKDDMK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 281 VMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGN--DGFlyltLPALPLGGVGN 358
Cdd:cd07142 378 IARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVF----DASIPFGGYKM 453
|
330 340
....*....|....*....|
gi 1958654670 359 SGMGRYHGKFSFDTFSHQRA 378
Cdd:cd07142 454 SGIGREKGIYALNNYLQVKA 473
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
50-366 |
1.04e-44 |
|
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: 161.00 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQ-LL 128
Cdd:cd07107 111 YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAaLV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 129 KHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANR-VAWFRYFNAGQTCVAPDYVLCSQE 206
Cdd:cd07107 191 RHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAaVAGMNFTWCGQSCGSTSRLFVHES 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 207 MQERLVPALQNAITRFYGDNPqTSPN--LGRIINQKHFERLQGLLGCG-----RVAIGGQSDEGER-----YIAPTVLVD 274
Cdd:cd07107 271 IYDEVLARVVERVAAIKVGDP-TDPAttMGPLVSRQQYDRVMHYIDSAkregaRLVTGGGRPEGPAleggfYVEPTVFAD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 275 VQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSF---GGNDGFLyltlpAL 351
Cdd:cd07107 350 VTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVwinGSSRHFL-----GA 424
|
330
....*....|....*
gi 1958654670 352 PLGGVGNSGMGRYHG 366
Cdd:cd07107 425 PFGGVKNSGIGREEC 439
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
54-321 |
1.86e-44 |
|
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: 161.62 E-value: 1.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ-LLKH- 130
Cdd:cd07124 165 RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDyLVEHp 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 131 KFDYIFFTGSPRVGKIVMAAAAK------HLTPITLELGGKNPCYVDDNCDPQTVANRV--AWFRYfnAGQTCVApdyvl 202
Cdd:cd07124 245 DVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIvrSAFGF--QGQKCSA----- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 203 CS---------QEMQERLVpALQNAITrfYGDNPQTSPNLGRIINQKHFERLQGLL----GCGRVAIGGQSDEGER---Y 266
Cdd:cd07124 318 CSrvivhesvyDEFLERLV-ERTKALK--VGDPEDPEVYMGPVIDKGARDRIRRYIeigkSEGRLLLGGEVLELAAegyF 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958654670 267 IAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN 321
Cdd:cd07124 395 VQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRS 449
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
49-363 |
2.74e-44 |
|
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: 160.43 E-value: 2.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSemsknTEKVL-AELLPQYLDQSCF-----AVVLG-GP 121
Cdd:cd07082 135 AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA-----TQGVLlGIPLAEAFHDAGFpkgvvNVVTGrGR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 122 EETGQLLKH-KFDYIFFTGSPRVGKIVMAAAAKhlTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 200
Cdd:cd07082 210 EIGDPLVTHgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 201 VLCSQEMQERLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSdEGERYIAPTVLV 273
Cdd:cd07082 288 VLVHESVADELVELLKEEVAKLKVGMPwDNGVDITPLIDPKSADFVEGLIddavakG-ATVLNGGGR-EGGNLIYPTLLD 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 274 DVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN----GQVVTQMLECT---SSGSFGGNDGFlyl 346
Cdd:cd07082 366 PVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDinkaRKLADALEVGTvniNSKCQRGPDHF--- 442
|
330
....*....|....*..
gi 1958654670 347 tlpalPLGGVGNSGMGR 363
Cdd:cd07082 443 -----PFLGRKDSGIGT 454
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
51-374 |
2.42e-43 |
|
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: 157.51 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 51 IRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQ--YLDQSCFAVVLGGPEETGQLL 128
Cdd:cd07120 113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 129 --KHKFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC--- 203
Cdd:cd07120 193 vaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVqrs 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 -SQEMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLLG-----CGRVAI-GGQSDEGER---YIAPTVLV 273
Cdd:cd07120 273 iADEVRDRLAARLAAVKV---GPGLDPASDMGPLIDRANVDRVDRMVEraiaaGAEVVLrGGPVTEGLAkgaFLRPTLLE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 274 DVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGND-GFLYltlPALP 352
Cdd:cd07120 350 VDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDwNKLF---AEAE 426
|
330 340
....*....|....*....|..
gi 1958654670 353 LGGVGNSGMGRYHGKFSFDTFS 374
Cdd:cd07120 427 EGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
51-374 |
2.52e-43 |
|
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: 157.47 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 51 IRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVL-AELLPQY-LDQSCFAVVLGGPEETG-QL 127
Cdd:cd07151 126 VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLlAKIFEEAgLPKGVLNVVVGAGSEIGdAF 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LKHKF-DYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQE 206
Cdd:cd07151 206 VEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHED 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 207 MQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSdEGeRYIAPTVLVDVQETE 279
Cdd:cd07151 286 VYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIeqaveeG-ATLLVGGEA-EG-NVLEPTVLSDVTNDM 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 280 PVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYlTLPALPLGGVGNS 359
Cdd:cd07151 363 EIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEPHVPFGGEKNS 441
|
330
....*....|....*
gi 1958654670 360 GMGRYHGKFSFDTFS 374
Cdd:cd07151 442 GLGRFNGEWALEEFT 456
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
49-374 |
8.38e-43 |
|
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: 156.35 E-value: 8.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELlpqyLDQSCFA-----VVLG-GPE 122
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASL----IKEAGFPpgvvnVVPGyGPT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 123 ETGQLLKH-KFDYIFFTGSPRVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 200
Cdd:cd07141 215 AGAAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 201 VLCSQEMQERLVP-ALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGqSDEGER--YIAPTVL 272
Cdd:cd07141 295 TFVQESIYDEFVKrSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGkkegaKLECGG-KRHGDKgyFIQPTVF 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 273 VDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDgfLYLTLPALP 352
Cdd:cd07141 374 SDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNC--YNVVSPQAP 451
|
330 340
....*....|....*....|..
gi 1958654670 353 LGGVGNSGMGRYHGKFSFDTFS 374
Cdd:cd07141 452 FGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
48-363 |
1.21e-42 |
|
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: 155.48 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 48 SAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELL-PQYLDQSCFAVVLGGPEETGQ 126
Cdd:cd07147 116 QGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKHK-FDYIFFTGSPRVG-KIVMAAAAKHltpITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 204
Cdd:cd07147 196 LVTDErIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 205 Q----EMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGerYIAPTVLVDV 275
Cdd:cd07147 273 RsvydEFKSRLVARVKALKT---GDPKDDATDVGPMISESEAERVEGWVneavdAGAKLLTGGKRDGA--LLEPTILEDV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 276 QETEPVMQEEIFGPILPLVTVRSLDEAVNFINQ-----------REKPLALYAFSNngqvvtqmLECtssgsfGG---ND 341
Cdd:cd07147 348 PPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDskfglqagvftRDLEKALRAWDE--------LEV------GGvviND 413
|
330 340
....*....|....*....|....*..
gi 1958654670 342 gflyltLPA-----LPLGGVGNSGMGR 363
Cdd:cd07147 414 ------VPTfrvdhMPYGGVKDSGIGR 434
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
54-321 |
3.38e-42 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 155.48 E-value: 3.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ-LLKH- 130
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDyLVDHp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 131 KFDYIFFTGSPRVGKIVMAAAAK------HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVApdyvlCS 204
Cdd:PRK03137 250 KTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA-----CS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 205 Q---------EMQERLVpALQNAITrfYGdNPQTSPNLGRIINQKHFERLQGLL----GCGRVAIGGQSDEGERY-IAPT 270
Cdd:PRK03137 325 RaivhedvydEVLEKVV-ELTKELT--VG-NPEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQPT 400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958654670 271 VLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN 321
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNN 451
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
54-367 |
1.88e-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: 152.55 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQLLKH-K 131
Cdd:cd07111 146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSFGSALANHpG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 132 FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERL 211
Cdd:cd07111 226 VDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEEL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 212 VPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCGRvAIGGQ--------SDEGERYiAPTVLVDVQETEPVM 282
Cdd:cd07111 306 IRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADvfqpgadlPSKGPFY-PPTLFTNVPPASRIA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 283 QEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYltLPALPLGGVGNSGMG 362
Cdd:cd07111 384 QEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLF--DAAAGFGGYRESGFG 461
|
....*
gi 1958654670 363 RYHGK 367
Cdd:cd07111 462 REGGK 466
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
53-386 |
4.40e-41 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 152.28 E-value: 4.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 53 KEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLG-GPEETGQLLKH 130
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGfGPTAGAAIASH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 131 -KFDYIFFTGSPRVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ 208
Cdd:PLN02766 236 mDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 209 ERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQS--DEGeRYIAPTVLVDVQETEP 280
Cdd:PLN02766 316 DEFVKKLVEKAKDWvVGDPFDPRARQGPQVDKQQFEKILSYIEHGKregatLLTGGKPcgDKG-YYIEPTIFTDVTEDMK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 281 VMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYltLPALPLGGVGNSG 360
Cdd:PLN02766 395 IAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAF--DPDCPFGGYKMSG 472
|
330 340
....*....|....*....|....*....
gi 1958654670 361 MGRYHGKFSFDTFSHQRAC---LLSSPGM 386
Cdd:PLN02766 473 FGRDQGMDALDKYLQVKSVvtpLYNSPWL 501
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
53-373 |
4.89e-40 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 148.90 E-value: 4.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 53 KEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLG-----GPEETGQ 126
Cdd:PRK11241 144 KQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGELTSN 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 LLKHKFDyifFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQE 206
Cdd:PRK11241 224 PLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 207 MQERLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFERLQ-----GLLGCGRVAIGGQSDE-GERYIAPTVLVDVQETE 279
Cdd:PRK11241 301 VYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANA 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 280 PVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFlyLTLPALPLGGVGNS 359
Cdd:PRK11241 381 KVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNEVAPFGGIKAS 458
|
330
....*....|....
gi 1958654670 360 GMGRYHGKFSFDTF 373
Cdd:PRK11241 459 GLGREGSKYGIEDY 472
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
55-379 |
5.92e-40 |
|
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: 148.48 E-value: 5.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPL-----NLMImplvgAIAAGNCVVLKPSE----MSKNTEKVLAELLPQY-LDQSCFAVVLGGpEET 124
Cdd:cd07086 133 PLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIAVTKILAEVLEKNgLPPGVVNLVTGG-GDG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 125 GQLLKH--KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL 202
Cdd:cd07086 207 GELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 203 CSQEMQERLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFERLQGLL------GcGRVAIGG---QSDEGERYIAPTVL 272
Cdd:cd07086 287 VHESVYDEFLERLVKAYKQVRIGDPLDEGTLvGPLINQAAVEKYLNAIeiaksqG-GTVLTGGkriDGGEPGNYVEPTIV 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 273 VDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLectssGSFGGNDGFLYLTLPA-- 350
Cdd:cd07086 366 TGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWL-----GPKGSDCGIVNVNIPTsg 440
|
330 340 350
....*....|....*....|....*....|...
gi 1958654670 351 ----LPLGGVGNSGMGRYHGKFSFDTFSHQRAC 379
Cdd:cd07086 441 aeigGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
49-307 |
8.37e-40 |
|
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: 148.05 E-value: 8.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLnlMI----MPLvgAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEE 123
Cdd:cd07085 130 TYSYRQPLGVVAGITPFNFPA--MIplwmFPM--AIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 124 TGQLLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL 202
Cdd:cd07085 206 VNALLDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAV 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 203 CSQEMQERLVPALQNAITRF---YGDNPQTspNLGRIINQKHFERLQGLLGCG-----RVAIGG---QSDEGER--YIAP 269
Cdd:cd07085 286 AVGDEADEWIPKLVERAKKLkvgAGDDPGA--DMGPVISPAAKERIEGLIESGveegaKLVLDGrgvKVPGYENgnFVGP 363
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958654670 270 TVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFIN 307
Cdd:cd07085 364 TILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIIN 401
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
55-321 |
3.72e-39 |
|
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: 146.93 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQ-LLKH-K 131
Cdd:TIGR01237 167 PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVVQFVPGSGSEVGDyLVDHpK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 132 FDYIFFTGSPRVGKIVMAAAAK------HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:TIGR01237 247 TSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 ----EMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLLGCG----RVAIGGQSDEGERY-IAPTVLVDVQ 276
Cdd:TIGR01237 327 kvydEVVERFVEITESLKV---GPPDSADVYVGPVIDQKSFNKIMEYIEIGkaegRLVSGGCGDDSKGYfIGPTIFADVD 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958654670 277 ETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN 321
Cdd:TIGR01237 404 RKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNN 448
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
54-378 |
1.96e-38 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 145.34 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLnLMIMPLVG-AIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLG-GPEETGQLLKH 130
Cdd:PLN02466 194 EPIGVAGQIIPWNFPL-LMFAWKVGpALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 131 -KFDYIFFTGSPRVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ 208
Cdd:PLN02466 273 mDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 209 ERLV-PALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQ--SDEGeRYIAPTVLVDVQETEP 280
Cdd:PLN02466 353 DEFVeKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGvesgaTLECGGDrfGSKG-YYIQPTVFSNVQDDML 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 281 VMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYLTlpALPLGGVGNSG 360
Cdd:PLN02466 432 IAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDA--AIPFGGYKMSG 509
|
330
....*....|....*...
gi 1958654670 361 MGRYHGKFSFDTFSHQRA 378
Cdd:PLN02466 510 IGREKGIYSLNNYLQVKA 527
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
49-374 |
9.24e-38 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 142.73 E-value: 9.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQL 127
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LK--HKFDYIFFTGSPRVGKIVMA-AAAKHLTPITLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPDYVLC 203
Cdd:PRK09847 231 LSrhNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 SQEMQERLVPALQNAITRFY-GD--NPQTSpnLGRIINQKHFER----LQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQ 276
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQpGHplDPATT--MGTLIDCAHADSvhsfIREGESKGQLLLDGRNAGLAAAIGPTIFVDVD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 277 ETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSF---GGNDGFLyltlpALPL 353
Cdd:PRK09847 389 PNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGDM-----TVPF 463
|
330 340
....*....|....*....|.
gi 1958654670 354 GGVGNSGMGRYHGKFSFDTFS 374
Cdd:PRK09847 464 GGYKQSGNGRDKSLHALEKFT 484
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
20-363 |
3.54e-35 |
|
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: 134.71 E-value: 3.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 20 NEVDLALKNLQTWMKDESVSTNFLTkfssAFIRKEPFGLVLIIAPWNYPLNL---MIMPlvgAIAAGNCVVLKPSEMSKN 96
Cdd:cd07095 66 GKIDISIKAYHERTGERATPMAQGR----AVLRHRPHGVMAVFGPFNFPGHLpngHIVP---ALLAGNTVVFKPSELTPA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 97 TEKVLAELL-PQYLDQSCFAVVLGGPEETGQLLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPI-TLELGGKNPCYVDDN 173
Cdd:cd07095 139 VAELMVELWeEAGLPPGVLNLVQGGRETGEALAAHEgIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 174 CDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ-ERLVPALQNAITRFYGDNPQTSPN-LGRIINQKHFERL----QG 247
Cdd:cd07095 219 ADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAARYllaqQD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 248 LLGCGRVAIGGQS--DEGERYIAPTvLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVV 325
Cdd:cd07095 299 LLALGGEPLLAMErlVAGTAFLSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALF 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958654670 326 TQMLEctssgsfGGNDGFLYLTLP------ALPLGGVGNSGMGR 363
Cdd:cd07095 378 ERFLA-------RIRAGIVNWNRPttgassTAPFGGVGLSGNHR 414
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
54-382 |
5.88e-35 |
|
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: 134.89 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSCFAVVLGGPEETGQLL--KHK 131
Cdd:cd07116 135 EPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLasSKR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 132 FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNP-CYVDD--NCDPQTVANRVAWFRYF--NAGQTCVAPDYVLCSQE 206
Cdd:cd07116 215 IAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADvmDADDAFFDKALEGFVMFalNQGEVCTCPSRALIQES 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 207 MQERLvpaLQNAITRF----YGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQ-----SDEGERYIAPTVL 272
Cdd:cd07116 295 IYDRF---MERALERVkaikQGNPLDTETMIGAQASLEQLEKILSYIDIGKeegaeVLTGGErnelgGLLGGGYYVPTTF 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 273 VDVQETEpVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYltlPA-L 351
Cdd:cd07116 372 KGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLY---PAhA 447
|
330 340 350
....*....|....*....|....*....|.
gi 1958654670 352 PLGGVGNSGMGRYHGKFSFDTFSHQRACLLS 382
Cdd:cd07116 448 AFGGYKQSGIGRENHKMMLDHYQQTKNLLVS 478
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
49-374 |
2.53e-34 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 133.08 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVlGGPEETGQL 127
Cdd:PRK13252 136 VYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVV-QGDGRVGAW 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LKH--KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQT------VANrvawfrYFNAGQTCVAPD 199
Cdd:PRK13252 215 LTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRaadiamLAN------FYSSGQVCTNGT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 200 YVLCSQEMQERLVPALQNAITRFY-GD--NPQTspNLGRIINQKHFERLQGLLGCG-----RVAIGGQ------SDEGEr 265
Cdd:PRK13252 289 RVFVQKSIKAAFEARLLERVERIRiGDpmDPAT--NFGPLVSFAHRDKVLGYIEKGkaegaRLLCGGErlteggFANGA- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 266 YIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNN----GQVVTQMlectSSG-----S 336
Cdd:PRK13252 366 FVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVIHQL----EAGicwinT 441
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958654670 337 FGgndgflyLTLPALPLGGVGNSGMGRYHGKFSFDTFS 374
Cdd:PRK13252 442 WG-------ESPAEMPVGGYKQSGIGRENGIATLEHYT 472
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
55-362 |
2.93e-34 |
|
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: 133.09 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQLL--KHK 131
Cdd:cd07083 154 GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLteHER 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 132 FDYIFFTGSPRVGKIVMAAAAKHLT------PITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07083 234 IRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQ 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCGR----VAIGGQSDEGERY-IAPTVLVDVQETE 279
Cdd:cd07083 314 GAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYfVAPTVVEEVPPKA 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 280 PVMQEEIFGPILPLVTVRSLD--EAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYLTLPALPLGGVG 357
Cdd:cd07083 394 RIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFK 473
|
....*
gi 1958654670 358 NSGMG 362
Cdd:cd07083 474 LSGTN 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
50-291 |
1.37e-29 |
|
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: 119.91 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-LPQYLDQSCFAVVLGGPEETGQLL 128
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 129 KHKFDY--IFFTGSPRVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 205
Cdd:cd07140 222 SDHPDVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 206 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERL-----QGLLGCGRVAIGG-QSDEGERYIAPTVLVDVQET 278
Cdd:cd07140 302 SIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDH 381
|
250
....*....|...
gi 1958654670 279 EPVMQEEIFGPIL 291
Cdd:cd07140 382 MFIAKEESFGPIM 394
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
51-308 |
3.05e-26 |
|
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: 110.36 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 51 IRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELL-----PQYLDQscfaVVLGGPEETG 125
Cdd:cd07125 163 LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheagvPRDVLQ----LVPGDGEEIG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 126 Q-LLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITL---ELGGKNPCYVDDNCDP-QTVANRVA-WFRyfNAGQTCVAP 198
Cdd:cd07125 239 EaLVAHPrIDGVIFTGSTETAKLINRALAERDGPILPliaETGGKNAMIVDSTALPeQAVKDVVQsAFG--SAGQRCSAL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 199 DyVLCSQE-MQERLVPALQNAITRFYGDNPQT-SPNLGRIINQKHFERLQGLL----GCGRVAIGGQSDEGE-RYIAPTV 271
Cdd:cd07125 317 R-LLYLQEeIAERFIEMLKGAMASLKVGDPWDlSTDVGPLIDKPAGKLLRAHTelmrGEAWLIAPAPLDDGNgYFVAPGI 395
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958654670 272 LVDVqeTEPVMQEEIFGPILPLVTVRS--LDEAVNFINQ 308
Cdd:cd07125 396 IEIV--GIFDLTTEVFGPILHVIRFKAedLDEAIEDINA 432
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
43-362 |
1.36e-24 |
|
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: 105.19 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 43 LTKFSS---AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-----LPQyldQSCF 114
Cdd:cd07148 109 LTPASAgriAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLlheagLPE---GWCQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 115 AVVLGGPEETGQLLKHKFDYIFFTGSPRVGKIVMAAAAKHlTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 194
Cdd:cd07148 186 AVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 195 CVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERL-----QGLLGCGRVAIGGQSdEGERYIA 268
Cdd:cd07148 265 CVSVQRVFVPAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVeewvnEAVAAGARLLCGGKR-LSDTTYA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 269 PTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINqrEKPLALYA--FSNNGQVVTQMLECTSSGSFGGNDGFLYL 346
Cdd:cd07148 344 PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQAN--SLPVAFQAavFTKDLDVALKAVRRLDATAVMVNDHTAFR 421
|
330
....*....|....*.
gi 1958654670 347 TlPALPLGGVGNSGMG 362
Cdd:cd07148 422 V-DWMPFAGRRQSGYG 436
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
47-363 |
9.02e-24 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 102.89 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 47 SSAFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETG 125
Cdd:PRK09406 115 SRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAgFPDGCFQTLLVGSGAVE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 126 QLLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 204
Cdd:PRK09406 195 AILRDpRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVH 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 205 ----QEMQERLVPALQnAITrfYGDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGER-YIAPTVLVD 274
Cdd:PRK09406 275 advyDAFAEKFVARMA-ALR--VGDPTDPDTDVGPLATEQGRDEVEKQVddavaAGATILCGGKRPDGPGwFYPPTVITD 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 275 VQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDgfLYLTLPALPLG 354
Cdd:PRK09406 352 ITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFG 429
|
....*....
gi 1958654670 355 GVGNSGMGR 363
Cdd:PRK09406 430 GVKRSGYGR 438
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
55-307 |
1.20e-23 |
|
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: 102.67 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPL-----NLMImplvgAIAAGNCVVLKPSE----MSKNTEKVLAELLPQY-LDQSCFAVVLGGPEET 124
Cdd:cd07130 132 PLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttplTAIAVTKIVARVLEKNgLPGAIASLVCGGADVG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 125 GQLLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC 203
Cdd:cd07130 207 EALVKDPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 SQEMQERLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFERLQGLL------GcGRVAIGGQSDEGE-RYIAPTVlVDV 275
Cdd:cd07130 287 HESIYDEVLERLKKAYKQVRIGDPLDDGTLvGPLHTKAAVDNYLAAIeeaksqG-GTVLFGGKVIDGPgNYVEPTI-VEG 364
|
250 260 270
....*....|....*....|....*....|..
gi 1958654670 276 QETEPVMQEEIFGPILPLVTVRSLDEAVNFIN 307
Cdd:cd07130 365 LSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
49-373 |
2.67e-23 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 101.48 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQL 127
Cdd:PRK13968 120 AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgIPQGVYGWLNADNDGVSQM 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 128 LKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC--- 203
Cdd:PRK13968 200 INDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIeeg 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 204 -SQEMQERLVPALQnAITrfYGDNPQTSPNLGRI----INQKHFERLQGLLGCG-RVAIGGQSDEGE-RYIAPTVLVDVQ 276
Cdd:PRK13968 280 iASAFTERFVAAAA-ALK--MGDPRDEENALGPMarfdLRDELHHQVEATLAEGaRLLLGGEKIAGAgNYYAPTVLANVT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 277 ETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQM---LECtsSGSFggNDGFlYLTLPALPL 353
Cdd:PRK13968 357 PEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMaarLEC--GGVF--INGY-CASDARVAF 431
|
330 340
....*....|....*....|
gi 1958654670 354 GGVGNSGMGRYHGKFSFDTF 373
Cdd:PRK13968 432 GGVKKSGFGRELSHFGLHEF 451
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
54-362 |
7.69e-23 |
|
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: 100.37 E-value: 7.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQY-LDQSCFAVVLGGPEETGQLLKH-- 130
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALTSdp 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 131 KFDYIFFTGSPRVGKIVMAAAAKHL---TPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDyVLCSQE- 206
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALR-VLCVQEd 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 207 MQERLVPALQNAITRFYGDNP-QTSPNLGRIINQK-------HFERLQGLLGCGRVAIGGQSDEGER--YIAPTV--LVD 274
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEakqnllaHIEHMSQTQKKIAQLTLDDSRACQHgtFVAPTLfeLDD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 275 VQEtepvMQEEIFGPILPLVTVRS--LDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGFLYLTLPALP 352
Cdd:TIGR01238 398 IAE----LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQP 473
|
330
....*....|
gi 1958654670 353 LGGVGNSGMG 362
Cdd:TIGR01238 474 FGGQGLSGTG 483
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
49-360 |
1.19e-22 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 99.65 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 49 AFIRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMsknTEKVlAELLPQYLDQS-----CFAVVLGGPEE 123
Cdd:PRK09457 128 AVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSEL---TPWV-AELTVKLWQQAglpagVLNLVQGGRET 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 124 TGQLLKHK-FDYIFFTGSPRVGKIVMAAAAKHLTPI-TLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 201
Cdd:PRK09457 204 GKALAAHPdIDGLLFTGSANTGYLLHRQFAGQPEKIlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 202 LCSQEMQ-ERLVPALQNAITRFYGDNP--QTSPNLGRIINQKHFERL----QGLLGCGRVAI--GGQSDEGERYIAPTvL 272
Cdd:PRK09457 284 LVPQGAQgDAFLARLVAVAKRLTVGRWdaEPQPFMGAVISEQAAQGLvaaqAQLLALGGKSLleMTQLQAGTGLLTPG-I 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 273 VDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDgflyltlP--- 349
Cdd:PRK09457 363 IDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNK-------Pltg 435
|
330
....*....|....
gi 1958654670 350 ---ALPLGGVGNSG 360
Cdd:PRK09457 436 assAAPFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
53-307 |
1.68e-21 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 96.36 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 53 KEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSemsknTEKVLAELLPqyldQSCF----------AVVLGGPE 122
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPP-----TQGAVAALHM----VHCFhlagfpkgliSCVTGKGS 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 123 ETGQLL-KHK-FDYIFFTGsprvGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 199
Cdd:PLN00412 227 EIGDFLtMHPgVNCISFTG----GDTGIAISKKaGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 200 YVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAIGGQSDEGER---YIAPTVLVDVQ 276
Cdd:PLN00412 303 VVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIWPLLLDNVR 382
|
250 260 270
....*....|....*....|....*....|.
gi 1958654670 277 ETEPVMQEEIFGPILPLVTVRSLDEAVNFIN 307
Cdd:PLN00412 383 PDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
55-379 |
1.68e-19 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 90.28 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLK--PSE--MSKNTEKVLAELLPQY-LDQSCFAVVLGGPEeTGQLLK 129
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCGGAE-IGEAIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 130 H--KFDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEM 207
Cdd:PLN02315 233 KdtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 208 QERLVPALQNAITRF-YGDNPQTSPNLGRI---INQKHFE------RLQGllgcGRVAIGGQSDEGE-RYIAPTVlVDVQ 276
Cdd:PLN02315 313 YDDVLEQLLTVYKQVkIGDPLEKGTLLGPLhtpESKKNFEkgieiiKSQG----GKILTGGSAIESEgNFVQPTI-VEIS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 277 ETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLectssGSFGGNDGFLYLTLPAL----- 351
Cdd:PLN02315 388 PDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWI-----GPLGSDCGIVNVNIPTNgaeig 462
|
330 340
....*....|....*....|....*....
gi 1958654670 352 -PLGGVGNSGMGRYHGKFSFDTFSHQRAC 379
Cdd:PLN02315 463 gAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
53-375 |
2.18e-19 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 90.19 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 53 KEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAEL-LPQYLDQSCFAVVLGGPEETGQLLKHK 131
Cdd:PLN02419 247 REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGTNDTVNAICDDE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 132 -FDYIFFTGSPRVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC---SQEM 207
Cdd:PLN02419 327 dIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSW 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 208 QERLVPALQnAITRFYGDNPQTspNLGRIINQKHFERLQGLLGCG-----RVAIGGQS-----DEGERYIAPTVLVDVQE 277
Cdd:PLN02419 407 EDKLVERAK-ALKVTCGSEPDA--DLGPVISKQAKERICRLIQSGvddgaKLLLDGRDivvpgYEKGNFIGPTILSGVTP 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 278 TEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQMLECTSSGSFGGNDGfLYLTLPALPLGGVG 357
Cdd:PLN02419 484 DMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVP-IPVPLPFFSFTGNK 562
|
330 340
....*....|....*....|
gi 1958654670 358 NSGMG--RYHGKFSFDTFSH 375
Cdd:PLN02419 563 ASFAGdlNFYGKAGVDFFTQ 582
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
55-310 |
3.17e-17 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 83.36 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPLNLMIMplvG-----AIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQS-----CFAVVLGGPEET 124
Cdd:cd07129 105 PLGPVAVFGASNFPLAFSVA---GgdtasALAAGCPVVVKAHPAHPGTSELVARAIRAALRATglpagVFSLLQGGGREV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 125 GQ-LLKH-KFDYIFFTGSPRVGKIVMAAAAKHLTPIT--LELGGKNPCYVddncDPQTVANR--------VAWFRyFNAG 192
Cdd:cd07129 182 GVaLVKHpAIKAVGFTGSRRGGRALFDAAAARPEPIPfyAELGSVNPVFI----LPGALAERgeaiaqgfVGSLT-LGAG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 193 QTCVAPDYVLCSQ-EMQERLVPALQNAITRFygdNPQT--SPNLgriinQKHF----ERLQGLLGcGRVAIGGQSDEGER 265
Cdd:cd07129 257 QFCTNPGLVLVPAgPAGDAFIAALAEALAAA---PAQTmlTPGI-----AEAYrqgvEALAAAPG-VRVLAGGAAAEGGN 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958654670 266 YIAPTVL-VDVQE--TEPVMQEEIFGPILPLVTVRSLDEAVNFINQRE 310
Cdd:cd07129 328 QAAPTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
54-307 |
3.62e-17 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 84.15 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEmskNTEKVLAEllpqyldqscfAVVL----GGPEETGQLLK 129
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE---QTPLIAAR-----------AVRLlheaGVPKDALQLLP 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 130 HKFDYI-------------FFTGSPRVGKIVMAAAAKHLTPITL---ELGGKNPCYVDDNCDP-QTVANRVA-WFRyfNA 191
Cdd:PRK11905 741 GDGRTVgaalvadpriagvMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPeQVVADVIAsAFD--SA 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 192 GQTCVAPDyVLCSQE-MQERLVPALQNAITRFYGDNP-QTSPNLGRIINQK-------HFERLQGLlGCG--RVAIGGQS 260
Cdd:PRK11905 819 GQRCSALR-VLCLQEdVADRVLTMLKGAMDELRIGDPwRLSTDVGPVIDAEaqanieaHIEAMRAA-GRLvhQLPLPAET 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958654670 261 DEGeRYIAPTVLvdvqETE--PVMQEEIFGPILPLVTVRS--LDEAVNFIN 307
Cdd:PRK11905 897 EKG-TFVAPTLI----EIDsiSDLEREVFGPVLHVVRFKAdeLDRVIDDIN 942
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
45-366 |
4.12e-17 |
|
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: 82.67 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 45 KFSSAFIRKePFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQ--YLDQSCFAVVLGGPE 122
Cdd:cd07084 91 KQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 123 ETGQLLKH-KFDYIFFTGSPRVGKIVMAAAakHLTPITLELGGKNPCYVDDNCDP-QTVANRVAWFRYFNAGQTCVAPDY 200
Cdd:cd07084 170 TMQALLLHpNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSGQKCTAQSM 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 201 VLCSQEMQ-ERLVPALQNAITRfygDNPQTSpNLGRIINQKHFERLQGLLG-CGRVAIGGQSDEGERYI--------APT 270
Cdd:cd07084 248 LFVPENWSkTPLVEKLKALLAR---RKLEDL-LLGPVQTFTTLAMIAHMENlLGSVLLFSGKELKNHSIpsiygacvASA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 271 VLVDVQE---TEPVMQEEIFGPILPLVTVRSLDEA--VNFINQREKPLALYAFSNNGQVVTQMLECTSSGsfggndGFLY 345
Cdd:cd07084 324 LFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVA------GRTY 397
|
330 340
....*....|....*....|.
gi 1958654670 346 LTLPalplgGVGNSGMGRYHG 366
Cdd:cd07084 398 AILR-----GRTGVAPNQNHG 413
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
55-307 |
4.90e-14 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 74.24 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEmskNTEKVLAEllpqyldqscfAVVL----GGPEETGQLL-- 128
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAE---QTPLIAAQ-----------AVRIlleaGVPAGVVQLLpg 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 129 -----------KHKFDYIFFTGSPRVGKIVMAAAAKHL------TPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 191
Cdd:PRK11809 834 rgetvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 192 GQTCVAPDyVLCSQE-MQERLVPALQNAITRFYGDNP-QTSPNLGRIIN-------QKHFERLQGllgCGRV---AIGGQ 259
Cdd:PRK11809 914 GQRCSALR-VLCLQDdVADRTLKMLRGAMAECRMGNPdRLSTDIGPVIDaeakaniERHIQAMRA---KGRPvfqAAREN 989
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958654670 260 SDEGER--YIAPTV--LVDVQEtepvMQEEIFGPILPLVTVRS--LDEAVNFIN 307
Cdd:PRK11809 990 SEDWQSgtFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIEQIN 1039
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
51-308 |
1.21e-13 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 72.92 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 51 IRKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEmskNTEKVLAE---LLPQY-LDQSCFAVVLGGPEETGQ 126
Cdd:PRK11904 680 LRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE---QTPLIAAEavkLLHEAgIPKDVLQLLPGDGATVGA 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 127 -LLKH-KFDYIFFTGSPRVGKIV-MAAAAKHLTPITL--ELGGKNPCYVDDNCDPQTVANRV---AwFRyfNAGQTCVAP 198
Cdd:PRK11904 757 aLTADpRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVvtsA-FR--SAGQRCSAL 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 199 DyVLCSQE-MQERLVPALQNA-----ItrfyGDNPQTSPNLGRIINQ-------KHFERLQ--GLLGCgRVAIGGQSDEG 263
Cdd:PRK11904 834 R-VLFVQEdIADRVIEMLKGAmaelkV----GDPRLLSTDVGPVIDAeakanldAHIERMKreARLLA-QLPLPAGTENG 907
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958654670 264 ErYIAPTvLVDVQETEpVMQEEIFGPILPLVTVRS--LDEAVNFINQ 308
Cdd:PRK11904 908 H-FVAPT-AFEIDSIS-QLEREVFGPILHVIRYKAsdLDKVIDAINA 951
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
57-291 |
1.10e-12 |
|
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: 69.54 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 57 GLVLIIAPWNYP---LNLMIMPlvgAIAaGNCVVLKPSEM----SKNTEKVLAEL-LP----QYL--DQSCF-AVVLGGP 121
Cdd:cd07123 172 GFVYAVSPFNFTaigGNLAGAP---ALM-GNVVLWKPSDTavlsNYLVYKILEEAgLPpgviNFVpgDGPVVgDTVLASP 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 122 EETGqllkhkfdyIFFTGSPRVGKIVMAAAAKHLT-----P-ITLELGGKNPCYVDDNCDPQTVAN---RVAwFRYfnAG 192
Cdd:cd07123 248 HLAG---------LHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTatvRGA-FEY--QG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 193 QTCVAPD--YVLCS--QEMQERLVPALQnAITrfYGDNPQTSPNLGRIINQKHFERLQGLLGCGR------VAIGGQSDE 262
Cdd:cd07123 316 QKCSAASraYVPESlwPEVKERLLEELK-EIK--MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCDD 392
|
250 260 270
....*....|....*....|....*....|
gi 1958654670 263 GERY-IAPTVLVDVQETEPVMQEEIFGPIL 291
Cdd:cd07123 393 SVGYfVEPTVIETTDPKHKLMTEEIFGPVL 422
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
55-330 |
6.21e-12 |
|
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: 67.12 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIA-----PWN-YPlnlmimPLVGAIAAGNCVVLKPSEMS--------KNTEKVLAELlpqYLDQSCFAVVLGG 120
Cdd:cd07127 193 PRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPHPAAilplaitvQVAREVLAEA---GFDPNLVTLAADT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 121 PEE--TGQLLKH-KFDYIFFTGSPRVGKIVMAAAAKHLtpITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 197
Cdd:cd07127 264 PEEpiAQTLATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 198 PDYVLCS----QEMQERLVP-----ALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAIGGQSDE-----G 263
Cdd:cd07127 342 PQNIYVPrdgiQTDDGRKSFdevaaDLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAhpefpD 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 264 ERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQ--REK-PLALYAFSNNGQVVTQMLE 330
Cdd:cd07127 422 ARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERVQE 491
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
54-307 |
4.29e-10 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 61.88 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEmskNT-----------------EKVLAeLLPqyldqscfav 116
Cdd:COG4230 679 RGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAE---QTpliaaravrllheagvpADVLQ-LLP---------- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 117 vlGGPEETG-QLLKHK-FDYIFFTGSPRVGKIV-MAAAAKHLTPITL--ELGGKNPCYVDDNCDPQTVANRV---AwFRy 188
Cdd:COG4230 745 --GDGETVGaALVADPrIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVlasA-FD- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 189 fNAGQTCVAPDyVLCSQE-----MQERLVPALQN-AItrfyGDNPQTSPNLGRIIN-------QKHFERLQ--GLLgCGR 253
Cdd:COG4230 821 -SAGQRCSALR-VLCVQEdiadrVLEMLKGAMAElRV----GDPADLSTDVGPVIDaearanlEAHIERMRaeGRL-VHQ 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958654670 254 VAIGGQSDEGeRYIAPTV--LVDVQEtepvMQEEIFGPILPLVTVRS--LDEAVNFIN 307
Cdd:COG4230 894 LPLPEECANG-TFVAPTLieIDSISD----LEREVFGPVLHVVRYKAdeLDKVIDAIN 946
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
55-304 |
8.67e-09 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 57.25 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 55 PFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYLDQSC----FAVVLGGP--EETGQLL 128
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGgpdnLVVTVEEPtiETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 129 KH-KFDYIFFTGSPRVGKIVMAAAAKhltpiTLELGGKNP-CYVDDNCDPQTVANRVAWFRYFNAGQTC----------- 195
Cdd:cd07121 177 AHpDINLLVVTGGPAVVKAALSSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVQGASFDNNLPCiaekeviavds 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 196 VAPD----------YVLCSQEMQERLVPALQNaitrfygdnpqtspNLGRIINQKHFER-LQGLLGcgrvAIGGQSDEGE 264
Cdd:cd07121 252 VADYliaamqrngaYVLNDEQAEQLLEVVLLT--------------NKGATPNKKWVGKdASKILK----AAGIEVPADI 313
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958654670 265 RYIaptvLVDVQETEPVMQEEIFGPILPLVTVRSLDEAVN 304
Cdd:cd07121 314 RLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
54-303 |
2.58e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 52.65 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 54 EPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQYldqscfAVVLGGPE----------- 122
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQA------AVAAGAPEnligwidnpsi 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 123 ETGQLLKHK--FDYIFFTGSPRVGKivmaAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGqtcvapdy 200
Cdd:cd07081 168 ELAQRLMKFpgIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNG-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 201 VLCSQEMQERLVPALQNAITRFYGDNPqtspnlGRIINQKHFERLQGLL---GCGRVAIGGQS-------------DEGE 264
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEGQG------AYKLTAEELQQVQPVIlknGDVNRDIVGQDaykiaaaaglkvpQETR 309
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958654670 265 RYIAPTVLVDvqETEPVMQEEIfGPILPLVTVRSLDEAV 303
Cdd:cd07081 310 ILIGEVTSLA--EHEPFAHEKL-SPVLAMYRAANFADAD 345
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
37-289 |
1.41e-05 |
|
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: 47.11 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 37 SVSTNFLTKFSSAFirKEPFGLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLK-PSEMSKNTEKVLAEL----LPQyldQ 111
Cdd:cd07126 126 NVPGDHQGQQSSGY--RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKvDSKVSVVMEQFLRLLhlcgMPA---T 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 112 SCFAVVLGGPEETGQLLKHKFDYIFFTGSPRV---------GKIVMAAAA---KHLTPITLELGgknpcYVDDNCDPQTv 179
Cdd:cd07126 201 DVDLIHSDGPTMNKILLEANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 180 anrvawfrYFNAGQTCVAPDyVLCSQE--MQERLVPALQNAITRFYGDNPQTSPNLG----RIINqkHFERLQGLLGcGR 253
Cdd:cd07126 275 --------YACSGQKCSAQS-ILFAHEnwVQAGILDKLKALAEQRKLEDLTIGPVLTwtteRILD--HVDKLLAIPG-AK 342
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958654670 254 VAIGGQSDEGERYIA------PT-VLVDVQ-----ETEPVMQEEIFGP 289
Cdd:cd07126 343 VLFGGKPLTNHSIPSiygayePTaVFVPLEeiaieENFELVTTEVFGP 390
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
57-386 |
1.89e-05 |
|
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: 46.88 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 57 GLVLIIAPWNYPLNLMIMPLVGAIAAGNCVVLKP-SEMSKNTEKVLAE-----LLPQyldqSCFAVVLGGpeeTGQLLKH 130
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPaTATAYLTEAVVKDivesgLLPE----GALQLICGS---VGDLLDH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 131 --KFDYIFFTGSPRVGKI--VMAAAAKHLTPITLELGGKNPCYVDDNCDPQT-----VANRVAWFRYFNAGQTCVAPDYV 201
Cdd:cd07128 219 lgEQDVVAFTGSAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDATPGTpefdlFVKEVAREMTVKAGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 202 LCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQG----LLGCGRVAIGGQSD--------EGERYIA 268
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVvVGDPRLEGVRMGPLVSREQREDVRAavatLLAEAEVVFGGPDRfevvgadaEKGAFFP 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 269 PTVLV--DVQETEPVMQEEIFGPILPLVTVRSLDEAVNFINQREKPLALYAFSNNGQVVTQML----------------- 329
Cdd:cd07128 379 PTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVlgaapyhgrllvlnrds 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958654670 330 --ECTSSGSfggndgflylTLPALPLGGVGNSGMGRYHGKFSFDTFSHQRACLLSSPGM 386
Cdd:cd07128 459 akESTGHGS----------PLPQLVHGGPGRAGGGEELGGLRGVKHYMQRTAVQGSPTM 507
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
50-183 |
9.88e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, 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. This group includes families ALDH18, ALDH19, and ALDH20 and represents 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: 143396 [Multi-domain] Cd Length: 397 Bit Score: 44.14 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 50 FIRKEPFGLVLIIAPWNYPLnLMIMPLVGAIAAGNCVVLKPSEMSKNTEKVLAELLPQyldqscfAVVLGGP-------- 121
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQA-------ADAAHGPkilvlyvp 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654670 122 ----EETGQLLKH-KFDYIFFTGSPRVGKivmaAAAKHLTPITLeLG---GKNPCYVDDNCDPQTVANRV 183
Cdd:cd07077 167 hpsdELAEELLSHpKIDLIVATGGRDAVD----AAVKHSPHIPV-IGfgaGNSPVVVDETADEERASGSV 231
|
|
| |
