|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
5-447 |
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: 853.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKD 84
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFA 164
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTC 244
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 245 VAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGCGRVAIGGQSEESDRYIAPTVLVDV 324
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 325 QETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILTSLPFGG 404
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 946758581 405 VGASGMGSYHGKFSFDTFSHHRACLLRGPGMEKIYSIRYPPYS 447
Cdd:cd07132 401 VGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-429 |
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: 702.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKD 84
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFA 164
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTC 244
Cdd:cd07087 161 VVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 245 VAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGCGRVAIGGQSEESDRYIAPTVLVDV 324
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 325 QETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILTSLPFGG 404
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
410 420
....*....|....*....|....*
gi 946758581 405 VGASGMGSYHGKFSFDTFSHHRACL 429
Cdd:cd07087 401 VGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-454 |
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: 644.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKD 84
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFA 164
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTC 244
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 245 VAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGCGRVAIGGQSEESDRYIAPTVLVDV 324
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 325 QETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILTSLPFGG 404
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 946758581 405 VGASGMGSYHGKFSFDTFSHHRACLLRGPGMEkiYSIRYPPYSPRNLRML 454
Cdd:cd07136 401 VGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYKGKKKKLK 448
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
2-459 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 618.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 2 DPFEDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAW 81
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 82 MKDETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRS 161
Cdd:PTZ00381 87 LKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 162 CFAVVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAG 241
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 242 QTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGC--GRVAIGGQSEESDRYIAPT 319
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 320 VLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILTS 399
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 400 LPFGGVGASGMGSYHGKFSFDTFSHHRACLLRGPGMEKIYSIRYPPYSPRNLRMLLVAME 459
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLK 466
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
1-427 |
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: 597.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 1 MDPFEDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRA 80
Cdd:cd07135 4 LDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 81 WMKDETVPKNLATQ-LDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLD 159
Cdd:cd07135 84 WAKDEKVKDGPLAFmFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 160 RSCFAVVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFN 239
Cdd:cd07135 164 PDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 240 AGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGC--GRVAIGGQSEESDRYIA 317
Cdd:cd07135 244 AGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 318 PTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLIL 397
Cdd:cd07135 324 PTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGV 403
|
410 420 430
....*....|....*....|....*....|
gi 946758581 398 TSLPFGGVGASGMGSYHGKFSFDTFSHHRA 427
Cdd:cd07135 404 DNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
5-429 |
0e+00 |
|
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: 525.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKD 84
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFA 164
Cdd:cd07137 82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRY-FNAGQT 243
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 244 CVAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGCGRVAI----GGQSEESDRYIAPT 319
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 320 VLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILTS 399
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
410 420 430
....*....|....*....|....*....|
gi 946758581 400 LPFGGVGASGMGSYHGKFSFDTFSHHRACL 429
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
9-429 |
0e+00 |
|
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: 522.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 9 QRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKDETVP 88
Cdd:cd07134 5 AAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 89 KNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFAVVLG 168
Cdd:cd07134 85 TPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 169 GPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPD 248
Cdd:cd07134 165 DAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 249 YILCSPEMQERLVPALQSAITRFYGEDP--RASPDLGRIVSEKHFQRLRGLL-----GCGRVAIGGQSEESDRYIAPTVL 321
Cdd:cd07134 245 YVFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIAPTVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 322 VDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILTSLP 401
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLP 404
|
410 420
....*....|....*....|....*...
gi 946758581 402 FGGVGASGMGSYHGKFSFDTFSHHRACL 429
Cdd:cd07134 405 FGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
5-427 |
8.49e-176 |
|
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: 499.70 E-value: 8.49e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDL-RKSAFESEVSEISISQGEINLALRNLRAWMK 83
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 84 DETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCF 163
Cdd:cd07133 81 PSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVVLGGpAETGQLLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQ 242
Cdd:cd07133 161 AVVTGG-ADVAAAFSSlPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 243 TCVAPDYILCSPEMQERLVPALQSAITRFYGeDPRASPDLGRIVSEKHFQRLRGLL------GCGRVAIGGQSEE--SDR 314
Cdd:cd07133 240 TCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLedarakGARVIELNPAGEDfaATR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMH 394
Cdd:cd07133 319 KLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLH 398
|
410 420 430
....*....|....*....|....*....|...
gi 946758581 395 LILTSLPFGGVGASGMGSYHGKFSFDTFSHHRA 427
Cdd:cd07133 399 VAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-454 |
1.86e-164 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 473.06 E-value: 1.86e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 1 MDPFEDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRA 80
Cdd:PLN02203 5 GETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 81 WMKDETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDR 160
Cdd:PLN02203 85 WMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 161 SCFAVVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVD---DNCDAQTVANRVAFFRY 237
Cdd:PLN02203 165 KAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 238 FN-AGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGCGRVAI----GGQSEES 312
Cdd:PLN02203 245 GScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSIDEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 313 DRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGF 392
Cdd:PLN02203 325 KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 946758581 393 MHLILTSLPFGGVGASGMGSYHGKFSFDTFSHHRACLLRGPGMEkiYSIRYPPYSPRNLRML 454
Cdd:PLN02203 405 IQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPPWNDFKLGFL 464
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
5-430 |
1.13e-135 |
|
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: 397.73 E-value: 1.13e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVsEISISQGEINLALRNLRAWMKD 84
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCF 163
Cdd:cd07078 80 VIPSPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVVLGGPAETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAG 241
Cdd:cd07078 157 NVVTGDGDEVGAaLASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 242 QTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEKHFQRLRGLL-----GCGRVAIGGQSEESD-- 313
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDpDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGkg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 314 RYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFM 393
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 946758581 394 HLILtSLPFGGVGASGMGSYHGKFSFDTFSHHRACLL 430
Cdd:cd07078 397 GAEP-SAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
11-454 |
1.58e-128 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 381.32 E-value: 1.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 11 LREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKDETVPKN 90
Cdd:PLN02174 19 LRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 91 LATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFAVVLGGP 170
Cdd:PLN02174 99 LTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 171 AETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRY-FNAGQTCVAPDY 249
Cdd:PLN02174 179 TETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 250 ILCSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLG----CGRVAIGGQSEESDRYIAPTVLVDVQ 325
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 326 ETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILTSLPFGGV 405
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGV 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 946758581 406 GASGMGSYHGKFSFDTFSHHRACLLRGPGMEKiySIRYPPYSPRNLRML 454
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAVLYRSLFGDS--AVRYPPYSRGKLRLL 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
12-430 |
5.06e-109 |
|
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: 327.26 E-value: 5.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESeVSEISISQGEINLALRNLRAWMKDETVPKNL 91
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 92 ATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLGGP 170
Cdd:cd06534 83 GGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 171 AETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPD 248
Cdd:cd06534 160 DEVGAaLLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 249 YILCSPEMQERLVPALQsaitrfygedpraspdlgrivsekhfqrlrgllgcgrvaiggqseesdryiapTVLVDVQETE 328
Cdd:cd06534 240 RLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDPDM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 329 PVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILtSLPFGGVGAS 408
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP-EAPFGGVKNS 345
|
410 420
....*....|....*....|..
gi 946758581 409 GMGSYHGKFSFDTFSHHRACLL 430
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
12-424 |
1.64e-104 |
|
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: 319.38 E-value: 1.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESevseisisQGEINLALRNLRAW------MKDE 85
Cdd:COG1012 53 RAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA--------RGEVDRAADFLRYYagearrLYGE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 86 TVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFA 164
Cdd:COG1012 125 TIPSDAPGTR--AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQ 242
Cdd:COG1012 203 VVTGDGSEVGAaLVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 243 TCVAPDYILCSPEMQERLVPALQSAITRF-YGeDPR-ASPDLGRIVSEKHFQRLRGLLGCG-----RVAIGGQ--SEESD 313
Cdd:COG1012 283 RCTAASRLLVHESIYDEFVERLVAAAKALkVG-DPLdPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRrpDGEGG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 314 RYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFM 393
Cdd:COG1012 362 YFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTT 441
|
410 420 430
....*....|....*....|....*....|.
gi 946758581 394 HLILTsLPFGGVGASGMGSYHGKFSFDTFSH 424
Cdd:COG1012 442 GAVPQ-APFGGVKQSGIGREGGREGLEEYTE 471
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-423 |
3.37e-92 |
|
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: 287.12 E-value: 3.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSafesevseISISQGEINLALRNLRAW------MKDE 85
Cdd:pfam00171 39 RAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP--------LAEARGEVDRAIDVLRYYaglarrLDGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 86 TVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFA 164
Cdd:pfam00171 111 TLPSDPGRL---AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQ 242
Cdd:pfam00171 188 VVTGSGAEVGEaLVEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 243 TCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEKHFQRLRGLL-----GCGRVAIGGQSEESD-RY 315
Cdd:pfam00171 268 VCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDpDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 316 IAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHL 395
Cdd:pfam00171 348 VEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGD 427
|
410 420
....*....|....*....|....*...
gi 946758581 396 ILTsLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:pfam00171 428 ADG-LPFGGFKQSGFGREGGPYGLEEYT 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-427 |
1.86e-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: 269.48 E-value: 1.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 6 DTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVseisisqgEINLALRNLRAW---- 81
Cdd:cd07099 22 AAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL--------EVLLALEAIDWAarna 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 82 ---MKDETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY- 157
Cdd:cd07099 94 prvLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 158 LDRSCFAVVLGGpAETGQ-LLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFR 236
Cdd:cd07099 174 PPQGVLQVVTGD-GATGAaLIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 237 YFNAGQTCVAPDYILCSPEMQERLVPALQSAITRF-YGEDPRASPDLGRIVSEKHFQRLRG-----LLGCGRVAIGGQSE 310
Cdd:cd07099 253 MVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRhvddaVAKGAKALTGGARS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 311 ESD-RYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGN 389
Cdd:cd07099 333 NGGgPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSIN 412
|
410 420 430
....*....|....*....|....*....|....*...
gi 946758581 390 DGFMHLILTSLPFGGVGASGMGSYHGKFSFDTFSHHRA 427
Cdd:cd07099 413 DVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
30-416 |
4.86e-70 |
|
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: 229.88 E-value: 4.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 30 LKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKDETVPKNLATQLDSAFIRKEPFGLVL 109
Cdd:cd07098 46 LRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 110 IIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLpryldRSCFAV---------VLGGPAETGQ-LLEH 179
Cdd:cd07098 126 AIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSII-----RECLAAcghdpdlvqLVTCLPETAEaLTSH 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 180 -KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQE 258
Cdd:cd07098 201 pVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 259 RLVPALQSAITRF---YGEDprASPDLGRIVSEKHFQRLRGLLG----------CGRVAIGGQSEESDRYIAPTVLVDVQ 325
Cdd:cd07098 281 KLLEILTDRVQALrqgPPLD--GDVDVGAMISPARFDRLEELVAdavekgarllAGGKRYPHPEYPQGHYFPPTLLVDVT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 326 ETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGND-GFMHLILtSLPFGG 404
Cdd:cd07098 359 PDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDfGVNYYVQ-QLPFGG 437
|
410
....*....|..
gi 946758581 405 VGASGMGSYHGK 416
Cdd:cd07098 438 VKGSGFGRFAGE 449
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
12-423 |
3.69e-69 |
|
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: 227.21 E-value: 3.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGR-TRPAEfRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINL---ALRNLRAWMKDETV 87
Cdd:cd07092 29 HAAFPSWRrTTPAE-RSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFfagAARTLEGPAAGEYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 88 PKNlatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFAVVL 167
Cdd:cd07092 108 PGH------TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 168 GGPAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCV 245
Cdd:cd07092 182 GGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 246 APDYILCSPEMQERLVPALQSAITRF-YGEDPRASPDLGRIVSEKHFQRLRGLL----GCGRVAIGGQSEESDRY-IAPT 319
Cdd:cd07092 262 AACRVYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 320 VLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfmHLILTS 399
Cdd:cd07092 342 VVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAA 418
|
410 420
....*....|....*....|....*
gi 946758581 400 -LPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07092 419 eMPHGGFKQSGYGKDLSIYALEDYT 443
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
12-423 |
1.87e-64 |
|
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: 214.89 E-value: 1.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTR--PAEFRAAQLKGLGRFLQDNkqllQEALAqdlRKSAFESEvSEISISQGEINLALRNLRawmkdetVPK 89
Cdd:cd07118 29 RKAFDKGPWPrmSGAERAAVLLKVADLIRAR----RERLA---LIETLESG-KPISQARGEIEGAADLWR-------YAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 90 NLATQL--DS---------AFIRKEPFGLVLIIAPWNYPLnLTL---VPLvgALAAGNCVVLKPSEISKNTERVLVEVLP 155
Cdd:cd07118 94 SLARTLhgDSynnlgddmlGLVLREPIGVVGIITPWNFPF-LILsqkLPF--ALAAGCTVVVKPSEFTSGTTLMLAELLI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 156 RY-LDRSCFAVVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRV 232
Cdd:cd07118 171 EAgLPAGVVNIVTGYGATVGQaMTEHPdVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 233 AFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLLGCGR-----VAIG 306
Cdd:cd07118 251 VFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPlDPETKVGAIINEAQLAKITDYVDAGRaegatLLLG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 307 GQ--SEESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSG 384
Cdd:cd07118 331 GErlASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAG 410
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 946758581 385 GFCGN---DGFmhlilTSLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07118 411 TVWVNtflDGS-----PELPFGGFKQSGIGRELGRYGVEEYT 447
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
12-427 |
2.49e-64 |
|
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: 214.80 E-value: 2.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSG-RTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKDETVP-K 89
Cdd:cd07089 29 RRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWEFDLPvP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRyldrSCFA 164
Cdd:cd07089 109 ALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaetdLPA----GVVN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQ 242
Cdd:cd07089 185 VVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 243 TCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRAsPD--LGRIVSEKHFQRLRGLLGCGR------VAIGGQSEESDR 314
Cdd:cd07089 265 GCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPAD-PGtvMGPLISAAQRDRVEGYIARGRdegarlVTGGGRPAGLDK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 --YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNdGF 392
Cdd:cd07089 344 gfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-GG 422
|
410 420 430
....*....|....*....|....*....|....*
gi 946758581 393 MHLiLTSLPFGGVGASGMGSYHGKFSFDTFSHHRA 427
Cdd:cd07089 423 GGY-GPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
5-424 |
2.82e-64 |
|
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: 213.55 E-value: 2.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQD----LRKSAFESEVSeISISQGEINLALRnlra 80
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIREsgstRPKAAFEVGAA-IAILREAAGLPRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 81 wMKDETVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLV-EV-----L 154
Cdd:cd07104 78 -PEGEILPSDVPGKE--SMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIfeeagL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 155 PRYLdrscFAVVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRV 232
Cdd:cd07104 155 PKGV----LNVVPGGGSEIGDaLVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 233 AFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRF-YGeDPRaSPD--LGRIVSEKHFQRLRGLL------GcGRV 303
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVG-DPR-DPDtvIGPLINERQVDRVHAIVedavaaG-ARL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 304 AIGGQSEesDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSS 383
Cdd:cd07104 308 LTGGTYE--GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLET 385
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 946758581 384 GGFCGNDGFMHlILTSLPFGGVGASGMGSYHGKFSFDTFSH 424
Cdd:cd07104 386 GMVHINDQTVN-DEPHVPFGGVKASGGGRFGGPASLEEFTE 425
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
12-424 |
5.66e-64 |
|
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: 213.75 E-value: 5.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVS--------EISISQGEinlALRNlrawMK 83
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDvddvagcfEYYADLAE---QLDA----KA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 84 DETVPknLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRyl 158
Cdd:cd07110 102 ERAVP--LPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPP-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 159 drSCFAVVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFR 236
Cdd:cd07110 178 --GVLNVVTGTGDEAGApLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 237 YFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRASP-DLGRIVSEKHFQRLRGLLGCG-----RVAIGGQSE 310
Cdd:cd07110 256 FWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARGkeegaRLLCGGRRP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 311 ESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFC 387
Cdd:cd07110 336 AHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVW 415
|
410 420 430
....*....|....*....|....*....|....*..
gi 946758581 388 GNDGfmHLILTSLPFGGVGASGMGSYHGKFSFDTFSH 424
Cdd:cd07110 416 INCS--QPCFPQAPWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
12-416 |
2.17e-63 |
|
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: 212.00 E-value: 2.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESevseisisQGEINLALrnlrAWMK-------- 83
Cdd:cd07106 29 KAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA--------QFEVGGAV----AWLRytasldlp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 84 DETVPKNlATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCF 163
Cdd:cd07106 97 DEVIEDD-DTR--RVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVVLGGpAETGQLL-EH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAG 241
Cdd:cd07106 174 NVVSGG-DELGPALtSHpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 242 QTCVAPD--YIlcsPEMQ-ERLVPALQSAITRFY---GEDPRAspDLGRIVSEKHFQRLRGLL-----GCGRVAIGGQSE 310
Cdd:cd07106 253 QVCAAIKrlYV---HESIyDEFCEALVALAKAAVvgdGLDPGT--TLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 311 ESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGN 389
Cdd:cd07106 328 DGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN 407
|
410 420
....*....|....*....|....*...
gi 946758581 390 dgfMHLILT-SLPFGGVGASGMGSYHGK 416
Cdd:cd07106 408 ---THGALDpDAPFGGHKQSGIGVEFGI 432
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
12-423 |
1.25e-62 |
|
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: 210.17 E-value: 1.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSG--RTRPAEfRAAQLKGLGRFLQDNKQLLQEALAQDLRKSafesevseISISQGEINLALRNLR--AWMKD--- 84
Cdd:cd07109 29 RRAFESGwlRLSPAE-RGRLLLRIARLIREHADELARLESLDTGKP--------LTQARADVEAAARYFEyyGGAADklh 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 -ETVP--KNLAtqldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDR 160
Cdd:cd07109 100 gETIPlgPGYF-----VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 161 SCFAVVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYF 238
Cdd:cd07109 175 GALNVVTGLGAEAGAaLVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 239 NAGQTCVAPDYILCSPEMQERLVPALQS---AITRFYGEDpraSPDLGRIVSEKHFQRLRGLL-----GCGRVAIGGQSE 310
Cdd:cd07109 255 NAGQTCSAGSRLLVHRSIYDEVLERLVErfrALRVGPGLE---DPDLGPLISAKQLDRVEGFVararaRGARIVAGGRIA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 311 ESDR----YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGF 386
Cdd:cd07109 332 EGAPaggyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQV 411
|
410 420 430
....*....|....*....|....*....|....*..
gi 946758581 387 CGNDGFMHLILtSLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07109 412 FVNNYGAGGGI-ELPFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
13-422 |
9.50e-62 |
|
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: 207.67 E-value: 9.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 13 EAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSafeseVSEisiSQGEINLALRNLRaWMKDE------- 85
Cdd:cd07103 30 AAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKP-----LAE---ARGEVDYAASFLE-WFAEEarriygr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 86 TVPKNLATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFA 164
Cdd:cd07103 101 TIPSPAPGK--RILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQ-LLEH----KfdyIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFN 239
Cdd:cd07103 179 VVTGSPAEIGEaLCASprvrK---ISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 240 AGQTCVAPDYILCSPEMQERLVPALQSAITRF---YGEDPraSPDLGRIVSEKHFQRLRGL----LGCG-RVAIGGQ-SE 310
Cdd:cd07103 256 AGQTCVCANRIYVHESIYDEFVEKLVERVKKLkvgNGLDE--GTDMGPLINERAVEKVEALvedaVAKGaKVLTGGKrLG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 311 ESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSG--GFcg 388
Cdd:cd07103 334 LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGmvGI-- 411
|
410 420 430
....*....|....*....|....*....|....
gi 946758581 389 NDGFMHliLTSLPFGGVGASGMGSYHGKFSFDTF 422
Cdd:cd07103 412 NTGLIS--DAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-422 |
2.30e-61 |
|
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: 206.97 E-value: 2.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSS-GRTRPAEfRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWmkdetvpkN 90
Cdd:cd07138 46 RRAFPAwSATSVEE-RAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDF--------E 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 91 LATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPryldRSCFAV 165
Cdd:cd07138 117 FEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEIldeagLP----AGVFNL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 166 VLGGPAETGQLL-EH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQT 243
Cdd:cd07138 193 VNGDGPVVGEALsAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 244 CVAPDYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGLLGCG-----RVAIGG----QSEESD 313
Cdd:cd07138 273 CNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRdPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGGpgrpEGLERG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 314 RYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFM 393
Cdd:cd07138 353 YFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAF 432
|
410 420
....*....|....*....|....*....
gi 946758581 394 HLiltSLPFGGVGASGMGSYHGKFSFDTF 422
Cdd:cd07138 433 NP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
100-412 |
3.55e-61 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 206.68 E-value: 3.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFAVVLGGPAETGQ-LLE 178
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDaLVG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 179 H-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQ 257
Cdd:PRK13473 214 HpKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 258 ERLVPALQSAITRF-YGEDPRASPDLGRIVSEKHFQRLRGL------LGCGRVAIGGQSEESD-RYIAPTVLVDVQETEP 329
Cdd:PRK13473 294 DDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFverakaLGHIRVVTGGEAPDGKgYYYEPTLLAGARQDDE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 330 VMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMhlILTSLPFGGVGASG 409
Cdd:PRK13473 374 IVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSG 451
|
...
gi 946758581 410 MGS 412
Cdd:PRK13473 452 YGK 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-425 |
4.71e-61 |
|
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: 205.94 E-value: 4.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 7 TLQRLREAFSSGRTRPAEFRAAQLKglgRFLqdnkqllqEALAQdlRKSAFESEVSE-----ISISQGEINLALRnlRAW 81
Cdd:cd07102 23 ALERARAAQKGWRAVPLEERKAIVT---RAV--------ELLAA--NTDEIAEELTWqmgrpIAQAGGEIRGMLE--RAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 82 MKDETVPKNLATQLDSA------FIRKEPFGLVLIIAPWNYPLnLTLV-PLVGALAAGNCVVLKPSEISKNT-ERV---L 150
Cdd:cd07102 88 YMISIAEEALADIRVPEkdgferYIRREPLGVVLIIAPWNYPY-LTAVnAVIPALLAGNAVILKHSPQTPLCgERFaaaF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 151 VEV-LPRYLdrscFAVVLGGPAETGQLL-EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTV 228
Cdd:cd07102 167 AEAgLPEGV----FQVLHLSHETSAALIaDPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 229 ANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQsAITRFY--GEDPRASPDLGRIVSEKHFQRLRGLL------Gc 300
Cdd:cd07102 243 AESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFV-AVVKGYklGDPLDPSTTLGPVVSARAADFVRAQIadaiakG- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 301 GRVAIGGQSEESDR----YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQ 376
Cdd:cd07102 321 ARALIDGALFPEDKaggaYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 946758581 377 VLARTSSGGFcgndgFMH---LILTSLPFGGVGASGMGSYHGKFSFDTF----SHH 425
Cdd:cd07102 401 LGEQLETGTV-----FMNrcdYLDPALAWTGVKDSGRGVTLSRLGYDQLtrpkSYH 451
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
69-423 |
5.29e-60 |
|
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: 202.94 E-value: 5.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 69 GEINLALRNLRAW------MKDETVPKNLATQLDSAFirKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEI 142
Cdd:cd07150 80 FETTFTPELLRAAagecrrVRGETLPSDSPGTVSMSV--RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 143 SKNTERVLVEVLPRY-LDRSCFAVVLGGPAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYV 219
Cdd:cd07150 158 TPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 220 DDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGLL 298
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRdPDTVIGPLISPRQVERIKRQV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 299 ------GcGRVAIGGqsEESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQ 372
Cdd:cd07150 318 edavakG-AKLLTGG--KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 946758581 373 VVKQvLARTSSGGFCG-NDGFMHlILTSLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07150 395 RAFK-LAERLESGMVHiNDPTIL-DEAHVPFGGVKASGFGREGGEWSMEEFT 444
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
12-411 |
2.79e-58 |
|
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: 198.74 E-value: 2.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKsAFESEvseisiSQGEINLALRNLRAW------MKDE 85
Cdd:cd07108 29 KAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGN-ALRTQ------ARPEAAVLADLFRYFgglageLKGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 86 TVPKNlATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFAV 165
Cdd:cd07108 102 TLPFG-PDVL--TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 166 VLGGPAETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYV--DDNCDaQTVANRVAFFRYFNAG 241
Cdd:cd07108 179 ITGYGEECGAaLVDHpDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 242 QTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGLLGCG------RVAIGGQSEESDR 314
Cdd:cd07108 258 QSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLdEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 -----YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGN 389
Cdd:cd07108 338 ladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVN 417
|
410 420
....*....|....*....|..
gi 946758581 390 DGfmHLILTSLPFGGVGASGMG 411
Cdd:cd07108 418 QG--GGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
12-423 |
3.39e-58 |
|
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: 198.56 E-value: 3.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISisqgeinLALRNLRAWmkdetvpKNL 91
Cdd:cd07093 29 KEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIP-------RAAANFRFF-------ADY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 92 ATQLDSAFI----------RKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPR 156
Cdd:cd07093 95 ILQLDGESYpqdggalnyvLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELaneagLPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 157 yldrSCFAVVLGGPAETGQLL-EHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAF 234
Cdd:cd07093 175 ----GVVNVVHGFGPEAGAALvAHPdVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 235 FRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGLLGCGR-----VAIGGQ 308
Cdd:cd07093 251 SSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLdPDTEVGPLISKEHLEKVLGYVELARaegatILTGGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 309 SEESDR-----YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSS 383
Cdd:cd07093 331 RPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 946758581 384 GGFCGNDGFM-HLiltSLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07093 411 GTVWVNCWLVrDL---RTPFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-423 |
3.50e-58 |
|
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: 199.07 E-value: 3.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSG--RTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEvseisISQGEINLALR---NLRAWMKDET 86
Cdd:cd07119 45 RRAFDSGewPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE-----IDIDDVANCFRyyaGLATKETGEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 87 VPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAV 165
Cdd:cd07119 120 YDVPPHVI---SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 166 VLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQT 243
Cdd:cd07119 197 VTGSGATVGAeLAESPdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 244 CVAPDYILCSPEMQERLVPAL---QSAITRFYGEDPRasPDLGRIVSEKHFQRLRGLLGCG-----RVAIGGQSEESDR- 314
Cdd:cd07119 277 CSAGSRLLVEESIHDKFVAALaerAKKIKLGNGLDAD--TEMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKRPTGDEl 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 ----YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGND 390
Cdd:cd07119 355 akgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND 434
|
410 420 430
....*....|....*....|....*....|...
gi 946758581 391 gfMHLILTSLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07119 435 --YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
5-411 |
6.54e-58 |
|
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: 197.66 E-value: 6.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVsEISISQGEINLALRNLRAwMKD 84
Cdd:cd07094 24 EEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-EVDRAIDTLRLAAEEAER-IRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPKNLATQLDS--AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVL-PRYLDRS 161
Cdd:cd07094 102 EEIPLDATQGSDNrlAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 162 CFAVVLGGPAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKhlTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFN 239
Cdd:cd07094 182 VLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 240 AGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRL-----RGLLGCGRVAIGGqsEESD 313
Cdd:cd07094 260 AGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVerwveEAVEAGARLLCGG--ERDG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 314 RYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGfM 393
Cdd:cd07094 338 ALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-S 416
|
410
....*....|....*...
gi 946758581 394 HLILTSLPFGGVGASGMG 411
Cdd:cd07094 417 AFRTDWMPFGGVKESGVG 434
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
12-423 |
3.63e-57 |
|
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: 195.90 E-value: 3.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSG---RTRPAEfraaqlkglgrflqdNKQLLQeALAQDLRKSAFESEVSE-------ISISQ-GEINLALRNLRa 80
Cdd:cd07112 34 RRAFESGvwsRLSPAE---------------RKAVLL-RLADLIEAHRDELALLEtldmgkpISDALaVDVPSAANTFR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 81 W-------MKDETVPknlaTQLDS-AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVE 152
Cdd:cd07112 97 WyaeaidkVYGEVAP----TGPDAlALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 153 V-----LPryldRSCFAVVLGGPAETGQLL-EHK-FDYIFFTGSPRVGKIVMAAAAK-HLTPVTLELGGKNPCYVDDNC- 223
Cdd:cd07112 173 LaleagLP----AGVLNVVPGFGHTAGEALgLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADAp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 224 DAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLLGCG- 301
Cdd:cd07112 249 DLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPlDPATRMGALVSEAHFDKVLGYIESGk 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 302 ----RVAIGGQS---EESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLA--LYT--FSNS 370
Cdd:cd07112 329 aegaRLVAGGKRvltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAasVWTsdLSRA 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 946758581 371 SQVVKQVLARTSSGGfCGNDGFMhliltSLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07112 409 HRVARRLRAGTVWVN-CFDEGDI-----TTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
96-423 |
4.24e-56 |
|
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: 192.41 E-value: 4.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 96 DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRyldrSCFAVVLGGP 170
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVfheagLPK----GVLNVVTHSP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 171 AE----TGQLLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCV 245
Cdd:cd07105 166 EDapevVEALIAHPaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICM 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 246 APDYILCSPEMQERLVPALQSAITRFYGedprASPDLGRIVSEKHFQRLRGL----LGCG-RVAIGGQSEESDR--YIAP 318
Cdd:cd07105 246 STERIIVHESIADEFVEKLKAAAEKLFA----GPVVLGSLVSAAAADRVKELvddaLSKGaKLVVGGLADESPSgtSMPP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 319 TVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHlILT 398
Cdd:cd07105 322 TILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH-DEP 400
|
330 340
....*....|....*....|....*
gi 946758581 399 SLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07105 401 TLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-370 |
1.12e-54 |
|
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: 189.40 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVsEISISQGEINLALRNLRAwMKDETVPKNL 91
Cdd:cd07088 45 EAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARR-IEGEIIPSDR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 92 ATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRYLdrscFAVV 166
Cdd:cd07088 123 PNE--NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagLPAGV----LNIV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 167 LGGPAETGQLL-EH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTC 244
Cdd:cd07088 197 TGRGSVVGDALvAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVC 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 245 VAPD--YILCS--PEMQERLVPALQSAItrfYGEDPRASPDLGRIVSEKHFQRLRGLL------GcGRVAIGGQSEESDR 314
Cdd:cd07088 277 TCAErvYVHEDiyDEFMEKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVEEMVeraveaG-ATLLTGGKRPEGEK 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 946758581 315 --YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNS 370
Cdd:cd07088 353 gyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTEN 410
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-427 |
1.41e-54 |
|
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: 188.80 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLGGPAETGQ-L 176
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAaL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 177 LEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPE 255
Cdd:cd07115 192 VEHPdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 256 MQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLLGCG-----RVAIGGQSE-ESDRYIAPTVLVDVQETE 328
Cdd:cd07115 272 IYDEFLERFTSLARSLRPGDPlDPKTQMGPLVSQAQFDRVLDYVDVGreegaRLLTGGKRPgARGFFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 329 PVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfMHLILTSLPFGGVGAS 408
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT--YNRFDPGSPFGGYKQS 429
|
330
....*....|....*....
gi 946758581 409 GMGSYHGKFSFDTFSHHRA 427
Cdd:cd07115 430 GFGREMGREALDEYTEVKS 448
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
12-411 |
1.38e-53 |
|
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: 186.01 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSafesevseISISQGEINLALRNLRAW------MKDE 85
Cdd:cd07145 31 EKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKP--------IKQSRVEVERTIRLFKLAaeeakvLRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 86 TVPKNLATQLDS--AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSC 162
Cdd:cd07145 103 TIPVDAYEYNERriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 163 FAVVLGGPAETG-QLLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNA 240
Cdd:cd07145 183 INVVTGYGSEVGdEIVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 241 GQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLL------GcGRVAIGGQSEESD 313
Cdd:cd07145 263 GQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERMENLVndavekG-GKILYGGKRDEGS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 314 rYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGfM 393
Cdd:cd07145 342 -FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-T 419
|
410
....*....|....*...
gi 946758581 394 HLILTSLPFGGVGASGMG 411
Cdd:cd07145 420 RFRWDNLPFGGFKKSGIG 437
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
21-415 |
2.48e-53 |
|
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: 185.19 E-value: 2.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 21 RPAEFRAAQLKGLGRFLQDNKQLLQEALAQD----LRKSAFESEVSEISISQGeINLALRNLrawmkDETVPKNlATQLD 96
Cdd:cd07152 32 TPPRERAAVLRRAADLLEEHADEIADWIVREsgsiRPKAGFEVGAAIGELHEA-AGLPTQPQ-----GEILPSA-PGRLS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 97 SAfiRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNT-----ERVLVEV-LPRYLDRscfavVLGGP 170
Cdd:cd07152 105 LA--RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggvviARLFEEAgLPAGVLH-----VLPGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 171 AETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPD 248
Cdd:cd07152 178 ADAGEaLVEDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 249 YILcspeMQERLVPALQSAITRFYGE----DPRASP-DLGRIVSEKHFQRLRGL------LGcGRVAIGGQSEesDRYIA 317
Cdd:cd07152 258 RHL----VHESVADAYTAKLAAKAKHlpvgDPATGQvALGPLINARQLDRVHAIvddsvaAG-ARLEAGGTYD--GLFYR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 318 PTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGfmhlil 397
Cdd:cd07152 331 PTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ------ 404
|
410 420
....*....|....*....|...
gi 946758581 398 TSL-----PFGGVGASGMGSYHG 415
Cdd:cd07152 405 TVNdephnPFGGMGASGNGSRFG 427
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
5-416 |
3.05e-53 |
|
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: 185.21 E-value: 3.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQealaqDL--------RKSAFEsEVSEISISqgeINLALR 76
Cdd:cd07101 21 EAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELL-----DLiqletgkaRRHAFE-EVLDVAIV---ARYYAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 77 NLRAWMKDETVPKNLATqLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPR 156
Cdd:cd07101 92 RAERLLKPRRRRGAIPV-LTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 157 Y-LDRSCFAVVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFF 235
Cdd:cd07101 171 AgLPRDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 236 RYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRF-YGEDPRASPDLGRIVSEKHFQRLRGLLGCGR-----VAIGGQS 309
Cdd:cd07101 251 CFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDDAVakgatVLAGGRA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 310 eesdR------YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSS 383
Cdd:cd07101 331 ----RpdlgpyFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRA 406
|
410 420 430
....*....|....*....|....*....|....
gi 946758581 384 GGFCGNDGFM-HLILTSLPFGGVGASGMGSYHGK 416
Cdd:cd07101 407 GTVNVNEGYAaAWASIDAPMGGMKDSGLGRRHGA 440
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
5-422 |
3.94e-53 |
|
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: 184.20 E-value: 3.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSafesevseISISQGEINLALRNLR----- 79
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKP--------IAEARAEVEKCAWICRyyaen 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 80 --AWMKDETVPknlaTQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEI----SKNTERVLVEV 153
Cdd:cd07100 74 aeAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNvpgcALAIEELFREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 154 -LPRYldrsCFAVVLGGPAETGQLLEHkfDYI---FFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVA 229
Cdd:cd07100 150 gFPEG----VFQNLLIDSDQVEAIIAD--PRVrgvTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 230 NRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEK-----HFQRLRGLLGCGRV 303
Cdd:cd07100 224 KTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDeDTDLGPLARKDlrdelHEQVEEAVAAGATL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 304 AIGGqsEESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLAR 380
Cdd:cd07100 304 LLGG--KRPDGpgaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARR 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 946758581 381 TSSG-----GFCGNDgfmhlilTSLPFGGVGASGMGSYHGKFSFDTF 422
Cdd:cd07100 382 LEAGmvfinGMVKSD-------PRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
96-423 |
9.15e-53 |
|
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: 184.24 E-value: 9.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 96 DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLGGPAETG 174
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 175 QLL-EHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILC 252
Cdd:TIGR01804 205 PLLvNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 253 SPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLLGCG-----RVAIGGQSEESDR-----YIAPTVL 321
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIKLGDPfDEATEMGPLISAAHRDKVLSYIEKGkaegaTLATGGGRPENVGlqngfFVEPTVF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 322 VDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfMHLILTSLP 401
Cdd:TIGR01804 365 ADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEAP 442
|
330 340
....*....|....*....|..
gi 946758581 402 FGGVGASGMGSYHGKFSFDTFS 423
Cdd:TIGR01804 443 FGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-411 |
1.00e-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: 183.95 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 8 LQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSafesevseISISQGEINLALRNLR------AW 81
Cdd:cd07149 27 IAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETLRlsaeeaKR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 82 MKDETVPknlatqLDS--------AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV 153
Cdd:cd07149 99 LAGETIP------FDAspggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 154 LPR-YLDRSCFAVVLGGPAETG-QLLEHK-FDYIFFTGSPRVGKIVMAAAAkhLTPVTLELGGKNPCYVDDNCDAQTVAN 230
Cdd:cd07149 173 LLEaGLPKGALNVVTGSGETVGdALVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 231 RVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEKHFQRLRGLL-----GCGRVA 304
Cdd:cd07149 251 RCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDeDTDVGPMISEAEAERIEEWVeeaveGGARLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 305 IGGQSEEsdRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSG 384
Cdd:cd07149 331 TGGKRDG--AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVG 408
|
410 420 430
....*....|....*....|....*....|.
gi 946758581 385 GFCGNDG----FMHliltsLPFGGVGASGMG 411
Cdd:cd07149 409 GVMINDSstfrVDH-----MPYGGVKESGTG 434
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-427 |
1.49e-52 |
|
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: 184.09 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFES--EVSE-ISISQGEINLALRnlrawMKDETVP 88
Cdd:cd07131 47 REAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGrgDVQEaIDMAQYAAGEGRR-----LFGETVP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 89 KNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVL 167
Cdd:cd07131 122 SELPNKD--AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 168 GGPAETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCV 245
Cdd:cd07131 200 GRGEEVGEaLVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 246 APDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRG-----------LLGCGRVAIGGQSEESd 313
Cdd:cd07131 280 ATSRLIVHESVYDEFLKRFVERAKRLRVGDGlDEETDMGPLINEAQLEKVLNyneigkeegatLLLGGERLTGGGYEKG- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 314 RYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPL--ALYT--FSNSSQVVKQVLARTSSGGFCGN 389
Cdd:cd07131 359 YFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLssAIYTedVNKAFRARRDLEAGITYVNAPTI 438
|
410 420 430
....*....|....*....|....*....|....*....
gi 946758581 390 DGFMHliltsLPFGGVGASGMGSYH-GKFSFDTFSHHRA 427
Cdd:cd07131 439 GAEVH-----LPFGGVKKSGNGHREaGTTALDAFTEWKA 472
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
98-423 |
9.27e-52 |
|
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: 181.21 E-value: 9.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRYLdrscFAVVLGGPAE 172
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV----VNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 173 TGQLL-EH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYI 250
Cdd:cd07114 189 TGEALvEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 251 LCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGLLGC-----GRVAIGGQSEESDR-----YIAPT 319
Cdd:cd07114 269 LVQRSIYDEFVERLVARARAIRVGDPLdPETQMGPLATERQLEKVERYVARareegARVLTGGERPSGADlgagyFFEPT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 320 VLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfMHLILTS 399
Cdd:cd07114 349 ILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRALSPS 426
|
330 340
....*....|....*....|....
gi 946758581 400 LPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07114 427 SPFGGFKDSGIGRENGIEAIREYT 450
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-422 |
2.57e-51 |
|
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: 180.46 E-value: 2.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSG---RTRPAEfRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISISQGEINLALRNLRAWMKDETVP 88
Cdd:cd07139 46 RRAFDNGpwpRLSPAE-RAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 89 knlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRYLdrscF 163
Cdd:cd07139 125 ---GSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAaeeagLPPGV----V 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVVLGGpAETGQLL-EHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAG 241
Cdd:cd07139 198 NVVPAD-REVGEYLvRHPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 242 QTCVAPDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLLGCGR------VAIGGQSEESDR 314
Cdd:cd07139 277 QVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPlDPATQIGPLASARQRERVEGYIAKGRaegarlVTGGGRPAGLDR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 --YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGF 392
Cdd:cd07139 357 gwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR 436
|
410 420 430
....*....|....*....|....*....|
gi 946758581 393 MHLiltSLPFGGVGASGMGSYHGKFSFDTF 422
Cdd:cd07139 437 LDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
5-415 |
4.71e-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: 179.48 E-value: 4.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEF-RAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVseisisqgEINLALRNLRAWMK 83
Cdd:cd07146 20 EEALREALALAASYRSTLTRYqRSAILNKAAALLEARREEFARLITLESGLCLKDTRY--------EVGRAADVLRFAAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 84 D------ETVPKNLATQLDS--AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLP 155
Cdd:cd07146 92 EalrddgESFSCDLTANGKArkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 156 RY-LDRSCFAVVLGGPAETGQLLEH--KFDYIFFTGSPRVGKIVMAAAA-KHLtpvTLELGGKNPCYVDDNCDAQTVANR 231
Cdd:cd07146 172 EAgLPPDMLSVVTGEPGEIGDELIThpDVDLVTFTGGVAVGKAIAATAGyKRQ---LLELGGNDPLIVMDDADLERAATL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 232 VAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEK---HFQR--LRGLLGCGRVAI 305
Cdd:cd07146 249 AVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPmDPATDMGTVIDEEaaiQIENrvEEAIAQGARVLL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 306 GGQSEESdrYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGG 385
Cdd:cd07146 329 GNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGT 406
|
410 420 430
....*....|....*....|....*....|
gi 946758581 386 FCGNDGfMHLILTSLPFGGVGASGMGSYHG 415
Cdd:cd07146 407 VNVNEV-PGFRSELSPFGGVKDSGLGGKEG 435
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-422 |
5.89e-51 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 180.27 E-value: 5.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNK----QL--------LQEALAQDLRKSAF-ESEVSEISISQGEI 71
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKedlaQLmtleqgkpLKEAIGEVAYGASFlEYFAEEAKRVYGDI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 72 nlalrnlrawmkdetVPKNLA-TQLdsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVL 150
Cdd:PLN02278 145 ---------------IPSPFPdRRL---LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 151 VEVLPRY-LDRSCFAVVLGGPAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQT 227
Cdd:PLN02278 207 AELALQAgIPPGVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 228 VANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRF-YGEDPRASPDLGRIVSEKHFQRLRG---------- 296
Cdd:PLN02278 287 AVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVEShvqdavskga 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 297 --LLGCGRVAIGGQseesdrYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVV 374
Cdd:PLN02278 367 kvLLGGKRHSLGGT------FYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRA 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 946758581 375 KQVLARTSSGGFCGNDGfmhLILT-SLPFGGVGASGMGSYHGKFSFDTF 422
Cdd:PLN02278 441 WRVSEALEYGIVGVNEG---LISTeVAPFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-411 |
1.45e-50 |
|
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: 178.56 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSG--RTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESevseisiSQGEINLALRNLR---AW---MK 83
Cdd:cd07091 51 RAAFETGwwRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES-------AKGDVALSIKCLRyyaGWadkIQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 84 DETVPKNlATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVL------------- 150
Cdd:cd07091 124 GKTIPID-GNFL--AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLaelikeagfppgv 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 151 VEVLPRYldrscfavvlgGPAETGQLLEH-KFDYIFFTGSPRVGKIVMAAAAK-HLTPVTLELGGKNPCYVDDNCDAQTV 228
Cdd:cd07091 201 VNIVPGF-----------GPTAGAAISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 229 ANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPrASPD--LGRIVSEKHFQRLRGLLGCG----- 301
Cdd:cd07091 270 VEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP-FDPDtfQGPQVSKAQFDKILSYIESGkkega 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 302 RVAIGGQSEESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLAR 380
Cdd:cd07091 349 TLLTGGERHGSKGYfIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRA 428
|
410 420 430
....*....|....*....|....*....|....
gi 946758581 381 TSSGGF---CGNDgFMHliltSLPFGGVGASGMG 411
Cdd:cd07091 429 LKAGTVwvnTYNV-FDA----AVPFGGFKQSGFG 457
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-412 |
2.79e-50 |
|
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: 177.83 E-value: 2.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEvseisisqGEINLALRNLR-----AW-MKDE 85
Cdd:cd07097 47 AAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEAR--------GEVTRAGQIFRyyageALrLSGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 86 TVP---KNLatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRS 161
Cdd:cd07097 119 TLPstrPGV-----EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 162 CFAVVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFN 239
Cdd:cd07097 194 VFNLVMGSGSEVGQaLVEHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 240 AGQTCVAPDYILCSPEMQERLVPALQSAITRF-YGEDPRASPDLGRIVSEKHFQRLRGLLG-----CGRVAIGGQ---SE 310
Cdd:cd07097 274 TGQRCTASSRLIVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIEiarseGAKLVYGGErlkRP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 311 ESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSggfcgnd 390
Cdd:cd07097 354 DEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEA------- 426
|
410 420
....*....|....*....|....*...
gi 946758581 391 GFMHLILTS------LPFGGVGASGMGS 412
Cdd:cd07097 427 GVVMVNLPTagvdyhVPFGGRKGSSYGP 454
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
14-431 |
4.98e-50 |
|
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: 177.11 E-value: 4.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 14 AFSS-GRTRPaEFRAAQLKGLGRFLQDNKQLLQEALAQDLRK---SAFESEVSEISISQGEINLALRNLRAWMKDETVPK 89
Cdd:TIGR03374 50 AFAEwGQTTP-KARAECLLKLADVIEENAQVFAELESRNCGKplhSVFNDEIPAIVDVFRFFAGAARCLSGLAAGEYLEG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 90 NlatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFAVVLGG 169
Cdd:TIGR03374 129 H------TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 170 PAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAP 247
Cdd:TIGR03374 203 GKTVGDPLtgHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 248 DYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGL------LGCGRVAIGG-QSEESDRYIAPT 319
Cdd:TIGR03374 283 CRIYAQRGIYDTLVEKLGAAVATLKSGAPDdESTELGPLSSLAHLERVMKAveeakaLGHIKVITGGeKRKGNGYYFAPT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 320 VLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMhlILTS 399
Cdd:TIGR03374 363 LLAGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFM--LVSE 440
|
410 420 430
....*....|....*....|....*....|..
gi 946758581 400 LPFGGVGASGMGSYHGKFSFDTFSHHRACLLR 431
Cdd:TIGR03374 441 MPHGGQKLSGYGKDMSLYGLEDYTVVRHIMVK 472
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
12-427 |
7.29e-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: 176.83 E-value: 7.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTR-PAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRK---SAFESEVSEIsisqgeINLaLRNLRAW---MKD 84
Cdd:cd07144 55 RKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAAIEALDSGKpyhSNALGDLDEI------IAV-IRYYAGWadkIQG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEiskNTERVLVeVLPRYLDRSCFA 164
Cdd:cd07144 128 KTIPTSPNKL---AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAE---NTPLSLL-YFANLVKEAGFP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 -----VVLGGPAETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRY 237
Cdd:cd07144 201 pgvvnIIPGYGAVAGSaLAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 238 FNAGQTCVAPDYILCSPEMQERLVPALQSAITRFY--GEDPRASPDLGRIVSEKHFQRLRGLLGCGR------VAIG--- 306
Cdd:cd07144 281 YNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKkegaklVYGGeka 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 307 GQSEESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGF 386
Cdd:cd07144 361 PEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMV 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 946758581 387 ---CGNDGFMHliltsLPFGGVGASGMGSYHGKFSFDTFSHHRA 427
Cdd:cd07144 441 winSSNDSDVG-----VPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-411 |
2.21e-49 |
|
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: 175.61 E-value: 2.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 8 LQRLREAFSS-GRTRPAEfRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISisqgeinLALRNLRAWMKDET 86
Cdd:cd07559 44 VDAAHEAFKTwGKTSVAE-RANILNKIADRIEENLELLAVAETLDNGKPIRETLAADIP-------LAIDHFRYFAGVIR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 87 VPKNLATQLDS---AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCF 163
Cdd:cd07559 116 AQEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNP-------CYVDDNCDAQTVANRVAF 234
Cdd:cd07559 196 NVVTGFGSEAGKpLASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPniffddaMDADDDFDDKAEEGQLGF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 235 FryFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPrASPD--LGRIVSEKHFQRLRGLLGCGR-----VAIGG 307
Cdd:cd07559 276 A--FNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP-LDPEtmMGAQVSKDQLEKILSYVDIGKeegaeVLTGG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 308 QSEESDR-----YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTS 382
Cdd:cd07559 353 ERLTLGGldkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQ 432
|
410 420
....*....|....*....|....*....
gi 946758581 383 SGGFCGNDgfMHLILTSLPFGGVGASGMG 411
Cdd:cd07559 433 TGRVWVNC--YHQYPAHAPFGGYKKSGIG 459
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-424 |
4.00e-48 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 172.61 E-value: 4.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTR-----PAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESE-----VS---EISISQGEiNLALRNl 78
Cdd:PLN02467 55 RKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdmddVAgcfEYYADLAE-ALDAKQ- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 79 rawmkdeTVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV----- 153
Cdd:PLN02467 133 -------KAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADIcrevg 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 154 LPRyldrSCFAVVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANR 231
Cdd:PLN02467 206 LPP----GVLNVVTGLGTEAGApLASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEW 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 232 VAFFRYFNAGQTCVAPDYILC----SPEMQERLVPALQS-AITRFYGEDPRaspdLGRIVSEKHFQRLRGLLGCGR---- 302
Cdd:PLN02467 282 AMFGCFWTNGQICSATSRLLVheriASEFLEKLVKWAKNiKISDPLEEGCR----LGPVVSEGQYEKVLKFISTAKsega 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 303 -VAIGGQSEESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVL 378
Cdd:PLN02467 358 tILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVS 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 946758581 379 ARTSSGGF---CGNDGFmhlilTSLPFGGVGASGMGSYHGKFSFDTFSH 424
Cdd:PLN02467 438 EAFQAGIVwinCSQPCF-----CQAPWGGIKRSGFGRELGEWGLENYLS 481
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
10-415 |
1.55e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 171.60 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 10 RLREAFSSGRTRPAEFRAAQLKGLGRFLQDNkqllQEALAqDL--------RKSAFEsEVSEISISqgeINLALRNLRAW 81
Cdd:PRK09407 62 RARAAQRAWAATPVRERAAVLLRFHDLVLEN----REELL-DLvqletgkaRRHAFE-EVLDVALT---ARYYARRAPKL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 82 MKDETVPKNLATqLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDR 160
Cdd:PRK09407 133 LAPRRRAGALPV-LTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 161 SCFAVVLGGPAETGQLLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNA 240
Cdd:PRK09407 212 DLWQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 241 GQTCVAPDYILCSPEMQERLVPALQSAITRF-YGEDPRASPDLGRIVSEKHFQRLRGLLGCGR-----VAIGGQSeesdR 314
Cdd:PRK09407 292 GQLCISIERIYVHESIYDEFVRAFVAAVRAMrLGAGYDYSADMGSLISEAQLETVSAHVDDAVakgatVLAGGKA----R 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 ------YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCG 388
Cdd:PRK09407 368 pdlgplFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNV 447
|
410 420
....*....|....*....|....*...
gi 946758581 389 NDGFMHLI-LTSLPFGGVGASGMGSYHG 415
Cdd:PRK09407 448 NEGYAAAWgSVDAPMGGMKDSGLGRRHG 475
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
12-415 |
1.87e-47 |
|
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: 169.86 E-value: 1.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDlrkSAFEsevseISISQGEINLALRNLRAW------MKDE 85
Cdd:cd07107 29 RAAFPEWRATTPLERARMLRELATRLREHAEELALIDALD---CGNP-----VSAMLGDVMVAAALLDYFaglvteLKGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 86 TVPknlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFAV 165
Cdd:cd07107 101 TIP---VGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 166 VLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFN-AGQ 242
Cdd:cd07107 178 LPGDGATAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGMNFTwCGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 243 TCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEKHFQRLRGLLGCGR------VAIGGQSE----E 311
Cdd:cd07107 258 SCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDpATTMGPLVSRQQYDRVMHYIDSAKregarlVTGGGRPEgpalE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 312 SDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDG 391
Cdd:cd07107 338 GGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGS 417
|
410 420
....*....|....*....|....
gi 946758581 392 FMHLIltSLPFGGVGASGMGSYHG 415
Cdd:cd07107 418 SRHFL--GAPFGGVKNSGIGREEC 439
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
4-412 |
4.46e-47 |
|
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: 170.10 E-value: 4.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 4 FEDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFES--EVSE-ISISQGEINLALRNLRA 80
Cdd:cd07124 71 AEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAdaDVAEaIDFLEYYAREMLRLRGF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 81 WMKDETVPKNlatqldsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LD 159
Cdd:cd07124 151 PVEMVPGEDN--------RYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 160 RSCFAVVLGGPAETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAK------HLTPVTLELGGKNPCYVDDNCDAQTVANR 231
Cdd:cd07124 223 PGVVNFLPGPGEEVGDyLVEHpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 232 V--AFFRYfnAGQTCVApdyilCS---------PEMQERLVpALQSAITRFYGEDPraSPDLGRIVSEKHFQRLRGLL-- 298
Cdd:cd07124 303 IvrSAFGF--QGQKCSA-----CSrvivhesvyDEFLERLV-ERTKALKVGDPEDP--EVYMGPVIDKGARDRIRRYIei 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 299 --GCGRVAIGGQSEESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQV 373
Cdd:cd07124 373 gkSEGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEH 452
|
410 420 430
....*....|....*....|....*....|....*....
gi 946758581 374 VKQVLARTSSGGFCGNDGFMHLILTSLPFGGVGASGMGS 412
Cdd:cd07124 453 LERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGS 491
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
4-428 |
1.18e-46 |
|
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: 168.13 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 4 FEDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFES--EVSE-ISISQGEINLALRnlra 80
Cdd:cd07086 37 VEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGlgEVQEmIDICDYAVGLSRM---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 81 wMKDETVPKNLATQldSAFIRKEPFGLVLIIAPWNYPL-----NLTLvplvgALAAGNCVVLKPSE----ISKNTERVLV 151
Cdd:cd07086 113 -LYGLTIPSERPGH--RLMEQWNPLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIAVTKILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 152 EVLPRY-LDRSCFAVVLGGpAETGQLLEH--KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTV 228
Cdd:cd07086 185 EVLEKNgLPPGVVNLVTGG-GDGGELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 229 ANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQR-LRGL-----LGcG 301
Cdd:cd07086 264 VRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLdEGTLVGPLINQAAVEKyLNAIeiaksQG-G 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 302 RVAIGGQSEESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPL--ALYTfSNSSQVVKQ 376
Cdd:cd07086 343 TVLTGGKRIDGGEpgnYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLssSIFT-EDLREAFRW 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 946758581 377 VLARTSSggfCG----NdgfmhlILTS-----LPFGGVGASGMGSYHGKFSFDTFSHHRAC 428
Cdd:cd07086 422 LGPKGSD---CGivnvN------IPTSgaeigGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
99-366 |
5.27e-46 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 164.91 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLGGPAETGQLL 177
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 178 --EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPE 255
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 256 MQERLVPALQSAITRFYGEDP--RASPDLGRIVSEKHFQRLRGLLG-----CGRVAIGGQSEESDRYI-APTVLVDVQET 327
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFGNPaeRNDIAMGPLINAAALERVEQKVAraveeGARVALGGKAVEGKGYYyPPTLLLDVRQE 305
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 946758581 328 EPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPL--ALYT 366
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLtsSIYT 346
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
85-427 |
8.96e-46 |
|
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: 165.78 E-value: 8.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPKNLAtqldsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCF 163
Cdd:cd07143 131 ETDIKKLT------YTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVVLGGPAETGQLLE-H-KFDYIFFTGSPRVGKIVMAAAAK-HLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNA 240
Cdd:cd07143 205 NVVSGYGRTCGNAISsHmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNH 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 241 GQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEKHFQRLRGLLGCGR-----VAIGGQSEESDR 314
Cdd:cd07143 285 GQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAeDTFQGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 Y-IAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGF---CGNd 390
Cdd:cd07143 365 YfIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVwvnCYN- 443
|
330 340 350
....*....|....*....|....*....|....*..
gi 946758581 391 gfmhLILTSLPFGGVGASGMGSYHGKFSFDTFSHHRA 427
Cdd:cd07143 444 ----LLHHQVPFGGYKQSGIGRELGEYALENYTQIKA 476
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
20-423 |
1.90e-45 |
|
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: 164.40 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 20 TRPAEfRAAQLKGLGRFLQDNKQLLQEALAQDL----RKSAFESEVSeISISQGEINLALRnlrawMKDETVPKNLATQl 95
Cdd:cd07151 51 TLPQE-RAEILEKAAQILEERRDEIVEWLIRESgstrIKANIEWGAA-MAITREAATFPLR-----MEGRILPSDVPGK- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 96 dSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNT-----ERVLVEV-LPRYLdrscFAVVLGG 169
Cdd:cd07151 123 -ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITgglllAKIFEEAgLPKGV----LNVVVGA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 170 PAETG-QLLEHKF-DYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAP 247
Cdd:cd07151 198 GSEIGdAFVEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 248 DYILCSPEMQERLVPALQSAITRF-YGeDPRAsPD--LGRIVSEKHFQRLRGLL------GcGRVAIGGQSEesDRYIAP 318
Cdd:cd07151 278 NRIIVHEDVYDEFVEKFVERVKALpYG-DPSD-PDtvVGPLINESQVDGLLDKIeqaveeG-ATLLVGGEAE--GNVLEP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 319 TVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHlILT 398
Cdd:cd07151 353 TVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEP 431
|
410 420
....*....|....*....|....*
gi 946758581 399 SLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07151 432 HVPFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-423 |
2.37e-45 |
|
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: 164.55 E-value: 2.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGR-TRPAEfRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVSEISisqgeinLALRNLRAWMKDETVPKN 90
Cdd:cd07117 48 QEAFKTWRkTTVAE-RANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIP-------LAADHFRYFAGVIRAEEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 91 LATQLDSAF---IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSCFAVVL 167
Cdd:cd07117 120 SANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 168 GGPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCV 245
Cdd:cd07117 200 GKGSKSGEyLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 246 APDYILCSPEMQERLVPALQSAITRFYGEDPRaSPD--LGRIVSEKHFQRLRGLLGCG-----RVAIGGQSEESDRY--- 315
Cdd:cd07117 280 AGSRIFVQEGIYDEFVAKLKEKFENVKVGNPL-DPDtqMGAQVNKDQLDKILSYVDIAkeegaKILTGGHRLTENGLdkg 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 316 --IAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfM 393
Cdd:cd07117 359 ffIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNT--Y 436
|
410 420 430
....*....|....*....|....*....|
gi 946758581 394 HLILTSLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07117 437 NQIPAGAPFGGYKKSGIGRETHKSMLDAYT 466
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
12-409 |
3.01e-44 |
|
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: 160.51 E-value: 3.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEvSEISISQGEINLALRNLrawmKDETVPKNL 91
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAAMAGKIDISIKAY----HERTGERAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 92 ATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVL-PRYLDRSCFAVVLGGP 170
Cdd:cd07095 85 PMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNLVQGGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 171 AETGQLLEHK-FDYIFFTGSPRVGKIVMAAAAKHltP---VTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCV- 245
Cdd:cd07095 165 ETGEALAAHEgIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTc 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 246 APDYILCSPEMQERLVPALQSAITRFYGEDPRASPD-LGRIVSEKHFQRlrGLLGCGR-VAIGGQS-------EESDRYI 316
Cdd:cd07095 243 ARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAAR--YLLAQQDlLALGGEPllamerlVAGTAFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 317 APTvLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNdgfmhLI 396
Cdd:cd07095 321 SPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN-----RP 394
|
410
....*....|....*..
gi 946758581 397 LT----SLPFGGVGASG 409
Cdd:cd07095 395 TTgassTAPFGGVGLSG 411
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
98-424 |
7.63e-44 |
|
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: 160.16 E-value: 7.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLGGpAETGQL 176
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 177 LEHKFDY--IFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTC------VAPD 248
Cdd:cd07090 189 LCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCsngtrvFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 249 YILcsPEMQERLVPALQS-AITRFYGEDPRaspdLGRIVSEKHFQRLRGLLGCG-----RVAIGGQSEESDR------YI 316
Cdd:cd07090 269 SIK--DEFTERLVERTKKiRIGDPLDEDTQ----MGALISEEHLEKVLGYIESAkqegaKVLCGGERVVPEDglengfYV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 317 APTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfMHLI 396
Cdd:cd07090 343 SPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNIS 420
|
330 340
....*....|....*....|....*...
gi 946758581 397 LTSLPFGGVGASGMGSYHGKFSFDTFSH 424
Cdd:cd07090 421 PVEVPFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
19-412 |
1.04e-43 |
|
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: 160.04 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 19 RTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEvSEISISQGEIN---LALRNL-RAWMKDETVPKNLATQ 94
Cdd:cd07082 56 PTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL-KEVDRTIDYIRdtiEELKRLdGDSLPGDWFPGTKGKI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 95 ldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSeisknTERVLV-EVLPRYLDRSCF-----AVVLG 168
Cdd:cd07082 135 ---AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA-----TQGVLLgIPLAEAFHDAGFpkgvvNVVTG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 169 GPAETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKhlTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVA 246
Cdd:cd07082 207 RGREIGDpLVTHgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 247 PDYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGLL------GcGRVAIGGQSEEsDRYIAPT 319
Cdd:cd07082 285 IKRVLVHESVADELVELLKEEVAKLKVGMPWdNGVDITPLIDPKSADFVEGLIddavakG-ATVLNGGGREG-GNLIYPT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 320 VLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLIlTS 399
Cdd:cd07082 363 LLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP-DH 441
|
410
....*....|...
gi 946758581 400 LPFGGVGASGMGS 412
Cdd:cd07082 442 FPFLGRKDSGIGT 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
97-431 |
1.21e-43 |
|
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: 159.91 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 97 SAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRyldrSCFAVVLGGPA 171
Cdd:cd07113 135 TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELakeagIPD----GVLNVVNGKGA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 172 ETGQLLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYI 250
Cdd:cd07113 211 VGAQLISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 251 LCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLLGCGR-----VAIGGQSEESDRY-IAPTVLVD 323
Cdd:cd07113 291 YVHRSKFDELVTKLKQALSSFQVGSPmDESVMFGPLANQPHFDKVCSYLDDARaegdeIVRGGEALAGEGYfVQPTLVLA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 324 VQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNdgfMHLIL-TSLPF 402
Cdd:cd07113 371 RSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLdPAVPF 447
|
330 340
....*....|....*....|....*....
gi 946758581 403 GGVGASGMGSYHGKFSFDTFSHHRACLLR 431
Cdd:cd07113 448 GGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
103-412 |
2.85e-43 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 159.72 E-value: 2.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLGGPAETGQ-LLEH- 179
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDyLVDHp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 180 KFDYIFFTGSPRVGKIVMAAAAK------HLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVApdyilCS 253
Cdd:PRK03137 250 KTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA-----CS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 254 ---------PEMQERLVpALQSAITRFYGEDPrasPDLGRIVSEKHFQRLRGLL----GCGRVAIGGQSEESDRY-IAPT 319
Cdd:PRK03137 325 raivhedvyDEVLEKVV-ELTKELTVGNPEDN---AYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQPT 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 320 VLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMHLILTS 399
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGY 480
|
330
....*....|...
gi 946758581 400 LPFGGVGASGMGS 412
Cdd:PRK03137 481 HPFGGFNMSGTDS 493
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
12-416 |
5.30e-43 |
|
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: 158.33 E-value: 5.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEvseisisQGEINLALRNLR---AWmkdetvp 88
Cdd:cd07111 69 RTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESR-------DCDIPLVARHFYhhaGW------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 89 knlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVL 167
Cdd:cd07111 135 ---AQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 168 GGPAETGQLLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVA 246
Cdd:cd07111 212 GNGSFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 247 PDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLLGCGRvAIGGQSEESDR-------YIAP 318
Cdd:cd07111 292 GSRLLVQESVAEELIRKLKERMSHLRVGDPlDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 319 TVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfMHLILT 398
Cdd:cd07111 371 TLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING--HNLFDA 448
|
410
....*....|....*...
gi 946758581 399 SLPFGGVGASGMGSYHGK 416
Cdd:cd07111 449 AAGFGGYRESGFGREGGK 466
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-415 |
1.46e-42 |
|
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: 157.72 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFES--EVSEisisqgEINLALRNLRAWM 82
Cdd:TIGR01237 72 EHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEAdaEVAE------AIDFMEYYARQMI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 83 KDETVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRS 161
Cdd:TIGR01237 146 ELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 162 CFAVVLGGPAETGQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAK------HLTPVTLELGGKNPCYVDDNCDAQTVANRVA 233
Cdd:TIGR01237 226 VVQFVPGSGSEVGDyLVDHpKTSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 234 FFRYFNAGQTCVA-PDYILCSP---EMQERLVPALQSAITrfyGEDPRASPDLGRIVSEKHFQRLRGLLGCG----RVAI 305
Cdd:TIGR01237 306 TSAFGFAGQKCSAgSRAVVHEKvydEVVERFVEITESLKV---GPPDSADVYVGPVIDQKSFNKIMEYIEIGkaegRLVS 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 306 GGQSEESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSG 384
Cdd:TIGR01237 383 GGCGDDSKGYfIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVG 462
|
410 420 430
....*....|....*....|....*....|.
gi 946758581 385 GFCGNDGFMHLILTSLPFGGVGASGMGSYHG 415
Cdd:TIGR01237 463 NLYFNRNITGAIVGYQPFGGFKMSGTDSKAG 493
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
67-427 |
2.09e-42 |
|
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: 156.50 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 67 SQGEINLALRNLR---AWMKD---ETVPknlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPS 140
Cdd:cd07142 101 RYAEVPLAARLFRyyaGWADKihgMTLP---ADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 141 EISKNTE----RVLVEV-LPRyldrSCFAVVLG-GPAETGQLLEHK-FDYIFFTGSPRVGKIVMAAAAK-HLTPVTLELG 212
Cdd:cd07142 178 EQTPLSAllaaKLAAEAgLPD----GVLNIVTGfGPTAGAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 213 GKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVP-ALQSAITRFYGEDPRASPDLGRIVSEKHF 291
Cdd:cd07142 254 GKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEkAKARALKRVVGDPFRKGVEQGPQVDKEQF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 292 QRLRGLLGCGR------VAIGGQSEESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALY 365
Cdd:cd07142 334 EKILSYIEHGKeegatlITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAG 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 946758581 366 TFSNSSQVVKQVLARTSSGGFCGN--DGFMhlilTSLPFGGVGASGMGSYHGKFSFDTFSHHRA 427
Cdd:cd07142 414 VFSKNIDTANTLSRALKAGTVWVNcyDVFD----ASIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
98-423 |
1.29e-40 |
|
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: 151.73 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVL-------------VEVLPRYldrscfa 164
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLaslikeagfppgvVNVVPGY------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 vvlgGPAETGQLLEH-KFDYIFFTGSPRVGKIVMAAAAK-HLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQ 242
Cdd:cd07141 212 ----GPTAGAAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 243 TCVAPDYILCSPEMQERLVP-ALQSAITRFYGeDPRASP-DLGRIVSEKHFQRLRGLLGCGR------VAIGGQSEESDR 314
Cdd:cd07141 288 CCCAGSRTFVQESIYDEFVKrSVERAKKRVVG-NPFDPKtEQGPQIDEEQFKKILELIESGKkegaklECGGKRHGDKGY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 YIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfMH 394
Cdd:cd07141 367 FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNC--YN 444
|
330 340
....*....|....*....|....*....
gi 946758581 395 LILTSLPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07141 445 VVSPQAPFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
82-359 |
1.60e-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: 151.52 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 82 MKDETVPkNLATQLDSAFIRkEPFGLVLIIAPWNYPLnltLVPL---VGALAAGNCVVLKPSEISKNTERVLVEV----- 153
Cdd:cd07085 116 LKGEYLE-NVARGIDTYSYR-QPLGVVAGITPFNFPA---MIPLwmfPMAIACGNTFVLKPSERVPGAAMRLAELlqeag 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 154 LPRyldrSCFAVVLGGPAETGQLLEH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRV 232
Cdd:cd07085 191 LPD----GVLNVVHGGKEAVNALLDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANAL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 233 AFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRF---YGEDPRAspDLGRIVSEKHFQRLRGLLGCG-----RVA 304
Cdd:cd07085 267 VGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkvgAGDDPGA--DMGPVISPAAKERIEGLIESGveegaKLV 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 305 IGGQSEESDRY-----IAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRRE 359
Cdd:cd07085 345 LDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP 404
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
13-411 |
2.07e-40 |
|
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: 150.47 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 13 EAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRK--SAFESEV----SEISISQGEinlALRNLRAWMKDET 86
Cdd:cd07147 32 KAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKpiKDARGEVaraiDTFRIAAEE---ATRIYGEVLPLDI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 87 VPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAV 165
Cdd:cd07147 109 SARGEGRQ---GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETgLPKGAFSV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 166 VLGGPAETGQLLEHK-FDYIFFTGSPRVG-KIVMAAAAKHltpVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQT 243
Cdd:cd07147 186 LPCSRDDADLLVTDErIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 244 CVAPDYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGLL-----GCGRVAIGGQSEESdrYIA 317
Cdd:cd07147 263 CISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKdDATDVGPMISESEAERVEGWVneavdAGAKLLTGGKRDGA--LLE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 318 PTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfmhlIL 397
Cdd:cd07147 341 PTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND-----VP 415
|
410
....*....|....*...
gi 946758581 398 T----SLPFGGVGASGMG 411
Cdd:cd07147 416 TfrvdHMPYGGVKDSGIG 433
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
23-423 |
1.91e-38 |
|
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: 145.18 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 23 AEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVsEISISQGEIN----LAlRNLRAWMKdETVPKNLATQLdsa 98
Cdd:cd07120 41 PRLRARVLLELADAFEANAERLARLLALENGKILGEARF-EISGAISELRyyagLA-RTEAGRMI-EPEPGSFSLVL--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 99 firKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP----SEISKNTERVLVEVlpRYLDRSCFAVVLGGPAETG 174
Cdd:cd07120 115 ---REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPagqtAQINAAIIRILAEI--PSLPAGVVNLFTESGSEGA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 175 QLL--EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILC 252
Cdd:cd07120 190 AHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 253 ----SPEMQERLVPALQsAITRFYGEDPRAspDLGRIVSEKHFQRLRGLLG-----CGRVAI-GGQSEESDR---YIAPT 319
Cdd:cd07120 270 qrsiADEVRDRLAARLA-AVKVGPGLDPAS--DMGPLIDRANVDRVDRMVEraiaaGAEVVLrGGPVTEGLAkgaFLRPT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 320 VLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgFMHLIlTS 399
Cdd:cd07120 347 LLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND-WNKLF-AE 424
|
410 420
....*....|....*....|....
gi 946758581 400 LPFGGVGASGMGSYHGKFSFDTFS 423
Cdd:cd07120 425 AEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
14-415 |
2.41e-37 |
|
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: 143.10 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 14 AFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFES--EVSEIsisqgeINLALRNLRAWMKDETVPKNL 91
Cdd:cd07083 67 AFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAidDVAEA------IDFIRYYARAALRLRYPAVEV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 92 AT---QLDSAFIRkePFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNTERVLVEV-LPRYLDRSCF 163
Cdd:cd07083 141 VPypgEDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFHEAgFPPGVVQFLP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVvlgGPAETGQLLEH-KFDYIFFTGSPRVGKIVMAAAAKHLT------PVTLELGGKNPCYVDDNCDAQTVANRVAFFR 236
Cdd:cd07083 219 GV---GEEVGAYLTEHeRIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 237 YFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEKHFQRLRGLLGCGR----VAIGGQSEE 311
Cdd:cd07083 296 FGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEnGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 312 SDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLD--EAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCG 388
Cdd:cd07083 376 GEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYI 455
|
410 420
....*....|....*....|....*..
gi 946758581 389 NDGFMHLILTSLPFGGVGASGMGSYHG 415
Cdd:cd07083 456 NRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
102-424 |
1.31e-36 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 141.11 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 102 KEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEiskntERVLVEVLPRYLDR------SCFAVVLG-GPAETG 174
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAE-----QTPLSALFYAHLAKlagvpdGVINVVTGfGPTAGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 175 QLLEH-KFDYIFFTGSPRVGKIVMAAAAK-HLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILC 252
Cdd:PLN02766 231 AIASHmDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 253 SPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLRGLLGCGR-----VAIGGQSE-ESDRYIAPTVLVDVQ 325
Cdd:PLN02766 311 QEGIYDEFVKKLVEKAKDWVVGDPfDPRARQGPQVDKQQFEKILSYIEHGKregatLLTGGKPCgDKGYYIEPTIFTDVT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 326 ETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDGFMhlILTSLPFGGV 405
Cdd:PLN02766 391 EDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFA--FDPDCPFGGY 468
|
330
....*....|....*....
gi 946758581 406 GASGMGSYHGKFSFDTFSH 424
Cdd:PLN02766 469 KMSGFGRDQGMDALDKYLQ 487
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
67-422 |
1.54e-36 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 140.43 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 67 SQGEINLALRNLRaWMKDE-------TVPKNlatQLDSAFIR-KEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLK 138
Cdd:PRK11241 105 AKGEISYAASFIE-WFAEEgkriygdTIPGH---QADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 139 PSEISKNTERVLVEVLPRY-LDRSCFAVVLGGPAETGQLLEHK--FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKN 215
Cdd:PRK11241 181 PASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 216 PCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFY-GEDPRASPDLGRIVSEKHFQRL 294
Cdd:PRK11241 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 295 R-----GLLGCGRVAIGGQSEE-SDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFS 368
Cdd:PRK11241 341 EehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYA 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 946758581 369 NSSQVVKQVLARTSSGGFCGNDGfmhLILTSL-PFGGVGASGMGSYHGKFSFDTF 422
Cdd:PRK11241 421 RDLSRVFRVGEALEYGIVGINTG---IISNEVaPFGGIKASGLGREGSKYGIEDY 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
98-411 |
2.20e-36 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 140.03 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLGGPAETGQL 176
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 177 L--EHKFDYIFFTGSPRVGKIVMA-AAAKHLTPVTLELGGKNPCYVDDNC-DAQTVANRVAFFRYFNAGQTCVAPDYILC 252
Cdd:PRK09847 231 LsrHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 253 SPEMQERLVPALQSAITRFYGEDPrASPD--LGRIVSEKHFQR----LRGLLGCGRVAIGGQSEESDRYIAPTVLVDVQE 326
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQPGHP-LDPAttMGTLIDCAHADSvhsfIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDP 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 327 TEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGG-FCG--NDGFMhliltSLPFG 403
Cdd:PRK09847 390 NASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSvFVNnyNDGDM-----TVPFG 464
|
....*...
gi 946758581 404 GVGASGMG 411
Cdd:PRK09847 465 GYKQSGNG 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-427 |
1.59e-35 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 138.40 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLG-GPAETGQLLEH- 179
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASHm 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 180 KFDYIFFTGSPRVGKIVMAAAAK-HLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQE 258
Cdd:PLN02466 274 DVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 259 RLV-PALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLL------GCGRVAIGGQSEESDRYIAPTVLVDVQETEPVM 331
Cdd:PLN02466 354 EFVeKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIksgvesGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 332 QEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVkQVLARTSSGGFCGNDGFmHLILTSLPFGGVGASGMG 411
Cdd:PLN02466 434 QDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTA-NTLSRALRVGTVWVNCF-DVFDAAIPFGGYKMSGIG 511
|
330
....*....|....*.
gi 946758581 412 SYHGKFSFDTFSHHRA 427
Cdd:PLN02466 512 REKGIYSLNNYLQVKA 527
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
96-411 |
9.40e-35 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 135.39 E-value: 9.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 96 DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRYLdrscFAVVlGGP 170
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIyteagLPDGV----FNVV-QGD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 171 AETGQLL-EH-KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCD------AQTVANrvaffrYFNAGQ 242
Cdd:PRK13252 209 GRVGAWLtEHpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADldraadIAMLAN------FYSSGQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 243 TCVAPDYILCSPEMQERLVPALQSAITRFYGEDPR-ASPDLGRIVSEKHFQRLRGLLGCG-----RVAIGG-----QSEE 311
Cdd:PRK13252 283 VCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMdPATNFGPLVSFAHRDKVLGYIEKGkaegaRLLCGGerlteGGFA 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 312 SDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNS----SQVVKQVLArtssgGFC 387
Cdd:PRK13252 363 NGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVIHQLEA-----GIC 437
|
330 340 350
....*....|....*....|....*....|
gi 946758581 388 gndgfmhLILT------SLPFGGVGASGMG 411
Cdd:PRK13252 438 -------WINTwgespaEMPVGGYKQSGIG 460
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
5-356 |
5.05e-34 |
|
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: 133.35 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSS-GRTRPAEfRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESevseisiSQGEINLALRNLRAWMK 83
Cdd:cd07116 41 ELALDAAHAAKEAwGKTSVAE-RANILNKIADRMEANLEMLAVAETWDNGKPVRET-------LAADIPLAIDHFRYFAG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 84 DETVPKNLATQLDS---AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDR 160
Cdd:cd07116 113 CIRAQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 161 SCFAVVLGGPAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNP-CYVDDNCDAQTvanrvAFFR- 236
Cdd:cd07116 193 GVVNVVNGFGLEAGKPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADVMDADD-----AFFDk 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 237 --------YFNAGQTCVAPDYILCSPEMQERLVP-ALQ--SAITRFYGEDPraSPDLGRIVSEKHFQRLRGLLGCGR--- 302
Cdd:cd07116 268 alegfvmfALNQGEVCTCPSRALIQESIYDRFMErALErvKAIKQGNPLDT--ETMIGAQASLEQLEKILSYIDIGKeeg 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 946758581 303 --VAIGGQ-----SEESDRYIAPTVLVDVQETEpVMQEEIFGPILPIVTVRSLDEAIDFIN 356
Cdd:cd07116 346 aeVLTGGErnelgGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIAN 405
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-409 |
8.19e-31 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 124.30 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 12 REAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEvSEISISQGEINLALR--NLRAWMKDETVPK 89
Cdd:PRK09457 47 RAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA-TEVTAMINKIAISIQayHERTGEKRSEMAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 90 NlatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPryldrscfA 164
Cdd:PRK09457 126 G------AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLP--------A 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLG---GPAETGQ-LLEHK-FDYIFFTGSPRVGKIVMAAAAKHltP---VTLELGGKNPCYVDDNCDAQTVANRVAFFR 236
Cdd:PRK09457 192 GVLNlvqGGRETGKaLAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 237 YFNAGQTCVAPDYILCSPEMQ-ERLVPALQSAITRFYGEDPRASPD--LGRIVSEKHFQRL----RGLLGCGRVAI--GG 307
Cdd:PRK09457 270 FISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAEPQpfMGAVISEQAAQGLvaaqAQLLALGGKSLleMT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 308 QSEESDRYIAPTvLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFC 387
Cdd:PRK09457 350 QLQAGTGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVN 428
|
410 420
....*....|....*....|....*.
gi 946758581 388 GNDGfmhliLT----SLPFGGVGASG 409
Cdd:PRK09457 429 WNKP-----LTgassAAPFGGVGASG 449
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-411 |
9.79e-31 |
|
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: 124.23 E-value: 9.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 5 EDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFE--SEVSEisisqgeinlA---LR--- 76
Cdd:cd07125 72 DAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADadAEVRE----------AidfCRyya 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 77 -NLRAWMKDETVPKNLAtQLDsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVL- 154
Cdd:cd07125 142 aQARELFSDPELPGPTG-ELN--GLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLh 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 155 ----PRYLdrscFAVVLGGPAETGQ-LLEHK-FDYIFFTGSPRVGKI---VMAAAAKHLTPVTLELGGKNPCYVDDNCDA 225
Cdd:cd07125 219 eagvPRDV----LQLVPGDGEEIGEaLVAHPrIDGVIFTGSTETAKLinrALAERDGPILPLIAETGGKNAMIVDSTALP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 226 -QTVANRV--AFfryFNAGQTCVAPDyILC-----SPEMQERLVPALQSAITrfyGeDPR-ASPDLGRIVSEKHFQRLRG 296
Cdd:cd07125 295 eQAVKDVVqsAF---GSAGQRCSALR-LLYlqeeiAERFIEMLKGAMASLKV---G-DPWdLSTDVGPLIDKPAGKLLRA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 297 LLGCGR-----VAIGGQSEESDRYIAPTVLVDVqeTEPVMQEEIFGPILPIVTVRS--LDEAIDFINRREKPLALYTFSN 369
Cdd:cd07125 367 HTELMRgeawlIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSR 444
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 946758581 370 SSQVVKQVLARTSSGGFCGNDGFMHLILTSLPFGGVGASGMG 411
Cdd:cd07125 445 DEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTG 486
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
86-411 |
2.73e-30 |
|
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: 122.60 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 86 TVPKNLA-TQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCF 163
Cdd:cd07140 128 TIPINQArPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVVLGGPAETGQLLEHKFDY--IFFTGSPRVGKIVMAAAAK-HLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNA 240
Cdd:cd07140 208 NILPGSGSLVGQRLSDHPDVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 241 GQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRL-----RGLLGCGRVAIGG-QSEESD 313
Cdd:cd07140 288 GENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPlDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 314 RYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRS--LDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDg 391
Cdd:cd07140 368 FFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT- 446
|
330 340
....*....|....*....|
gi 946758581 392 fMHLILTSLPFGGVGASGMG 411
Cdd:cd07140 447 -YNKTDVAAPFGGFKQSGFG 465
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
2-422 |
2.04e-28 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 117.27 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 2 DPFEDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSafesevseISISQGEINLAlRNLRAW 81
Cdd:PRK13968 29 DDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP--------INQARAEVAKS-ANLCDW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 82 MKdETVPKNLATQL-----DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPR 156
Cdd:PRK13968 100 YA-EHGPAMLKAEPtlvenQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 157 Y-LDRSCFAVVLGGPAETGQLL-EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAF 234
Cdd:PRK13968 179 AgIPQGVYGWLNADNDGVSQMInDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 235 FRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRASP-DLGRIV-----SEKHFQRLRGLLGCGRVAIGGQ 308
Cdd:PRK13968 259 GRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEEnALGPMArfdlrDELHHQVEATLAEGARLLLGGE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 309 SEESD-RYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSG--- 384
Cdd:PRK13968 339 KIAGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGgvf 418
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 946758581 385 --GFCGNDGfmhliltSLPFGGVGASGMGSYHGKFSFDTF 422
Cdd:PRK13968 419 inGYCASDA-------RVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
22-411 |
3.76e-27 |
|
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: 113.28 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 22 PAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESEVsEISISQGEINLALRNLRAwMKDETVPKNLaTQLDS---A 98
Cdd:cd07148 42 PAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV-EVTRAIDGVELAADELGQ-LGGREIPMGL-TPASAgriA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPrylDRSCFAVVLGGPAET 173
Cdd:cd07148 119 FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLlheagLP---EGWCQAVPCENAVAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 174 GQLLEHKFDYIFFTGSPRVGKIVMAAAAKHlTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCS 253
Cdd:cd07148 196 KLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 254 PEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEKHFQRLR-----GLLGCGRVAIGGQsEESDRYIAPTVLVDVQET 327
Cdd:cd07148 275 AEIADDFAQRLAAAAEKLVVGDPtDPDTEVGPLIRPREVDRVEewvneAVAAGARLLCGGK-RLSDTTYAPTVLLDPPRD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 328 EPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGNDgfmHLILTS--LPFGGV 405
Cdd:cd07148 354 AKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HTAFRVdwMPFAGR 430
|
....*.
gi 946758581 406 GASGMG 411
Cdd:cd07148 431 RQSGYG 436
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
4-356 |
9.67e-26 |
|
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: 109.22 E-value: 9.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 4 FEDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFES--EVSE-ISISqgeinlalrnlra 80
Cdd:cd07130 36 YESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGlgEVQEmIDIC------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 81 wmkDETVpkNLATQLDSAFIRKE-----------PFGLVLIIAPWNYPL-----NLTLvplvgALAAGNCVVLKPSE--- 141
Cdd:cd07130 103 ---DFAV--GLSRQLYGLTIPSErpghrmmeqwnPLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttp 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 142 -ISKNTERVLVEVLPRY-LDRSCFAVVLGGpAETGQLLEH--KFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPC 217
Cdd:cd07130 173 lTAIAVTKIVARVLEKNgLPGAIASLVCGG-ADVGEALVKdpRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 218 YVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDL-GRIVSEKHFQRLRG 296
Cdd:cd07130 252 IVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLvGPLHTKAAVDNYLA 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 946758581 297 LL------GcGRVAIGGQSEESD-RYIAPTVlVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFIN 356
Cdd:cd07130 332 AIeeaksqG-GTVLFGGKVIDGPgNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
13-415 |
8.23e-25 |
|
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: 106.92 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 13 EAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSafesevseISISQGEINLALRNLRAWMKD--ETVPKN 90
Cdd:TIGR01238 85 QAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKT--------IHNAIAEVREAVDFCRYYAKQvrDVLGEF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 91 LAtqldsafirkEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVLGG 169
Cdd:TIGR01238 157 SV----------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 170 PAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKHL---TPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTC 244
Cdd:TIGR01238 227 GADVGAALtsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRC 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 245 VAPDYILCSPEMQERLVPALQSAITRFYGEDP-RASPDLGRIVSEK-------HFQRLRGLLGCGRVAIGGQSEESDR-- 314
Cdd:TIGR01238 307 SALRVLCVQEDVADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEakqnllaHIEHMSQTQKKIAQLTLDDSRACQHgt 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 315 YIAPTV--LVDVQEtepvMQEEIFGPILPIVTVRS--LDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFCGND 390
Cdd:TIGR01238 387 FVAPTLfeLDDIAE----LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNR 462
|
410 420
....*....|....*....|....*
gi 946758581 391 GFMHLILTSLPFGGVGASGMGSYHG 415
Cdd:TIGR01238 463 NQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
26-356 |
1.95e-24 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 105.61 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 26 RAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFESeVSEISISQGEINLA----LRNLR--AWMKDETVPKNLATQLdsAF 99
Cdd:PLN00412 77 RAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVRSGDLISYTaeegVRILGegKFLVSDSFPGNERNKY--CL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-----LPRYLdrscFAVVLGGPAETG 174
Cdd:PLN00412 154 TSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCfhlagFPKGL----ISCVTGKGSEIG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 175 QLL-EHK-FDYIFFTGsprvGKIVMAAAAK-HLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYIL 251
Cdd:PLN00412 230 DFLtMHPgVNCISFTG----GDTGIAISKKaGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 252 CSPEMQERLVPALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGCGRVAIGGQSEESDR---YIAPTVLVDVQETE 328
Cdd:PLN00412 306 VMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIWPLLLDNVRPDM 385
|
330 340
....*....|....*....|....*...
gi 946758581 329 PVMQEEIFGPILPIVTVRSLDEAIDFIN 356
Cdd:PLN00412 386 RIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
98-419 |
8.88e-23 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 100.58 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRY-LDRSCFAVVL-GGPAETGQ 175
Cdd:PRK09406 117 AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAgFPDGCFQTLLvGSGAVEAI 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 176 LLEHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDYILCSPE 255
Cdd:PRK09406 197 LRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHAD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 256 MQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEKH----FQRLRGLLGCG-RVAIGGQSEESDR-YIAPTVLVDVQETE 328
Cdd:PRK09406 277 VYDAFAEKFVARMAALRVGDPTDpDTDVGPLATEQGrdevEKQVDDAVAAGaTILCGGKRPDGPGwFYPPTVITDITPDM 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 329 PVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFcgndgFMHLILTS---LPFGGV 405
Cdd:PRK09406 357 RLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQV-----FINGMTVSypeLPFGGV 431
|
330
....*....|....*..
gi 946758581 406 GASGMG---SYHGKFSF 419
Cdd:PRK09406 432 KRSGYGrelSAHGIREF 448
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
104-415 |
3.38e-22 |
|
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: 98.46 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP----SEISKNTERVLVEVLprYLDRSCFAVVLGGPAETGQLLEH 179
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPhtavSIVMQIMVRLLHYAG--LLPPEDVTLINGDGKTMQALLLH 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 180 -KFDYIFFTGSPRVGKIVMAAAakHLTPVTLELGGKNPCYVDDNCDA-QTVANRVAFFRYFNAGQTCVAPDYILCSPEMQ 257
Cdd:cd07084 178 pNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSGQKCTAQSMLFVPENWS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 258 -ERLVPALQSAITRFYGEDPRaspdLGRIVSEKHFQRL--RGLLGcGRVAIGGQSEESDRYI--------APTVLVDVQE 326
Cdd:cd07084 256 kTPLVEKLKALLARRKLEDLL----LGPVQTFTTLAMIahMENLL-GSVLLFSGKELKNHSIpsiygacvASALFVPIDE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 327 ---TEPVMQEEIFGPILPIVTVRSLDEA--IDFINRREKPLALYTFSNSSQVVKQVLARTSSGGfcgndgfmhliltSLP 401
Cdd:cd07084 331 ilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAG-------------RTY 397
|
330
....*....|....*.
gi 946758581 402 FGGVGASGM--GSYHG 415
Cdd:cd07084 398 AILRGRTGVapNQNHG 413
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
4-428 |
4.81e-22 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 98.75 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 4 FEDTLQRLREAFSSGRTRPAEFRAAQLKGLGRFLQDNKQLLQEALAQDLRKSAFES--EVSEIsisqgeINlalrnlraw 81
Cdd:PLN02315 58 YEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGigEVQEI------ID--------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 82 MKDETVpkNLATQLDSAFIRKE-----------PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLK--PSE--ISKNT 146
Cdd:PLN02315 123 MCDFAV--GLSRQLNGSIIPSErpnhmmmevwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIAM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 147 ERVLVEVLPRY-LDRSCFAVVLGGpAETGQLL--EHKFDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNC 223
Cdd:PLN02315 201 TKLVAEVLEKNnLPGAIFTSFCGG-AEIGEAIakDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 224 DAQTVANRVAFFRYFNAGQTCVAPDYILCSPEMQERLVPALQSAITRFYGEDPRASPDL--------GRIVSEKHFQRLR 295
Cdd:PLN02315 280 DIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLlgplhtpeSKKNFEKGIEIIK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 296 GllGCGRVAIGGQSEESD-RYIAPTVlVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVV 374
Cdd:PLN02315 360 S--QGGKILTGGSAIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETI 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 946758581 375 KQVLARTSSGgfCGndgfmhLILTSLP---------FGGVGASGMGSYHGKFSFDTFSHHRAC 428
Cdd:PLN02315 437 FKWIGPLGSD--CG------IVNVNIPtngaeiggaFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
85-424 |
7.11e-20 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 92.50 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 85 ETVPkNLATQLDSAFIRkEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEV-LPRYLDRSCF 163
Cdd:PLN02419 232 EYLP-NVSNGVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 164 AVVLGGPAETGQLLEHK-FDYIFFTGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYV--DDNCDAQTVANRVAFFRyfNA 240
Cdd:PLN02419 310 NIVHGTNDTVNAICDDEdIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVlpDANIDATLNALLAAGFG--AA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 241 GQTCVAPDYILC---SPEMQERLVPALQsAITRFYGEDPRAspDLGRIVSEKHFQRLRGLLGCG-----RVAIGGQS--- 309
Cdd:PLN02419 388 GQRCMALSTVVFvgdAKSWEDKLVERAK-ALKVTCGSEPDA--DLGPVISKQAKERICRLIQSGvddgaKLLLDGRDivv 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 310 --EESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSGGFc 387
Cdd:PLN02419 465 pgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQI- 543
|
330 340 350
....*....|....*....|....*....|....*....
gi 946758581 388 GNDGFMHLILTSLPFGGVGASGMG--SYHGKFSFDTFSH 424
Cdd:PLN02419 544 GINVPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-411 |
2.39e-19 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 91.57 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNTERVLVEVlpryldrscfavvlGGPAETGQLL-- 177
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRILLEA--------------GVPAGVVQLLpg 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 178 -----------EHKFDYIFFTGSPRVGKIVMAAAAKHL------TPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNA 240
Cdd:PRK11809 834 rgetvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 241 GQTCVAPDyILCSPE-MQERLVPALQSAITRFYGEDP-RASPDLG-------RIVSEKHFQRLRgllGCGRV---AIGGQ 308
Cdd:PRK11809 914 GQRCSALR-VLCLQDdVADRTLKMLRGAMAECRMGNPdRLSTDIGpvidaeaKANIERHIQAMR---AKGRPvfqAAREN 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 309 SEESDR--YIAPTV--LVDVQEtepvMQEEIFGPILPIVTVRS--LDEAIDFINRREKPLALYTFSNSSQVVKQVLARTS 382
Cdd:PRK11809 990 SEDWQSgtFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAH 1065
|
330 340
....*....|....*....|....*....
gi 946758581 383 SGGFCGNDGFMHLILTSLPFGGVGASGMG 411
Cdd:PRK11809 1066 VGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
103-411 |
3.52e-16 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 81.45 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNTERVLVEV-LPRyldrSCFAVVLGGPAETGQLL 177
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEqtplIAARAVRLLHEAgVPK----DALQLLPGDGRTVGAAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 178 --EHKFDYIFFTGSPRVGKIVMAAAAKHLT-PVTL--ELGGKNPCYVDDNCDA-QTVANRVA-FFRyfNAGQTCVAPDyI 250
Cdd:PRK11905 751 vaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSALPeQVVADVIAsAFD--SAGQRCSALR-V 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 251 LCspeMQE----RLVPALQSAITRFYGEDP-RASPDLGRIVSEK-------HFQRLRGLlGCG--RVAIGGQSEESdRYI 316
Cdd:PRK11905 828 LC---LQEdvadRVLTMLKGAMDELRIGDPwRLSTDVGPVIDAEaqanieaHIEAMRAA-GRLvhQLPLPAETEKG-TFV 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 317 APTVLvdvqETE--PVMQEEIFGPILPIVTVRS--LDEAIDFINRREKPLalyTF---SNSSQVVKQVLARTSSGGFCGN 389
Cdd:PRK11905 903 APTLI----EIDsiSDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGL---TFglhSRIDETIAHVTSRIRAGNIYVN 975
|
330 340
....*....|....*....|..
gi 946758581 390 DGFMHLILTSLPFGGVGASGMG 411
Cdd:PRK11905 976 RNIIGAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
104-377 |
1.55e-15 |
|
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: 79.06 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 104 PFGLVLIIA-----PWN-YPlnltlvPLVGALAAGNCVVLKPSEIS----KNTERVLVEVLPRY-LDRSCFAVVLGGPAE 172
Cdd:cd07127 193 PRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPHPAAilplAITVQVAREVLAEAgFDPNLVTLAADTPEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 173 --TGQLLEH-KFDYIFFTGSPRVGKIVMAAAAKHLtpVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGQTCVAPDY 249
Cdd:cd07127 267 piAQTLATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 250 ILCSPE----MQERLVP-----ALQSAITRFYGEDPRASPDLGRIVSEKHFQRLRGLLGCGRVAIGGQSEESDRYI---- 316
Cdd:cd07127 345 IYVPRDgiqtDDGRKSFdevaaDLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPdarv 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 946758581 317 -APTVLVDVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINR--REK-PLALYTFSNSSQVVKQV 377
Cdd:cd07127 425 rTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERV 489
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
100-357 |
3.17e-14 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 75.24 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEiskNTERVlvevlpryldrSCFAVVL----GGPAETGQ 175
Cdd:PRK11904 680 LRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE---QTPLI-----------AAEAVKLlheaGIPKDVLQ 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 176 LL-------------EHKFDYIFFTGSPRVGKIV-MAAAAKHLTPVTL--ELGGKNPCYVDDNCDAQTVANRV---AFfr 236
Cdd:PRK11904 746 LLpgdgatvgaaltaDPRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVvtsAF-- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 237 yFNAGQTCVAPDyILCSPE-MQERLVPALQSAItrfyGE----DPR-ASPDLGRIVS-------EKHFQRLR--GLLGCg 301
Cdd:PRK11904 824 -RSAGQRCSALR-VLFVQEdIADRVIEMLKGAM----AElkvgDPRlLSTDVGPVIDaeakanlDAHIERMKreARLLA- 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 946758581 302 RVAIGGQSEESDrYIAPTvLVDVQETEpVMQEEIFGPILPIVTVRS--LDEAIDFINR 357
Cdd:PRK11904 897 QLPLPAGTENGH-FVAPT-AFEIDSIS-QLEREVFGPILHVIRYKAsdLDKVIDAINA 951
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
104-359 |
4.58e-13 |
|
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: 70.65 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 104 PFGLVLIIAPWNYPLNLTLVplvG-----ALAAGNCVVLK--PS--EISKNTERVLVEVLPRY-LDRSCFAVVLGGPAET 173
Cdd:cd07129 105 PLGPVAVFGASNFPLAFSVA---GgdtasALAAGCPVVVKahPAhpGTSELVARAIRAALRATgLPAGVFSLLQGGGREV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 174 GQ-LLEH-KFDYIFFTGSPRVGKIVMAAAAKHLT--PVTLELGGKNPCYV-----DDNCD--AQTVANRVAFfryfNAGQ 242
Cdd:cd07129 182 GVaLVKHpAIKAVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFIlpgalAERGEaiAQGFVGSLTL----GAGQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 243 TCVAPDYILC--SPEmQERLVPALQSAItrfygedpRASPDL----GRIVS--EKHFQRLRGLLGcGRVAIGGQSEESDR 314
Cdd:cd07129 258 FCTNPGLVLVpaGPA-GDAFIAALAEAL--------AAAPAQtmltPGIAEayRQGVEALAAAPG-VRVLAGGAAAEGGN 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 946758581 315 YIAPTVL-VDVQE--TEPVMQEEIFGPILPIVTVRSLDEAIDFINRRE 359
Cdd:cd07129 328 QAAPTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
106-409 |
8.62e-13 |
|
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: 70.31 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 106 GLVLIIAPWNYP---LNLTLVPlvgALAaGNCVVLKPSEISKNTERVLVEVLpryldRSC--------FaVVLGGPAETG 174
Cdd:cd07123 172 GFVYAVSPFNFTaigGNLAGAP---ALM-GNVVLWKPSDTAVLSNYLVYKIL-----EEAglppgvinF-VPGDGPVVGD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 175 QLLEHK-FDYIFFTGSPRVGKIVMAAAAKHLT-----P-VTLELGGKNPCYVDDNCDAQTVAN---RVAFfRYfnAGQTC 244
Cdd:cd07123 242 TVLASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTatvRGAF-EY--QGQKC 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 245 VA------PDYILcsPEMQERLVPALQSaITrfYGEDPRASPDLGRIVSEKHFQRLRGLLGCGR------VAIGGQSEES 312
Cdd:cd07123 319 SAasrayvPESLW--PEVKERLLEELKE-IK--MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCDDS 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 313 DRY-IAPTVLVDVQETEPVMQEEIFGPILpivTV-----RSLDEAIDFINRREkPLALyT---FSNSSQVVKQVLA--RT 381
Cdd:cd07123 394 VGYfVEPTVIETTDPKHKLMTEEIFGPVL---TVyvypdSDFEETLELVDTTS-PYAL-TgaiFAQDRKAIREATDalRN 468
|
330 340
....*....|....*....|....*...
gi 946758581 382 SSGGFCGNDGFMHLILTSLPFGGVGASG 409
Cdd:cd07123 469 AAGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
90-356 |
3.34e-12 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 68.81 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNTERVLVEV-LPryldRSCFA 164
Cdd:COG4230 666 AQARRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEqtplIAARAVRLLHEAgVP----ADVLQ 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 165 VVLGGPAETGQLL--EHKFDYIFFTGSPRVGKIV-MAAAAKHLTPVTL--ELGGKNPCYVDDNcdA---QTVANRV--AF 234
Cdd:COG4230 742 LLPGDGETVGAALvaDPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSS--AlpeQVVDDVLasAF 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 235 fryFNAGQTCVAPDyILCSPE-MQERLVPALQSAItrfyGE----DP-RASPDLGRIVS-------EKHFQRLRGLlgcG 301
Cdd:COG4230 820 ---DSAGQRCSALR-VLCVQEdIADRVLEMLKGAM----AElrvgDPaDLSTDVGPVIDaearanlEAHIERMRAE---G 888
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 946758581 302 R-VAIGGQSEESDR--YIAPTV--LVDVQEtepvMQEEIFGPILPIVTVRS--LDEAIDFIN 356
Cdd:COG4230 889 RlVHQLPLPEECANgtFVAPTLieIDSISD----LEREVFGPVLHVVRYKAdeLDKVIDAIN 946
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
48-384 |
1.11e-10 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 63.67 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 48 LAQDLRKSAFES-------EVSEISISQ--GEI--------NLALRNLRAWMKDETVPKNLATQLDSAFirKEPFGLVLI 110
Cdd:cd07126 71 VAHELRKPEVEDffarliqRVAPKSDAQalGEVvvtrkfleNFAGDQVRFLARSFNVPGDHQGQQSSGY--RWPYGPVAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 111 IAPWNYPLNLTLVPLVGALAAGNCVVLK-PSEISknterVLVEVLPRYLDR------SCFAVVLGGPAETGQLLEHKFDY 183
Cdd:cd07126 149 ITPFNFPLEIPALQLMGALFMGNKPLLKvDSKVS-----VVMEQFLRLLHLcgmpatDVDLIHSDGPTMNKILLEANPRM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 184 IFFTGSPRV---------GKIVMAAAA---KHLTPVTLELGgknpcYVDDNCDAQTvanrvaffrYFNAGQTCVAPDyIL 251
Cdd:cd07126 224 TLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA---------YACSGQKCSAQS-IL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 252 CSPE--MQERLVPALQSAITRFYGEDPRASPDLG----RIVSekHFQRLRGLLGcGRVAIGGQ------------SEESD 313
Cdd:cd07126 289 FAHEnwVQAGILDKLKALAEQRKLEDLTIGPVLTwtteRILD--HVDKLLAIPG-AKVLFGGKpltnhsipsiygAYEPT 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 946758581 314 RYIAPTVLVDVQETEPVMQEEIFGPiLPIVTV---RSLDEAIDFINRREKPLALYTFSNSSQVVKQVLARTSSG 384
Cdd:cd07126 366 AVFVPLEEIAIEENFELVTTEVFGP-FQVVTEykdEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
104-353 |
1.90e-08 |
|
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: 56.48 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRYLDRSC----FAVVLGGP--AETGQLL 177
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGgpdnLVVTVEEPtiETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 178 EH-KFDYIFFTGSPRVGKIVMAAAAKhltpvTLELGGKNP-CYVDDNCDAQTVANRVAFFRYFNAGQTC----------- 244
Cdd:cd07121 177 AHpDINLLVVTGGPAVVKAALSSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVQGASFDNNLPCiaekeviavds 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 245 VAPD----------YILCSPEMQERLVPALQsaitrfYGEDPRASPDL-GRIVSEkhfqrlrgLLGcgrvAIGGQSEESD 313
Cdd:cd07121 252 VADYliaamqrngaYVLNDEQAEQLLEVVLL------TNKGATPNKKWvGKDASK--------ILK----AAGIEVPADI 313
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 946758581 314 RYIaptvLVDVQETEPVMQEEIFGPILPIVTVRSLDEAID 353
Cdd:cd07121 314 RLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
106-378 |
1.34e-06 |
|
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: 50.73 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 106 GLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP-SEISKNTERV---LVE--VLPRyldrSCFAVVLGGpaeTGQLLEH 179
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPaTATAYLTEAVvkdIVEsgLLPE----GALQLICGS---VGDLLDH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 180 --KFDYIFFTGSPRVGKI--VMAAAAKHLTPVTLELGGKNPCYV--DDNCDAQTVAnrvAFFRYF------NAGQTCVAP 247
Cdd:cd07128 219 lgEQDVVAFTGSAATAAKlrAHPNIVARSIRFNAEADSLNAAILgpDATPGTPEFD---LFVKEVaremtvKAGQKCTAI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 248 DYILCSPEMQERLVPALQSAITRFYGEDPRA-SPDLGRIVSEKHFQRLRG----LLGCGRVAIGG------QSEESDR-- 314
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLeGVRMGPLVSREQREDVRAavatLLAEAEVVFGGpdrfevVGADAEKga 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 946758581 315 YIAPTVLV--DVQETEPVMQEEIFGPILPIVTVRSLDEAIDFINRREKPLALYTFSNSSQVVKQVL 378
Cdd:cd07128 376 FFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
103-394 |
3.79e-06 |
|
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: 49.19 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLpryLDRscfAVVLGGPA----------- 171
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLL---LQA---AVAAGAPEnligwidnpsi 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 172 ETGQLLEHK--FDYIFFTGSPRVGKivmaAAAKHLTPVTLELGGKNPCYVDDNCDAQTVANRVAFFRYFNAGqtcvapdy 249
Cdd:cd07081 168 ELAQRLMKFpgIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNG-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 250 ILCSPEMQERLVPALQSAITRFYGEDPraspdlGRIVSEKHFQRLRGLL---GCGRVAIGGQSEESdryIAPTVLVDVQE 326
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEGQG------AYKLTAEELQQVQPVIlknGDVNRDIVGQDAYK---IAAAAGLKVPQ 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 946758581 327 TEPVMqeeifgpilpIVTVRSLDEAIDFINRREKP-LALYTFSNSSQVVKQVLARTSSGGfCGNDGFMH 394
Cdd:cd07081 307 ETRIL----------IGEVTSLAEHEPFAHEKLSPvLAMYRAANFADADAKALALKLEGG-CGHTSAMY 364
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
104-353 |
2.20e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 46.82 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNTERVLVEVLPRyldrscFAVVLGGPAE----------- 172
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNE------AIVAAGGPENlvvtvaeptie 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 173 -TGQLLEH-KFDYIFFTGSPRV-------GKIVMAAAAkhltpvtlelgGKNPCYVDDNCD----AQTVANRVAFfryfn 239
Cdd:PRK15398 203 tAQRLMKHpGIALLVVTGGPAVvkaamksGKKAIGAGA-----------GNPPVVVDETADiekaARDIVKGASF----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 240 agqtcvapDY-ILCSPE----------------MQE----RLVPALQSAITRF-YGEDPRASPDL-GRIVSEkhfqrlrg 296
Cdd:PRK15398 267 --------DNnLPCIAEkevivvdsvadelmrlMEKngavLLTAEQAEKLQKVvLKNGGTVNKKWvGKDAAK-------- 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 946758581 297 LLGcgrvAIGGQSEESDRYIaptvLVDVQETEPVMQEEIFGPILPIVTVRSLDEAID 353
Cdd:PRK15398 331 ILE----AAGINVPKDTRLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
24-232 |
2.34e-04 |
|
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: 43.37 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 24 EFRAAQLKGLGRFLQDNKQLLQEALAQDLR---KSAFESEVSEISISQGEIN-LALRNLRAWMKDETVPKNLATQLDSAF 99
Cdd:cd07077 16 EQRDLIINAIANALYDTRQRLASEAVSERGayiRSLIANWIAMMGCSESKLYkNIDTERGITASVGHIQDVLLPDNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946758581 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGaLAAGNCVVLKPSEISKNTERVLVEVLPRyldrscfAVVLGGPAETGQLLEH 179
Cdd:cd07077 96 VRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQA-------ADAAHGPKILVLYVPH 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 946758581 180 -------------KFDYIFFTGSPRVGKivmaAAAKH--LTPVTLELGGKNPCYVDDNCDAQTVANRV 232
Cdd:cd07077 168 psdelaeellshpKIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERASGSV 231
|
|
| |
