|
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: 861.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWMKD 84
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFA 164
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 245 VAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGHVAIGGQSDESDRYIAPTVLVDV 324
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 325 QETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGG 404
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 685584907 405 VGASGMGQYHGKFSFDTFSHHRACLLRRPGMEKLNALRYPPHS 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: 698.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWMKD 84
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFA 164
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:cd07087 161 VVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 245 VAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGHVAIGGQSDESDRYIAPTVLVDV 324
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 325 QETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGG 404
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
410 420
....*....|....*....|....*
gi 685584907 405 VGASGMGQYHGKFSFDTFSHHRACL 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: 625.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWMKD 84
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFA 164
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 245 VAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGHVAIGGQSDESDRYIAPTVLVDV 324
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 325 QETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGG 404
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 685584907 405 VGASGMGQYHGKFSFDTFSHHRACLLRRPGMEklNALRYPPHSPRRLRVL 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: 613.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 2 DPFEDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAW 81
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 82 MKDEHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDES 161
Cdd:PTZ00381 87 LKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 162 CFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 242 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC--GHVAIGGQSDESDRYIAPT 319
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 320 VLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLAS 399
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 400 LPFGGVGASGMGQYHGKFSFDTFSHHRACLLRRPGMEKLNALRYPPHSPRRLRVLLVAME 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: 585.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 1 MDPFEDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRA 80
Cdd:cd07135 4 LDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 81 WMKDEHVPKNLATQ-LDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLD 159
Cdd:cd07135 84 WAKDEKVKDGPLAFmFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 160 ESCFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07135 164 PDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 240 AGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC--GHVAIGGQSDESDRYIA 317
Cdd:cd07135 244 AGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 318 PTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTL 397
Cdd:cd07135 324 PTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGV 403
|
410 420 430
....*....|....*....|....*....|
gi 685584907 398 ASLPFGGVGASGMGQYHGKFSFDTFSHHRA 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: 518.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWMKD 84
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFA 164
Cdd:cd07137 82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQT 243
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 244 CVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGHVAI----GGQSDESDRYIAPT 319
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 320 VLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLAS 399
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
410 420 430
....*....|....*....|....*....|
gi 685584907 400 LPFGGVGASGMGQYHGKFSFDTFSHHRACL 429
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
10-429 |
4.54e-178 |
|
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: 505.61 E-value: 4.54e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 10 RLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWMKDEHVPK 89
Cdd:cd07134 6 AQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAVVLGG 169
Cdd:cd07134 86 PLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 170 PQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07134 166 AEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 250 VLCSPEMQERLLPALQSTITRFYGDDP--QSSPNLGRIINQKQFQRLRALL-----GCGHVAIGGQSDESDRYIAPTVLV 322
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIAPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 323 DVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPF 402
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPF 405
|
410 420
....*....|....*....|....*..
gi 685584907 403 GGVGASGMGQYHGKFSFDTFSHHRACL 429
Cdd:cd07134 406 GGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
5-427 |
1.55e-169 |
|
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: 483.91 E-value: 1.55e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDL-HKSAFESELSEVAISQGEITLALRNLRAWMK 83
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 84 DEHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCF 163
Cdd:cd07133 81 PSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 164 AVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 243
Cdd:cd07133 161 AVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 244 CVAPDYVLCSPEMQERLLPALQSTITRFYGDDPqSSPNLGRIINQKQFQRLRALL------GCGHVAIG--GQSDESDRY 315
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLA-DNPDYTSIINERHYARLQGLLedarakGARVIELNpaGEDFAATRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 316 IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHM 395
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHV 399
|
410 420 430
....*....|....*....|....*....|..
gi 685584907 396 TLASLPFGGVGASGMGQYHGKFSFDTFSHHRA 427
Cdd:cd07133 400 AQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-454 |
4.82e-165 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 474.21 E-value: 4.82e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 1 MDPFEDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRA 80
Cdd:PLN02203 5 GETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 81 WMKDEHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDE 160
Cdd:PLN02203 85 WMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 161 SCFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVD---DNCDPQTVANRVAWFRY 237
Cdd:PLN02203 165 KAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 238 FN-AGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGHVAI----GGQSDES 312
Cdd:PLN02203 245 GScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSIDEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 313 DRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGF 392
Cdd:PLN02203 325 KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685584907 393 MHMTLASLPFGGVGASGMGQYHGKFSFDTFSHHRACLLRRPGMEKLnaLRYPPHSPRRLRVL 454
Cdd:PLN02203 405 IQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEFE--FRYPPWNDFKLGFL 464
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
5-430 |
1.19e-133 |
|
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: 392.34 E-value: 1.19e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAfESELSEVAISQGEITLALRNLRAWMKD 84
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPI-EEALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EHVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK-SMEKvLAEVLPRY-LDESC 162
Cdd:cd07078 80 VIPSPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPlTALL-LAELLAEAgLPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 163 FAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:cd07078 156 LNVVTGDGDEVGAaLASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 241 GQTCVAPDYVLCSPEMQERLLPALQSTITRFY-GDDPQSSPNLGRIINQKQFQRLRALL-----GCGHVAIGGQSDESD- 313
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKvGNPLDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGk 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 314 -RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGF 392
Cdd:cd07078 316 gYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 685584907 393 MHMTlASLPFGGVGASGMGQYHGKFSFDTFSHHRACLL 430
Cdd:cd07078 396 VGAE-PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
11-454 |
3.60e-124 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 370.15 E-value: 3.60e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 11 LREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWMKDEHVPKN 90
Cdd:PLN02174 19 LRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 91 LATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAVVLGGP 170
Cdd:PLN02174 99 LTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 171 QETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCVAPDY 249
Cdd:PLN02174 179 TETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 250 VLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGHVA----IGGQSDESDRYIAPTVLVDVQ 325
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSdkivYGGEKDRENLKIAPTILLDVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 326 ETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGV 405
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGV 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 685584907 406 GASGMGQYHGKFSFDTFSHHRACLLRrpGMEKLNALRYPPHSPRRLRVL 454
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAVLYR--SLFGDSAVRYPPYSRGKLRLL 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
12-430 |
1.75e-107 |
|
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: 323.41 E-value: 1.75e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESeLSEVAISQGEITLALRNLRAWMKDEHVPKNL 91
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 92 ATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGP 170
Cdd:cd06534 83 GGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 171 QETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:cd06534 160 DEVGAaLLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 249 YVLCSPEMQERLLPALQstitrfygddpqsspnlgriinqkqfqrlrallgcghvaiggqsdesdryiapTVLVDVQETE 328
Cdd:cd06534 240 RLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDPDM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 329 PVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTlASLPFGGVGAS 408
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVG-PEAPFGGVKNS 345
|
410 420
....*....|....*....|..
gi 685584907 409 GMGQYHGKFSFDTFSHHRACLL 430
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
12-424 |
7.86e-103 |
|
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: 315.14 E-value: 7.86e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESelsevaisQGEITLALRNLRAW------MKDE 85
Cdd:COG1012 53 RAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA--------RGEVDRAADFLRYYagearrLYGE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 86 HVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFA 164
Cdd:COG1012 125 TIPSDAPGTR--AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:COG1012 203 VVTGDGSEVGAaLVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 243 TCVAPDYVLC----SPEMQERLLPALQSTItrfYGDDPQSSPNLGRIINQKQFQRLRALLGCG-----HVAIGGQ--SDE 311
Cdd:COG1012 283 RCTAASRLLVhesiYDEFVERLVAAAKALK---VGDPLDPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRrpDGE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 312 SDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDG 391
Cdd:COG1012 360 GGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDG 439
|
410 420 430
....*....|....*....|....*....|...
gi 685584907 392 FMHMtLASLPFGGVGASGMGQYHGKFSFDTFSH 424
Cdd:COG1012 440 TTGA-VPQAPFGGVKQSGIGREGGREGLEEYTE 471
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-423 |
1.33e-89 |
|
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: 280.57 E-value: 1.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESElsevaisqGEITLALRNLRAW------MKDE 85
Cdd:pfam00171 39 RAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR--------GEVDRAIDVLRYYaglarrLDGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 86 HVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS-KSMEKvLAEVLPRY-LDESCF 163
Cdd:pfam00171 111 TLPSDPGRL---AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTpLTALL-LAELFEEAgLPAGVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 164 AVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:pfam00171 187 NVVTGSGAEVGEaLVEHpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 242 QTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRALL-----GCGHVAIGGQSDESD-R 314
Cdd:pfam00171 267 QVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgY 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 315 YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMH 394
Cdd:pfam00171 347 FVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTG 426
|
410 420
....*....|....*....|....*....
gi 685584907 395 mTLASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:pfam00171 427 -DADGLPFGGFKQSGFGREGGPYGLEEYT 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-427 |
5.25e-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: 268.32 E-value: 5.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 6 DTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAfeselsevAISQGEITLALRNLRAW---- 81
Cdd:cd07099 22 AAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR--------ADAGLEVLLALEAIDWAarna 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 82 ---MKDEHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEI----SKSMEKVLAEVL 154
Cdd:cd07099 94 prvLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVtplvGELLAEAWAAAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 155 PrylDESCFAVVLGGpQETGQ-LLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVA 233
Cdd:cd07099 174 P---PQGVLQVVTGD-GATGAaLIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 234 WFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLR-----ALLGCGHVAIGG 307
Cdd:cd07099 250 WGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRrhvddAVAKGAKALTGG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 308 -QSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07099 330 aRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAV 409
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 685584907 387 CGNDGFMHMTLASLPFGGVGASGMGQYHGKFSFDTFSHHRA 427
Cdd:cd07099 410 SINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
10-416 |
4.94e-69 |
|
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: 227.18 E-value: 4.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 10 RLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWMKDEHVPK 89
Cdd:cd07098 26 AARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS--------KSMEKVLAEvlpRYLDES 161
Cdd:cd07098 106 GLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVawssgfflSIIRECLAA---CGHDPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 162 CFAVVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANrvAWFR--YF 238
Cdd:cd07098 183 LVQLVTCLPETAEALTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIAS--IIMRgtFQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 239 NAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRALLG----------CGHVAIGG 307
Cdd:cd07098 261 SSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVAdavekgarllAGGKRYPH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 308 QSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFC 387
Cdd:cd07098 341 PEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVA 420
|
410 420 430
....*....|....*....|....*....|
gi 685584907 388 GND-GFMHMtLASLPFGGVGASGMGQYHGK 416
Cdd:cd07098 421 INDfGVNYY-VQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
26-424 |
2.22e-66 |
|
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: 219.32 E-value: 2.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 26 RAAQLRGLGRFLHENKQLLHDALAQD----LHKSAFESELSeVAISQGEITLALRnlrawMKDEHVPKNLATQLdsAFIR 101
Cdd:cd07104 24 RAAILRKAAEILEERRDEIADWLIREsgstRPKAAFEVGAA-IAILREAAGLPRR-----PEGEILPSDVPGKE--SMVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 102 KEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE---ISKSMekVLAEV-----LPryldESCFAVVLGGPQET 173
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrtpVTGGL--LIAEIfeeagLP----KGVLNVVPGGGSEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 174 GQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL 251
Cdd:cd07104 170 GDaLVEHpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 252 CSPEMQERLLPALQSTITRF-YGD--DPQSSpnLGRIINQKQFQRLRALL------GcGHVAIGGQSDesDRYIAPTVLV 322
Cdd:cd07104 250 VHESVYDEFVEKLVAKAKALpVGDprDPDTV--IGPLINERQVDRVHAIVedavaaG-ARLLTGGTYE--GLFYQPTVLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 323 DVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHmTLASLPF 402
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVN-DEPHVPF 403
|
410 420
....*....|....*....|..
gi 685584907 403 GGVGASGMGQYHGKFSFDTFSH 424
Cdd:cd07104 404 GGVKASGGGRFGGPASLEEFTE 425
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
13-411 |
5.82e-66 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 218.84 E-value: 5.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 13 EAFHTGRTRSAEFRAAQLRGLGRFLHENKqllhDALAQDLH----KSafeseLSEvaiSQGEITLALRNLRaWMKDE--- 85
Cdd:cd07103 30 AAFKTWRKTTARERAAILRRWADLIRERA----EDLARLLTleqgKP-----LAE---ARGEVDYAASFLE-WFAEEarr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 86 ----HVPKNLATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDE 160
Cdd:cd07103 97 iygrTIPSPAPGK--RILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 161 SCFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYF 238
Cdd:cd07103 175 GVLNVVTGSPAEIGEaLCASpRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 239 NAGQTCVAPD--YVLCS--PEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRAL----LGCG-HVAIGGQS 309
Cdd:cd07103 255 NAGQTCVCANriYVHESiyDEFVEKLVERVKKLKV---GNGLDEGTDMGPLINERAVEKVEALvedaVAKGaKVLTGGKR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 310 DESD-RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG--GF 386
Cdd:cd07103 332 LGLGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGmvGI 411
|
410 420
....*....|....*....|....*
gi 685584907 387 cgNDGFmhMTLASLPFGGVGASGMG 411
Cdd:cd07103 412 --NTGL--ISDAEAPFGGVKESGLG 432
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
12-427 |
3.87e-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: 214.03 E-value: 3.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAF-HTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEI-TLALRNLRAWMKDEHVPK 89
Cdd:cd07089 29 RRAFdTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLrYFADLADSFPWEFDLPVP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVlpryLDES-----CFA 164
Cdd:cd07089 109 ALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEI----IAETdlpagVVN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:cd07089 185 VVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 243 TCVAPDYVLCSPEMQERLLPALQSTITRF-YGD--DPqsSPNLGRIINQKQFQRLRALLGCGH------VAIGGQSDESD 313
Cdd:cd07089 265 GCALTTRLLVPRSRYDEVVEALAAAFEALpVGDpaDP--GTVMGPLISAAQRDRVEGYIARGRdegarlVTGGGRPAGLD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 314 R--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdG 391
Cdd:cd07089 343 KgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-G 421
|
410 420 430
....*....|....*....|....*....|....*.
gi 685584907 392 FMHMtLASLPFGGVGASGMGQYHGKFSFDTFSHHRA 427
Cdd:cd07089 422 GGGY-GPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
12-416 |
4.60e-64 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 213.54 E-value: 4.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSafeselseVAISQGEITLALrnlrAWMK-------- 83
Cdd:cd07106 29 KAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKP--------LAEAQFEVGGAV----AWLRytasldlp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 84 DEHVPKNlATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS-----KSMEkVLAEVLPRyl 158
Cdd:cd07106 97 DEVIEDD-DTR--RVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTplctlKLGE-LAQEVLPP-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 159 descfAV--VLGGPQETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAW 234
Cdd:cd07106 171 -----GVlnVVSGGDELGPALtSHpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFW 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 235 FRYFNAGQTCVAPD--YVlcsPEMQ-ERLLPALQSTITRFY-GDDPQSSPNLGRIINQKQFQRLRALL-----GCGHVAI 305
Cdd:cd07106 246 GAFINSGQVCAAIKrlYV---HESIyDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 306 GGQSDESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07106 323 GGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAG 402
|
410 420 430
....*....|....*....|....*....|...
gi 685584907 385 GFCGNdgfMHMTLA-SLPFGGVGASGMGQYHGK 416
Cdd:cd07106 403 TVWIN---THGALDpDAPFGGHKQSGIGVEFGI 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-425 |
1.76e-63 |
|
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: 212.11 E-value: 1.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 7 TLRRLREAFHTGRTRSAEFRAAQLRglgRFLhenkqllhDALAQdlHKSAFESELSE-----VAISQGEITLALRnlRAW 81
Cdd:cd07102 23 ALERARAAQKGWRAVPLEERKAIVT---RAV--------ELLAA--NTDEIAEELTWqmgrpIAQAGGEIRGMLE--RAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 82 MKDEHVPKNLATQLDSA------FIRKEPFGLVLIIAPWNYPLnLTLV-PLVGALAAGNCVVLKPSE----ISKSMEKVL 150
Cdd:cd07102 88 YMISIAEEALADIRVPEkdgferYIRREPLGVVLIIAPWNYPY-LTAVnAVIPALLAGNAVILKHSPqtplCGERFAAAF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 151 AEV-LPRYLdescFAVVLGGPQETGQLL-EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTV 228
Cdd:cd07102 167 AEAgLPEGV----FQVLHLSHETSAALIaDPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 229 ANRVAWFRYFNAGQTCvapdyvlCSPE-------MQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLR----- 295
Cdd:cd07102 243 AESLVDGAFFNSGQSC-------CSIEriyvhesIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRaqiad 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 296 ALLGCGHVAIGGQ----SDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSS 371
Cdd:cd07102 316 AIAKGARALIDGAlfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685584907 372 QVVKRVLTQTSSGGFCGN-----DgfmhmtlASLPFGGVGASGMGQYHGKFSFDTF----SHH 425
Cdd:cd07102 396 ARAEALGEQLETGTVFMNrcdylD-------PALAWTGVKDSGRGVTLSRLGYDQLtrpkSYH 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
97-423 |
7.38e-63 |
|
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: 210.65 E-value: 7.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 97 SAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAVVLGGPQETGQL 176
Cdd:cd07092 111 TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 177 L--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSP 254
Cdd:cd07092 191 LvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 255 EMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRALL----GCGHVAIGGQSDESDRY-IAPTVLVDVQETE 328
Cdd:cd07092 271 SVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTVVAGVAQDD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 329 PVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfmHMTLAS-LPFGGVGA 407
Cdd:cd07092 351 EIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAAeMPHGGFKQ 427
|
330
....*....|....*.
gi 685584907 408 SGMGQYHGKFSFDTFS 423
Cdd:cd07092 428 SGYGKDLSIYALEDYT 443
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-424 |
1.63e-62 |
|
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: 209.90 E-value: 1.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESE--LSEVAIsqgeiTLALRNLRAWM 82
Cdd:cd07110 22 DAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdVDDVAG-----CFEYYADLAEQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 83 KDEHVPKNLATQLD--SAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV-----LP 155
Cdd:cd07110 97 LDAKAERAVPLPSEdfKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 156 RyldeSCFAVVLGGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVA 233
Cdd:cd07110 177 P----GVLNVVTGTGDEAGApLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 234 WFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSP-NLGRIINQKQFQRLRALLGCG-----HVAIGG 307
Cdd:cd07110 253 FGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARGkeegaRLLCGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 308 QSDESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07110 333 RRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAG 412
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 685584907 385 GF---CGNDGFMHmtlasLPFGGVGASGMGQYHGKFSFDTFSH 424
Cdd:cd07110 413 IVwinCSQPCFPQ-----APWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
69-423 |
1.31e-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: 204.87 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 69 GEITLALRNLRAWMKDEHVPKNLATQLDSA----FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK 144
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPSDSPgtvsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 145 SMEKVLAEVLPRY-LDESCFAVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDD 221
Cdd:cd07150 160 VIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 222 NCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLR----- 295
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKrqved 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 296 ALLGCGHVAIGGQSDesDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLalyafsnSSQVVK 375
Cdd:cd07150 320 AVAKGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGL-------SAAILT 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 685584907 376 RVLTQTSSGGFCGNDGFMHMTLASL------PFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHINDPTIldeahvPFGGVKASGFGREGGEWSMEEFT 444
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
12-423 |
6.42e-59 |
|
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: 200.15 E-value: 6.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTR-SAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSafeseLSEvaiSQGEITLALRNLR--AWMKDEHVP 88
Cdd:cd07109 29 RRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKP-----LTQ---ARADVEAAARYFEyyGGAADKLHG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 89 KNLATQLD-SAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVV 166
Cdd:cd07109 101 ETIPLGPGyFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 167 LGGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:cd07109 181 TGLGAEAGAaLVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 245 VAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALL-----GCGHVAIGGQ----SDESDRY 315
Cdd:cd07109 261 SAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRiaegAPAGGYF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 316 IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHM 395
Cdd:cd07109 341 VAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGG 420
|
410 420
....*....|....*....|....*...
gi 685584907 396 TLaSLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07109 421 GI-ELPFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
12-423 |
6.05e-58 |
|
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: 197.56 E-value: 6.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTR--SAEFRAAQLRGLGRFLHENKqllhDALAQdlhksaFESELSEVAISQ--GEITLAL----------RN 77
Cdd:cd07118 29 RKAFDKGPWPrmSGAERAAVLLKVADLIRARR----ERLAL------IETLESGKPISQarGEIEGAAdlwryaaslaRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 78 LRAwmkDEHvpKNLATQLdSAFIRKEPFGLVLIIAPWNYPLnLTL---VPLvgALAAGNCVVLKPSEISKSMEKVLAEVL 154
Cdd:cd07118 99 LHG---DSY--NNLGDDM-LGLVLREPIGVVGIITPWNFPF-LILsqkLPF--ALAAGCTVVVKPSEFTSGTTLMLAELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 155 PRY-LDESCFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANR 231
Cdd:cd07118 170 IEAgLPAGVVNIVTGYGATVGQaMTEHpDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 232 VAWFRYFNAGQTCVAPDYVLCSPEMQERLLPAL--QSTITRFyGD--DPQSspNLGRIINQKQFQRLRALLGCG-----H 302
Cdd:cd07118 250 VVFGVYFNAGECCNSGSRLLVHESIADAFVAAVvaRSRKVRV-GDplDPET--KVGAIINEAQLAKITDYVDAGraegaT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 303 VAIGGQSDESD--RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQ 380
Cdd:cd07118 327 LLLGGERLASAagLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARR 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 685584907 381 TSSGGFCGN---DGFmhmtlASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07118 407 IRAGTVWVNtflDGS-----PELPFGGFKQSGIGRELGRYGVEEYT 447
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-422 |
1.61e-57 |
|
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: 196.95 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHT-GRTRSAEfRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWmkdehvpkN 90
Cdd:cd07138 46 RRAFPAwSATSVEE-RAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDF--------E 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 91 LATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVlpryLDES-----CFAV 165
Cdd:cd07138 117 FEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEI----LDEAglpagVFNL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 166 VLGGPQETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCD-----PQTVANrvawfRYF 238
Cdd:cd07138 193 VNGDGPVVGEALsAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADlekavPRGVAA-----CFA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 239 NAGQTCVAPDYVL----CSPEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRALLGCG-----HVAIGG-- 307
Cdd:cd07138 268 NSGQSCNAPTRMLvprsRYAEAEEIAAAAAEAYVV---GDPRDPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGGpg 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 308 --QSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGG 385
Cdd:cd07138 345 rpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQ 424
|
410 420 430
....*....|....*....|....*....|....*..
gi 685584907 386 FCGNDGFMHMtlaSLPFGGVGASGMGQYHGKFSFDTF 422
Cdd:cd07138 425 VHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
5-422 |
4.81e-57 |
|
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: 194.60 E-value: 4.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSafeseLSEvaiSQGEITLALRNLR----- 79
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKP-----IAE---ARAEVEKCAWICRyyaen 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 80 --AWMKDEHVPknlaTQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEI----SKSMEKVLAEV 153
Cdd:cd07100 74 aeAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNvpgcALAIEELFREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 154 -LPryldESCFAVVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANR 231
Cdd:cd07100 150 gFP----EGVFQNLLIDSDQVEAIIADpRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 232 VAWFRYFNAGQTCVAP----------DyvlcspEMQERLLPALQSTITrfyGDD--------PQSSPNLGRIInQKQFQr 293
Cdd:cd07100 226 AVKGRLQNAGQSCIAAkrfivhedvyD------EFLEKFVEAMAALKV---GDPmdedtdlgPLARKDLRDEL-HEQVE- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 294 lRALLGCGHVAIGGQSDESDR-YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQ 372
Cdd:cd07100 295 -EAVAAGATLLLGGKRPDGPGaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLE 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 685584907 373 VVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGQYHGKFSFDTF 422
Cdd:cd07100 374 RAERVARRLEAGMVFING--MVKSDPRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
12-420 |
2.14e-56 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 193.73 E-value: 2.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISqGEITLALRNLRAWMKDEHVPKNl 91
Cdd:cd07108 29 KAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVL-ADLFRYFGGLAGELKGETLPFG- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 92 ATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAVVLGGPQ 171
Cdd:cd07108 107 PDVL--TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 172 ETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYV--DDNCDpQTVANRVAWFRYFNAGQTCVAP 247
Cdd:cd07108 185 ECGAaLVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQGQSCTAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 248 DYVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCG------HVAIGGQSDESDR-----Y 315
Cdd:cd07108 264 SRLFVHEDIYDAFLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPladgfF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 316 IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHM 395
Cdd:cd07108 344 VQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQ 423
|
410 420
....*....|....*....|....*
gi 685584907 396 tlASLPFGGVGASGMGQyhgKFSFD 420
Cdd:cd07108 424 --PGQSYGGFKQSGLGR---EASLE 443
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
100-411 |
1.73e-55 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 191.66 E-value: 1.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAVVLGGPQETGQ-LLE 178
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDaLVG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 179 HR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQ 257
Cdd:PRK13473 214 HPkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 258 ERL---LPALQSTITrfYGDDPQSSPNLGRIINQKQFQRL-----RAlLGCGHVAI---GGQSDESDRYIAPTVLVDVQE 326
Cdd:PRK13473 294 DDLvakLAAAVATLK--VGDPDDEDTELGPLISAAHRDRVagfveRA-KALGHIRVvtgGEAPDGKGYYYEPTLLAGARQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 327 TEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMhmtLAS-LPFGGV 405
Cdd:PRK13473 371 DDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM---LVSeMPHGGQ 447
|
....*.
gi 685584907 406 GASGMG 411
Cdd:PRK13473 448 KQSGYG 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
96-423 |
7.93e-55 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 188.94 E-value: 7.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 96 DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS-KSME---KVLAEV-LPryldESCFAVVLGGP 170
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSpRTHWligRVFHEAgLP----KGVLNVVTHSP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 171 QE----TGQLLEH---RFdyIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 243
Cdd:cd07105 166 EDapevVEALIAHpavRK--VNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 244 CVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQsspnLGRIINQKQFQRLRAL----LGCG-HVAIGGQSDESDR--YI 316
Cdd:cd07105 244 CMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV----LGSLVSAAAADRVKELvddaLSKGaKLVVGGLADESPSgtSM 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 317 APTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGfcgndgfMH-- 394
Cdd:cd07105 320 PPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA-------VHin 392
|
330 340 350
....*....|....*....|....*....|...
gi 685584907 395 -MTL---ASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07105 393 gMTVhdePTLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-427 |
8.17e-55 |
|
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: 189.57 E-value: 8.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETGQ-L 176
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAaL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 177 LEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPE 255
Cdd:cd07115 192 VEHpDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 256 MQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCGH------VAIGGQSDESDRYIAPTVLVDVQETE 328
Cdd:cd07115 272 IYDEFLERFTSLARSLRPGDPlDPKTQMGPLVSQAQFDRVLDYVDVGReegarlLTGGKRPGARGFFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 329 PVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGAS 408
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT--YNRFDPGSPFGGYKQS 429
|
330
....*....|....*....
gi 685584907 409 GMGQYHGKFSFDTFSHHRA 427
Cdd:cd07115 430 GFGREMGREALDEYTEVKS 448
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
103-423 |
9.50e-55 |
|
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: 189.31 E-value: 9.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV-----LPryldESCFAVVLG-GPqETGQL 176
Cdd:cd07093 116 QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELaneagLP----PGVVNVVHGfGP-EAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 177 L-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCvapdyvLCSp 254
Cdd:cd07093 191 LvAHpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVC------LAG- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 255 emqERLLpaLQSTI-----TRF--------YGDDPQSSPNLGRIINQKQFQRL-----RALLGCGHVAIGGQSDESDR-- 314
Cdd:cd07093 264 ---SRIL--VQRSIydeflERFverakalkVGDPLDPDTEVGPLISKEHLEKVlgyveLARAEGATILTGGGRPELPDle 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 315 ---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDG 391
Cdd:cd07093 339 ggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCW 418
|
330 340 350
....*....|....*....|....*....|...
gi 685584907 392 FM-HMTlasLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07093 419 LVrDLR---TPFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
26-415 |
1.11e-54 |
|
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: 188.66 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 26 RAAQLRGLGRFLHENKQLLHDALAQD----LHKSAFEselseVAISQGEITLAlrnlrawmkdehvpKNLATQ-----LD 96
Cdd:cd07152 37 RAAVLRRAADLLEEHADEIADWIVREsgsiRPKAGFE-----VGAAIGELHEA--------------AGLPTQpqgeiLP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 97 SA-----FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP---SEISKSMekVLAEVLPRY-LDESCFAVVL 167
Cdd:cd07152 98 SApgrlsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdprTPVSGGV--VIARLFEEAgLPAGVLHVLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 168 GGPqETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCV 245
Cdd:cd07152 176 GGA-DAGEaLVEDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 246 APDYVLCSPEMQERLLPALQSTITRFYGDDPQSSP-NLGRIINQKQFQRLRAL------LGcGHVAIGGQSDesDRYIAP 318
Cdd:cd07152 255 AAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIvddsvaAG-ARLEAGGTYD--GLFYRP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 319 TVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfmhmTLA 398
Cdd:cd07152 332 TVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVN 407
|
410 420
....*....|....*....|
gi 685584907 399 S---LPFGGVGASGMGQYHG 415
Cdd:cd07152 408 DephNPFGGMGASGNGSRFG 427
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
5-377 |
5.37e-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: 187.47 E-value: 5.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRL---REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSafeselseVAISQGEITLA---LRNL 78
Cdd:cd07088 35 EDADRAVdaaEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKT--------LSLARVEVEFTadyIDYM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 79 RAW---MKDEHVPKNLATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKsmekVLAEVLP 155
Cdd:cd07088 107 AEWarrIEGEIIPSDRPNE--NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETP----LNALEFA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 156 RYLDES-----CFAVVLGGPQETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTV 228
Cdd:cd07088 181 ELVDEAglpagVLNIVTGRGSVVGDALvAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 229 ANRVAWFRYFNAGQTCVAPD--YVLCS--PEMQERLLPALQSTItrfYGDDPQSSPNLGRIINQKQFQRL-----RALLG 299
Cdd:cd07088 261 VKAIVDSRIINCGQVCTCAErvYVHEDiyDEFMEKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVeemveRAVEA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 300 CGHVAIGGQSDESDR--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRV 377
Cdd:cd07088 338 GATLLTGGKRPEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRA 417
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-411 |
3.20e-53 |
|
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: 185.88 E-value: 3.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTG--RTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESelsevaiSQGEITLALRNLR--AWMKDEHV 87
Cdd:cd07091 51 RAAFETGwwRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES-------AKGDVALSIKCLRyyAGWADKIQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 88 PKNLATQLDS-AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPryldESCFA-- 164
Cdd:cd07091 124 GKTIPIDGNFlAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIK----EAGFPpg 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 ---VVLG-GPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANrVAWFR-Y 237
Cdd:cd07091 200 vvnIVPGfGPTAGAAISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVE-WAAFGiF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 238 FNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFY-GDDPQSSPNLGRIINQKQFQRL----------RALLGCGhvaiG 306
Cdd:cd07091 279 FNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKIlsyiesgkkeGATLLTG----G 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 307 GQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07091 355 ERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTV 434
|
410 420
....*....|....*....|....*
gi 685584907 387 CGNDGfmHMTLASLPFGGVGASGMG 411
Cdd:cd07091 435 WVNTY--NVFDAAVPFGGFKQSGFG 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-423 |
8.48e-53 |
|
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: 184.82 E-value: 8.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTG--RTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESElsevaISQGEITLALR---NLRAWMKDEH 86
Cdd:cd07119 45 RRAFDSGewPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE-----IDIDDVANCFRyyaGLATKETGEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 87 VPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----SMEKVLAEV-LPRyldeS 161
Cdd:cd07119 120 YDVPPHVI---SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPlttiALFELIEEAgLPA----G 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 162 CFAVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07119 193 VVNLVTGSGATVGAELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 240 AGQTCVAPDYVLCSPEMQERLLPALQSTITRF---YGDDPqsSPNLGRIINQKQFQRLRALLGCG-----HVAIGGQSDE 311
Cdd:cd07119 273 AGQVCSAGSRLLVEESIHDKFVAALAERAKKIklgNGLDA--DTEMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKRPT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 312 SDR-----YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07119 351 GDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTV 430
|
410 420 430
....*....|....*....|....*....|....*..
gi 685584907 387 CGNDgfMHMTLASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07119 431 WIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
5-416 |
3.73e-52 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 182.51 E-value: 3.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHK---SAFEsELSEVAISqgeITLALRNLRAW 81
Cdd:cd07101 21 EAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrHAFE-EVLDVAIV---ARYYARRAERL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 82 MKDEHVPKNLATqLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSeiSKSMEKVLAEV-------L 154
Cdd:cd07101 97 LKPRRRRGAIPV-LTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTALTALWAVellieagL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 155 PRYLdescFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVAnRVAW 234
Cdd:cd07101 174 PRDL----WQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAA-AGAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 235 FRYF-NAGQTCVAPD--YVLCS--PEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRAllgcgHVA----- 304
Cdd:cd07101 249 RACFsNAGQLCVSIEriYVHESvyDEFVRRFVARTRALRL---GAALDYGPDMGSLISQAQLDRVTA-----HVDdavak 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 305 -----IGGQS--DESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRV 377
Cdd:cd07101 321 gatvlAGGRArpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 685584907 378 LTQTSSGGFCGNDGFMhMTLASL--PFGGVGASGMGQYHGK 416
Cdd:cd07101 401 AARLRAGTVNVNEGYA-AAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
98-423 |
3.79e-52 |
|
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: 182.42 E-value: 3.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV-----LPryldESCFAVVLGGPQE 172
Cdd:cd07112 118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLP----AGVLNVVPGFGHT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 173 TGQLL-EHR-FDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:cd07112 194 AGEALgLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 249 YVLCSPEMQERLLPALQSTITRFY-GD--DPQSSpnLGRIINQKQFQRLRALLGCGH-----VAIGGQSDESDR---YIA 317
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKpGDplDPATR--MGALVSEAHFDKVLGYIESGKaegarLVAGGKRVLTETggfFVE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 318 PTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNDGFMh 394
Cdd:cd07112 352 PTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVwvnCFDEGDI- 430
|
330 340
....*....|....*....|....*....
gi 685584907 395 mtlaSLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07112 431 ----TTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
96-423 |
5.44e-52 |
|
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: 182.32 E-value: 5.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 96 DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETG 174
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 175 QLL-EHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC 252
Cdd:TIGR01804 205 PLLvNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 253 SPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCG-----HVAIGGQSDESDR-----YIAPTVL 321
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIKLGDPfDEATEMGPLISAAHRDKVLSYIEKGkaegaTLATGGGRPENVGlqngfFVEPTVF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 322 VDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLP 401
Cdd:TIGR01804 365 ADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEAP 442
|
330 340
....*....|....*....|..
gi 685584907 402 FGGVGASGMGQYHGKFSFDTFS 423
Cdd:TIGR01804 443 FGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
5-411 |
8.98e-52 |
|
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: 181.48 E-value: 8.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESeLSEVAISQGEITLALRNLRAwMKD 84
Cdd:cd07094 24 EEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEVDRAIDTLRLAAEEAER-IRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EHVPKNLATQLDS--AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVL-PRYLDES 161
Cdd:cd07094 102 EEIPLDATQGSDNrlAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 162 CFAVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKhlTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07094 182 VLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 240 AGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRL-----RALLGCGHVAIGGQSDesD 313
Cdd:cd07094 260 AGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVerwveEAVEAGARLLCGGERD--G 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 314 RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfM 393
Cdd:cd07094 338 ALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-S 416
|
410
....*....|....*...
gi 685584907 394 HMTLASLPFGGVGASGMG 411
Cdd:cd07094 417 AFRTDWMPFGGVKESGVG 434
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-427 |
7.75e-51 |
|
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: 179.47 E-value: 7.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESelsevaisQGEITLAL----------RNlraw 81
Cdd:cd07131 47 REAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEG--------RGDVQEAIdmaqyaagegRR---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 82 MKDEHVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDE 160
Cdd:cd07131 115 LFGETVPSELPNKD--AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 161 SCFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYF 238
Cdd:cd07131 193 GVVNVVHGRGEEVGEaLVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 239 NAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNL-GRIINQKQFQRL-----------RALLGCGHVAIG 306
Cdd:cd07131 273 TTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDmGPLINEAQLEKVlnyneigkeegATLLLGGERLTG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 307 GQSDESdRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07131 353 GGYEKG-YFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGIT 431
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 685584907 387 CGNDGfmhmTL---ASLPFGGVGASGMGQYH-GKFSFDTFSHHRA 427
Cdd:cd07131 432 YVNAP----TIgaeVHLPFGGVKKSGNGHREaGTTALDAFTEWKA 472
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
98-427 |
1.39e-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: 178.76 E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETGQ- 175
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSa 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 176 LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSP 254
Cdd:cd07144 218 LAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 255 EMQERLLPALQSTITRFY--GDDPQSSPNLGRIINQKQFQRLRALLGCGH------VAIG---GQSDESDRYIAPTVLVD 323
Cdd:cd07144 298 SIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKkegaklVYGGekaPEGLGKGYFIPPTIFTD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 324 VQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNDGFMHMtlasl 400
Cdd:cd07144 378 VPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSNDSDVGV----- 452
|
330 340
....*....|....*....|....*..
gi 685584907 401 PFGGVGASGMGQYHGKFSFDTFSHHRA 427
Cdd:cd07144 453 PFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-411 |
1.63e-50 |
|
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: 177.79 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 8 LRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSafeselseVAISQGEITLALRNLR------AW 81
Cdd:cd07149 27 IAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETLRlsaeeaKR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 82 MKDEHVPknlatqLDS--------AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV 153
Cdd:cd07149 99 LAGETIP------FDAspggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 154 LPR-YLDESCFAVVLGGPQETG-QLLEH-RFDYIFFTGSPRVGKIVMTAAAkhLTPVTLELGGKNPCYVDDNCDPQTVAN 230
Cdd:cd07149 173 LLEaGLPKGALNVVTGSGETVGdALVTDpRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 231 RVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRL-----RALLGCGHVA 304
Cdd:cd07149 251 RCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIeewveEAVEGGARLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 305 IGGQSDEsdRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07149 331 TGGKRDG--AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVG 408
|
410 420 430
....*....|....*....|....*....|.
gi 685584907 385 GFCGNDG----FMHMtlaslPFGGVGASGMG 411
Cdd:cd07149 409 GVMINDSstfrVDHM-----PYGGVKESGTG 434
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
12-423 |
2.25e-49 |
|
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: 175.05 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTG--RTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSafeseLSEVaisQGEITLALRNLR--AWMKDEH- 86
Cdd:cd07114 29 RAAFEGGawRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL-----IRET---RAQVRYLAEWYRyyAGLADKIe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 87 ---VPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV-----LPRYL 158
Cdd:cd07114 101 gavIPVDKGDYL--NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 159 descFAVVLGGPQETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFR 236
Cdd:cd07114 179 ----VNVVTGFGPETGEALvEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 237 YFNAGQTCVAPDYVLCSPEMQERLLPALqSTITRF--YGDDPQSSPNLGRIINQKQFQRLRALLG----------CGHVA 304
Cdd:cd07114 255 FAAAGQTCVAGSRLLVQRSIYDEFVERL-VARARAirVGDPLDPETQMGPLATERQLEKVERYVArareegarvlTGGER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 305 IGGQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07114 334 PSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAG 413
|
410 420 430
....*....|....*....|....*....|....*....
gi 685584907 385 GFCGNDgfMHMTLASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07114 414 TVWVNT--YRALSPSSPFGGFKDSGIGRENGIEAIREYT 450
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
5-411 |
4.42e-49 |
|
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: 174.08 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEF-RAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESelsevaisQGEITLALRNLRAWMK 83
Cdd:cd07146 20 EEALREALALAASYRSTLTRYqRSAILNKAAALLEARREEFARLITLESGLCLKDT--------RYEVGRAADVLRFAAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 84 D------EHVPKNLATQLDS--AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLP 155
Cdd:cd07146 92 EalrddgESFSCDLTANGKArkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 156 RY-LDESCFAVVLGGPQETGQLLEH--RFDYIFFTGSPRVGK-IVMTAAAKHLTpvtLELGGKNPCYVDDNCDPQTVANR 231
Cdd:cd07146 172 EAgLPPDMLSVVTGEPGEIGDELIThpDVDLVTFTGGVAVGKaIAATAGYKRQL---LELGGNDPLIVMDDADLERAATL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 232 VAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQK---QFQR--LRALLGCGHVAI 305
Cdd:cd07146 249 AVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDEEaaiQIENrvEEAIAQGARVLL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 306 GGQSDESdrYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGG 385
Cdd:cd07146 329 GNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGT 406
|
410 420
....*....|....*....|....*.
gi 685584907 386 FCGNDGfMHMTLASLPFGGVGASGMG 411
Cdd:cd07146 407 VNVNEV-PGFRSELSPFGGVKDSGLG 431
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-422 |
9.48e-49 |
|
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: 173.53 E-value: 9.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTG---RTRSAEfRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWMKDEHVP 88
Cdd:cd07139 46 RRAFDNGpwpRLSPAE-RAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 89 knlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV-----LPryldESCF 163
Cdd:cd07139 125 ---GSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAaeeagLP----PGVV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 164 AVVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:cd07139 198 NVVPADREVGEYLVRHpGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 243 TCVAPDYVLCSPEMQERLLPALQSTITRF-YGD--DPqsSPNLGRIINQKQFQRLR----------ALLGCGhvaiGGQS 309
Cdd:cd07139 278 VCVALTRILVPRSRYDEVVEALAAAVAALkVGDplDP--ATQIGPLASARQRERVEgyiakgraegARLVTG----GGRP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 310 DESDR--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFC 387
Cdd:cd07139 352 AGLDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVG 431
|
410 420 430
....*....|....*....|....*....|....*
gi 685584907 388 GNDGFMHMtlaSLPFGGVGASGMGQYHGKFSFDTF 422
Cdd:cd07139 432 VNGFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-423 |
1.58e-48 |
|
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: 172.87 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 26 RAAQLRGLGRFLHENKQLLHDALAQDLH----KSAFESELSeVAISQGEITLALRnlrawMKDEHVPKNLATQldSAFIR 101
Cdd:cd07151 56 RAEILEKAAQILEERRDEIVEWLIRESGstriKANIEWGAA-MAITREAATFPLR-----MEGRILPSDVPGK--ENRVY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 102 KEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE---ISKSMekVLAEVLPRY-LDESCFAVVLGGPQETG-QL 176
Cdd:cd07151 128 REPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASdtpITGGL--LLAKIFEEAgLPKGVLNVVVGAGSEIGdAF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 177 LEHRF-DYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPE 255
Cdd:cd07151 206 VEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHED 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 256 MQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRL-----RALLGCGHVAIGGQSDesDRYIAPTVLVDVQETEP 329
Cdd:cd07151 286 VYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLldkieQAVEEGATLLVGGEAE--GNVLEPTVLSDVTNDME 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 330 VMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHmTLASLPFGGVGASG 409
Cdd:cd07151 364 IAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEPHVPFGGEKNSG 442
|
410
....*....|....
gi 685584907 410 MGQYHGKFSFDTFS 423
Cdd:cd07151 443 LGRFNGEWALEEFT 456
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-422 |
1.88e-48 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 173.34 E-value: 1.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESeLSEVAISQGEITlalrnlraWMKD 84
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEA-IGEVAYGASFLE--------YFAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EH-------VPKNLA-TQLdsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPR 156
Cdd:PLN02278 136 EAkrvygdiIPSPFPdRRL---LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 157 Y-LDESCFAVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVA 233
Cdd:PLN02278 213 AgIPPGVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 234 WFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRA------------LLGC 300
Cdd:PLN02278 293 ASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVEShvqdavskgakvLLGG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 301 GHVAIGGQsdesdrYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQ 380
Cdd:PLN02278 373 KRHSLGGT------FYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEA 446
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 685584907 381 TSSGGFCGNDGFMHMTLAslPFGGVGASGMGQYHGKFSFDTF 422
Cdd:PLN02278 447 LEYGIVGVNEGLISTEVA--PFGGVKQSGLGREGSKYGIDEY 486
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
9-415 |
2.19e-48 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 173.91 E-value: 2.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 9 RRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDaLAQ----DLHKSAFEsELSEVAISQGEItlaLRNLRAWMKD 84
Cdd:PRK09407 61 ARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLD-LVQletgKARRHAFE-EVLDVALTARYY---ARRAPKLLAP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EHVPKNLATqLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSeiSKSMEKVLAEV-------LPRY 157
Cdd:PRK09407 136 RRRAGALPV-LTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTPLTALAAVellyeagLPRD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 158 LdescFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY 237
Cdd:PRK09407 213 L----WQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 238 FNAGQTCVAPD--YVLCS--PEMQERLLPALQS-TITRFYGDDPQsspnLGRIINQKQFQRLRAllgcgHVA-------- 304
Cdd:PRK09407 289 SNAGQLCISIEriYVHESiyDEFVRAFVAAVRAmRLGAGYDYSAD----MGSLISEAQLETVSA-----HVDdavakgat 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 305 --IGGQS--DESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINrrEKPLALYA--FSNSSQVVKRVL 378
Cdd:PRK09407 360 vlAGGKArpDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN--DTPYGLNAsvWTGDTARGRAIA 437
|
410 420 430
....*....|....*....|....*....|....*....
gi 685584907 379 TQTSSGGFCGNDGFMhMTLASL--PFGGVGASGMGQYHG 415
Cdd:PRK09407 438 ARIRAGTVNVNEGYA-AAWGSVdaPMGGMKDSGLGRRHG 475
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-411 |
4.07e-48 |
|
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: 172.05 E-value: 4.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSafeseLSEvaiSQGEITLALRNLR-----AW-MKDE 85
Cdd:cd07097 47 AAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKT-----LPE---ARGEVTRAGQIFRyyageALrLSGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 86 HVP---KNLatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDES 161
Cdd:cd07097 119 TLPstrPGV-----EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 162 CFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07097 194 VFNLVMGSGSEVGQaLVEHpDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 240 AGQTCVAPDYVLCSPEMQERLLPAL-QSTITRFYGDDPQSSPNLGRIINQKQFQR-LRAL-LG---CGHVAIGGQ---SD 310
Cdd:cd07097 274 TGQRCTASSRLIVTEGIHDRFVEALvERTKALKVGDALDEGVDIGPVVSERQLEKdLRYIeIArseGAKLVYGGErlkRP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 311 ESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREkplalyaFSNSSQVVKRVL---------TQT 381
Cdd:cd07097 354 DEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTE-------FGLSAGIVTTSLkhathfkrrVEA 426
|
410 420 430
....*....|....*....|....*....|....*.
gi 685584907 382 ssggfcgndGFMHMTLAS------LPFGGVGASGMG 411
Cdd:cd07097 427 ---------GVVMVNLPTagvdyhVPFGGRKGSSYG 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
98-411 |
4.80e-48 |
|
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: 171.38 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETG-Q 175
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGdE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 176 LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSP 254
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 255 EMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRL-----RALLGCGHVAIGGQSDESDrYIAPTVLVDVQETE 328
Cdd:cd07145 277 EVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERMenlvnDAVEKGGKILYGGKRDEGS-FFPPTVLENDTPDM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 329 PVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfMHMTLASLPFGGVGAS 408
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-TRFRWDNLPFGGFKKS 434
|
...
gi 685584907 409 GMG 411
Cdd:cd07145 435 GIG 437
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
12-424 |
7.06e-48 |
|
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: 171.37 E-value: 7.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEvaisqgeITLALRNLRAWMKDEHVPKNL 91
Cdd:cd07559 48 HEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAAD-------IPLAIDHFRYFAGVIRAQEGS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 92 ATQLDS---AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAVVLG 168
Cdd:cd07559 121 LSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 169 GPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNP-------CYVDDNCDPQTVANRVAWFryFN 239
Cdd:cd07559 201 FGSEAGKpLASHpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPniffddaMDADDDFDDKAEEGQLGFA--FN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 240 AGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQ-SSPNLGRIINQKQFQRLRALLGCG-----HVAIGGQSDESD 313
Cdd:cd07559 279 QGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLdPETMMGAQVSKDQLEKILSYVDIGkeegaEVLTGGERLTLG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 314 R-----YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCG 388
Cdd:cd07559 359 GldkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWV 438
|
410 420 430
....*....|....*....|....*....|....*.
gi 685584907 389 NDgfMHMTLASLPFGGVGASGMGQYHGKFSFDTFSH 424
Cdd:cd07559 439 NC--YHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQ 472
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-423 |
1.47e-46 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 167.63 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEvaisqgeITLALRNLRAWMKDEHVPKNL 91
Cdd:cd07117 48 QEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVD-------IPLAADHFRYFAGVIRAEEGS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 92 ATQLDSAF---IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----SMEKVLAEVLPRyldeSCFA 164
Cdd:cd07117 121 ANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSlsllELAKIIQDVLPK----GVVN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:cd07117 197 IVTGKGSKSGEyLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 243 TCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLRALLGCG-----HVAIGGQ---SDESD 313
Cdd:cd07117 277 VCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDpDTQMGAQVNKDQLDKILSYVDIAkeegaKILTGGHrltENGLD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 314 R--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDg 391
Cdd:cd07117 357 KgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNT- 435
|
410 420 430
....*....|....*....|....*....|..
gi 685584907 392 fMHMTLASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07117 436 -YNQIPAGAPFGGYKKSGIGRETHKSMLDAYT 466
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-424 |
8.31e-46 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 166.45 E-value: 8.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTR-----SAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESE--LSEVA------ISQGEiTLALRNl 78
Cdd:PLN02467 55 RKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdMDDVAgcfeyyADLAE-ALDAKQ- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 79 rawmkdeHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV----- 153
Cdd:PLN02467 133 -------KAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADIcrevg 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 154 LPRyldeSCFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDpqtVANR 231
Cdd:PLN02467 206 LPP----GVLNVVTGLGTEAGApLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVD---LDKA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 232 VAW--FRYF-NAGQTCVAPDYVLC----SPEMQERLLPALQStITrfYGDDPQSSPNLGRIINQKQFQRLRALLGCGH-- 302
Cdd:PLN02467 279 VEWamFGCFwTNGQICSATSRLLVheriASEFLEKLVKWAKN-IK--ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKse 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 303 ---VAIGGQSDESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKR 376
Cdd:PLN02467 356 gatILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCER 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 685584907 377 VLTQTSSGGF---CGNDGFmhmtlASLPFGGVGASGMGQYHGKFSFDTFSH 424
Cdd:PLN02467 436 VSEAFQAGIVwinCSQPCF-----CQAPWGGIKRSGFGRELGEWGLENYLS 481
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
103-411 |
5.94e-45 |
|
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: 164.32 E-value: 5.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETGQ-LLEH- 179
Cdd:cd07124 165 RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDyLVEHp 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 180 RFDYIFFTGSPRVGKIVMTAAAK------HLTPVTLELGGKNPCYVDDNCDPQTVANRV--AWFRYfnAGQTCVApdyvl 251
Cdd:cd07124 245 DVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIvrSAFGF--QGQKCSA----- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 252 CS---------PEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLR----ALLGCGHVAIGGQSDESDR---Y 315
Cdd:cd07124 318 CSrvivhesvyDEFLERLVERTKALKV---GDPEDPEVYMGPVIDKGARDRIRryieIGKSEGRLLLGGEVLELAAegyF 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 316 IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHM 395
Cdd:cd07124 395 VQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGA 474
|
330
....*....|....*.
gi 685584907 396 TLASLPFGGVGASGMG 411
Cdd:cd07124 475 LVGRQPFGGFKMSGTG 490
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
98-427 |
6.34e-45 |
|
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: 163.47 E-value: 6.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKsmekVLAEVLPRYLDESCFA-----VVLGGPQE 172
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP----LSALYMTKLIPEAGFPpgvinVVSGYGRT 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 173 TGQLLE-H-RFDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07143 214 CGNAISsHmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSR 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 250 VLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCGH-----VAIGGQSDESDRY-IAPTVLV 322
Cdd:cd07143 294 IYVQEGIYDKFVKRFKEKAKKLKVGDPfAEDTFQGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 323 DVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNdgfmhMTLAS 399
Cdd:cd07143 374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVwvnCYN-----LLHHQ 448
|
330 340
....*....|....*....|....*...
gi 685584907 400 LPFGGVGASGMGQYHGKFSFDTFSHHRA 427
Cdd:cd07143 449 VPFGGYKQSGIGRELGEYALENYTQIKA 476
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
12-415 |
1.38e-44 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 162.16 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDlhkSAFEselseVAISQGEITLALRNLRAW------MKDE 85
Cdd:cd07107 29 RAAFPEWRATTPLERARMLRELATRLREHAEELALIDALD---CGNP-----VSAMLGDVMVAAALLDYFaglvteLKGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 86 HVPknlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAV 165
Cdd:cd07107 101 TIP---VGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 166 VLGGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANR-VAWFRYFNAGQ 242
Cdd:cd07107 178 LPGDGATAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAaVAGMNFTWCGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 243 TCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPqSSPN--LGRIINQKQFQRLRALLGCGH------VAIGGQSD---- 310
Cdd:cd07107 258 SCGSTSRLFVHESIYDEVLARVVERVAAIKVGDP-TDPAttMGPLVSRQQYDRVMHYIDSAKregarlVTGGGRPEgpal 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 311 ESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGND 390
Cdd:cd07107 337 EGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWING 416
|
410 420
....*....|....*....|....*
gi 685584907 391 GFMHmtLASLPFGGVGASGMGQYHG 415
Cdd:cd07107 417 SSRH--FLGAPFGGVKNSGIGREEC 439
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
67-427 |
1.43e-44 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 162.28 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 67 SQGEITLALRNLR---AWMKDEHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS 143
Cdd:cd07142 101 RYAEVPLAARLFRyyaGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 144 K----SMEKVLAEV-LPryldESCFAVVLG-GPQETGQLLEHR-FDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKN 215
Cdd:cd07142 181 PlsalLAAKLAAEAgLP----DGVLNIVTGfGPTAGAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 216 PCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLP-ALQSTITRFYGDDPQSSPNLGRIINQKQFQRL 294
Cdd:cd07142 257 PFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEkAKARALKRVVGDPFRKGVEQGPQVDKEQFEKI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 295 ----------RALLGCGHVAIGGQSdesdRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLAL 364
Cdd:cd07142 337 lsyiehgkeeGATLITGGDRIGSKG----YYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAA 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685584907 365 YAFSNSSQVVKRVLTQTSSGGFCGN--DGFMhmtlASLPFGGVGASGMGQYHGKFSFDTFSHHRA 427
Cdd:cd07142 413 GVFSKNIDTANTLSRALKAGTVWVNcyDVFD----ASIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
98-424 |
1.85e-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: 161.70 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGpQETGQL 176
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 177 LEHRFDY--IFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSP 254
Cdd:cd07090 189 LCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 255 EMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLR----------ALLGCGHVAIGGQSD-ESDRYIAPTVLV 322
Cdd:cd07090 269 SIKDEFTERLVERTKKIRIGDPlDEDTQMGALISEEHLEKVLgyiesakqegAKVLCGGERVVPEDGlENGFYVSPCVLT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 323 DVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPF 402
Cdd:cd07090 349 DCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVPF 426
|
330 340
....*....|....*....|..
gi 685584907 403 GGVGASGMGQYHGKFSFDTFSH 424
Cdd:cd07090 427 GGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
97-431 |
2.46e-44 |
|
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: 161.84 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 97 SAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV-----LPryldESCFAVVLGGPQ 171
Cdd:cd07113 135 TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELakeagIP----DGVLNVVNGKGA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 172 ETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 250
Cdd:cd07113 211 VGAQLISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 251 LCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLRALLGCGH------VAIGGQSDESDRYIAPTVLVD 323
Cdd:cd07113 291 YVHRSKFDELVTKLKQALSSFQVGSPMDeSVMFGPLANQPHFDKVCSYLDDARaegdeiVRGGEALAGEGYFVQPTLVLA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 324 VQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgfMHMTL-ASLPF 402
Cdd:cd07113 371 RSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLdPAVPF 447
|
330 340
....*....|....*....|....*....
gi 685584907 403 GGVGASGMGQYHGKFSFDTFSHHRACLLR 431
Cdd:cd07113 448 GGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
14-431 |
7.10e-44 |
|
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: 160.55 E-value: 7.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 14 AF-HTGRTrSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHK---SAFESELSEVAISQGEITLALRNLRAWMKDEHVPK 89
Cdd:TIGR03374 50 AFaEWGQT-TPKARAECLLKLADVIEENAQVFAELESRNCGKplhSVFNDEIPAIVDVFRFFAGAARCLSGLAAGEYLEG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 90 NlatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAVVLGG 169
Cdd:TIGR03374 129 H------TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 170 PQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAP 247
Cdd:TIGR03374 203 GKTVGDPLtgHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 248 DYVLCSPEMQERLLPALQSTITRFYGDDPQ-SSPNLGRIINQKQFQRLRALL----GCGHVAI---GGQSDESDRYIAPT 319
Cdd:TIGR03374 283 CRIYAQRGIYDTLVEKLGAAVATLKSGAPDdESTELGPLSSLAHLERVMKAVeeakALGHIKVitgGEKRKGNGYYFAPT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 320 VLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFmhMTLAS 399
Cdd:TIGR03374 363 LLAGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHF--MLVSE 440
|
410 420 430
....*....|....*....|....*....|..
gi 685584907 400 LPFGGVGASGMGQYHGKFSFDTFSHHRACLLR 431
Cdd:TIGR03374 441 MPHGGQKLSGYGKDMSLYGLEDYTVVRHIMVK 472
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
12-409 |
3.18e-42 |
|
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: 155.12 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESeLSEVAISQGEITLALRNL--RAWmkdehvPK 89
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYheRTG------ER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV-----LPRyldeSCFA 164
Cdd:cd07095 83 ATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELweeagLPP----GVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHltP---VTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:cd07095 159 LVQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 241 GQTCVAPDYVLCSPEMQ-ERLLPALQSTITRFYGDDPQSSPN--LGRIINQKQFQRLRA---LLGCGHVAIGGQS--DES 312
Cdd:cd07095 237 GQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPfmGPLIIAAAAARYLLAqqdLLALGGEPLLAMErlVAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 313 DRYIAPTvLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgf 392
Cdd:cd07095 317 TAFLSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN--- 392
|
410
....*....|....*....
gi 685584907 393 MHMTLAS--LPFGGVGASG 409
Cdd:cd07095 393 RPTTGASstAPFGGVGLSG 411
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
4-428 |
4.56e-42 |
|
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: 155.41 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 4 FEDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESeLSEV---------AISQGEItla 74
Cdd:cd07086 37 VEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEG-LGEVqemidicdyAVGLSRM--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 75 lrnlrawMKDEHVPKNLATQldSAFIRKEPFGLVLIIAPWNYPL-----NLTLvplvgALAAGNCVVLKPSE----ISKS 145
Cdd:cd07086 113 -------LYGLTIPSERPGH--RLMEQWNPLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 146 MEKVLAEVLPRY-LDESCFAVVLGGpQETGQLLEH--RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDN 222
Cdd:cd07086 179 VTKILAEVLEKNgLPPGVVNLVTGG-GDGGELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 223 CDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNL-GRIINQKQFQR-LRAL--- 297
Cdd:cd07086 258 ADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLvGPLINQAAVEKyLNAIeia 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 298 --LGcGHVAIGG---QSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQ 372
Cdd:cd07086 338 ksQG-GTVLTGGkriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLR 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685584907 373 VVKRVLTQTSSGgfCG----NDGfmhmTL---ASLPFGGVGASGMGQYHGKFSFDTFSHHRAC 428
Cdd:cd07086 417 EAFRWLGPKGSD--CGivnvNIP----TSgaeIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
12-423 |
8.45e-42 |
|
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: 154.42 E-value: 8.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFH-TGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELsEVAISQGEI----TLAlRNLRAWMKdEH 86
Cdd:cd07120 29 RRAFDeTDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF-EISGAISELryyaGLA-RTEAGRMI-EP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 87 VPKNLATQLdsafirKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP----SEISKSMEKVLAEVlpRYLDESC 162
Cdd:cd07120 106 EPGSFSLVL------REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPagqtAQINAAIIRILAEI--PSLPAGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 163 FAVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:cd07120 178 VNLFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 241 GQTCVAPDYVLC----SPEMQERLLPALQStITRFYGDDPQSspNLGRIINQKQFQRL-----RALLGCGHVAI-GGQSD 310
Cdd:cd07120 258 GQFCMAGSRVLVqrsiADEVRDRLAARLAA-VKVGPGLDPAS--DMGPLIDRANVDRVdrmveRAIAAGAEVVLrGGPVT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 311 ESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFC 387
Cdd:cd07120 335 EGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVW 414
|
410 420 430
....*....|....*....|....*....|....*..
gi 685584907 388 GNDgfmHMTL-ASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07120 415 IND---WNKLfAEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
103-409 |
8.75e-42 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 155.48 E-value: 8.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKSMEKVLAEV-LPRyldeSCFAVVLGGPQETGQ-L 176
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASdtpvIAAKFVEVLEEAgLPA----GVVNFVPGSGSEVGDyL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 177 LEH-RFDYIFFTGSPRVGKIVMTAAAK------HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVApdy 249
Cdd:PRK03137 246 VDHpKTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA--- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 250 vlCS---------PEMQERLLpALQSTITrfYGDdPQSSPNLGRIINQKQFQRLRALL----GCGHVAIGGQSDESDRY- 315
Cdd:PRK03137 323 --CSraivhedvyDEVLEKVV-ELTKELT--VGN-PEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYf 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 316 IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHM 395
Cdd:PRK03137 397 IQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGA 476
|
330
....*....|....
gi 685584907 396 TLASLPFGGVGASG 409
Cdd:PRK03137 477 IVGYHPFGGFNMSG 490
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
98-411 |
1.19e-41 |
|
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: 154.27 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSeiskSMEKVLAEVLPRYLDESCF-----AVVLGGPQE 172
Cdd:cd07082 135 AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA----TQGVLLGIPLAEAFHDAGFpkgvvNVVTGRGRE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 173 TGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKhlTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 250
Cdd:cd07082 211 IGDpLVTHgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRV 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 251 LCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALL------GcGHVAIGGQSdESDRYIAPTVLVD 323
Cdd:cd07082 289 LVHESVADELVELLKEEVAKLKVGMPwDNGVDITPLIDPKSADFVEGLIddavakG-ATVLNGGGR-EGGNLIYPTLLDP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 324 VQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG-----GFC--GNDGFmhmt 396
Cdd:cd07082 367 VTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGtvninSKCqrGPDHF---- 442
|
330
....*....|....*
gi 685584907 397 laslPFGGVGASGMG 411
Cdd:cd07082 443 ----PFLGRKDSGIG 453
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
98-423 |
6.98e-41 |
|
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: 152.50 E-value: 6.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVlpryLDESCFA-----VVLG-GPQ 171
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASL----IKEAGFPpgvvnVVPGyGPT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 172 ETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07141 215 AGAAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 250 VLC-SPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRAL----------LGCGhvaiGGQSDESDRYIAP 318
Cdd:cd07141 295 TFVqESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELiesgkkegakLECG----GKRHGDKGYFIQP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 319 TVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSsqvVKRVLTQTSS--GGFCGNDGFMHMT 396
Cdd:cd07141 371 TVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAITFSNAlrAGTVWVNCYNVVS 447
|
330 340
....*....|....*....|....*..
gi 685584907 397 lASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:cd07141 448 -PQAPFGGYKMSGNGRELGEYGLQEYT 473
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
99-384 |
8.21e-41 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 150.66 E-value: 8.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETGQLL 177
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 178 --EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD--YVLCS 253
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAErvYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 254 --PEMQERLLPALQSTItrfYGDDPQ-SSPNLGRIINQKQFQRL-----RALLGCGHVAIGGQSDESDRYI-APTVLVDV 324
Cdd:PRK10090 226 iyDQFVNRLGEAMQAVQ---FGNPAErNDIAMGPLINAAALERVeqkvaRAVEEGARVALGGKAVEGKGYYyPPTLLLDV 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 325 QETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:PRK10090 303 RQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
104-415 |
6.30e-40 |
|
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: 150.40 E-value: 6.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETGQ-LLEH-R 180
Cdd:TIGR01237 167 PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVVQFVPGSGSEVGDyLVDHpK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 181 FDYIFFTGSPRVGKIVMTAAAK------HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA-PDYVLCS 253
Cdd:TIGR01237 247 TSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAgSRAVVHE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 254 P---EMQERLLPALQSTITRfYGDDPqsSPNLGRIINQKQFQRLRALLGCG----HVAIGGQSDESDRY-IAPTVLVDVQ 325
Cdd:TIGR01237 327 KvydEVVERFVEITESLKVG-PPDSA--DVYVGPVIDQKSFNKIMEYIEIGkaegRLVSGGCGDDSKGYfIGPTIFADVD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 326 ETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGV 405
Cdd:TIGR01237 404 RKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGF 483
|
330
....*....|
gi 685584907 406 GASGMGQYHG 415
Cdd:TIGR01237 484 KMSGTDSKAG 493
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
38-422 |
8.82e-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: 149.20 E-value: 8.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 38 HENKQLLHDALAqDLHKSAfesELSEVAISqgeitlaLRNLrawMKDEHVPkNLATQLDSAFIRkEPFGLVLIIAPWNYP 117
Cdd:cd07085 86 LEHGKTLADARG-DVLRGL---EVVEFACS-------IPHL---LKGEYLE-NVARGIDTYSYR-QPLGVVAGITPFNFP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 118 LnltLVPL---VGALAAGNCVVLKPSEISKSMEKVLAEV-----LPryldESCFAVVLGGPQETGQLLEH-RFDYIFFTG 188
Cdd:cd07085 150 A---MIPLwmfPMAIACGNTFVLKPSERVPGAAMRLAELlqeagLP----DGVLNVVHGGKEAVNALLDHpDIKAVSFVG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 189 SPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTI 268
Cdd:cd07085 223 STPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 269 TRF---YGDDPqsSPNLGRIINQKQFQRLRALLGCG-----HVAIGGQSDESDRY-----IAPTVLVDVQETEPVMQEEI 335
Cdd:cd07085 303 KKLkvgAGDDP--GADMGPVISPAAKERIEGLIESGveegaKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEI 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 336 FGPILPIVNVRSVDEAIEFINRREkplalYA-----FSNSSQVVKRVLTQTsSGGFCG-NDGfMHMTLASLPFGGVGASG 409
Cdd:cd07085 381 FGPVLSIVRVDTLDEAIAIINANP-----YGngaaiFTRSGAAARKFQREV-DAGMVGiNVP-IPVPLAFFSFGGWKGSF 453
|
410
....*....|....*
gi 685584907 410 MGQYH--GKFSFDTF 422
Cdd:cd07085 454 FGDLHfyGKDGVRFY 468
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
102-424 |
1.85e-39 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 148.82 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 102 KEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE---ISKSMEKVLAEV--LPryldESCFAVVLG-GPQETGQ 175
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEqtpLSALFYAHLAKLagVP----DGVINVVTGfGPTAGAA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 176 LLEHR-FDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 253
Cdd:PLN02766 232 IASHMdVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 254 PEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALL------GCGHVAIGGQSDESDRYIAPTVLVDVQE 326
Cdd:PLN02766 312 EGIYDEFVKKLVEKAKDWVVGDPfDPRARQGPQVDKQQFEKILSYIehgkreGATLLTGGKPCGDKGYYIEPTIFTDVTE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 327 TEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTlaSLPFGGVG 406
Cdd:PLN02766 392 DMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDP--DCPFGGYK 469
|
330
....*....|....*...
gi 685584907 407 ASGMGQYHGKFSFDTFSH 424
Cdd:PLN02766 470 MSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
14-411 |
7.42e-39 |
|
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: 147.34 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 14 AFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFEsELSEVAISQGEITLALRNLRAWMKDEHVPKNLAT 93
Cdd:cd07083 67 AFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 94 QLDSAFIRkePFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKSMEKVLAEV-LPRYLDESCFAVvlg 168
Cdd:cd07083 146 EDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFHEAgFPPGVVQFLPGV--- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 169 GPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLT------PVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:cd07083 221 GEEVGAYLTEHeRIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 242 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLRALL----GCGHVAIGGQSDESDRY- 315
Cdd:cd07083 301 QKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEnGTDLGPVIDAEQEAKVLSYIehgkNEGQLVLGGKRLEGEGYf 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 316 IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVD--EAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFM 393
Cdd:cd07083 381 VAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKIT 460
|
410
....*....|....*...
gi 685584907 394 HMTLASLPFGGVGASGMG 411
Cdd:cd07083 461 GALVGVQPFGGFKLSGTN 478
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
19-422 |
4.16e-38 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 144.66 E-value: 4.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 19 RTRSAEFRAAQLRGLGRFLHENKQllhdalaqDLHKSAFESELSEVAISQGEITLALRNLRaWMKDEH-------VPKNl 91
Cdd:PRK11241 65 RALTAKERANILRRWFNLMMEHQD--------DLARLMTLEQGKPLAEAKGEISYAASFIE-WFAEEGkriygdtIPGH- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 92 atQLDSAFIR-KEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGG 169
Cdd:PRK11241 135 --QADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 170 PQETGQLLEHR--FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAP 247
Cdd:PRK11241 213 AGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 248 DYVLCSPEMQERLLPALQSTITRFY-GDDPQSSPNLGRIINQKQFQRLR-----ALLGCGHVAIGGQSDE-SDRYIAPTV 320
Cdd:PRK11241 293 NRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 321 LVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLAsl 400
Cdd:PRK11241 373 LVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA-- 450
|
410 420
....*....|....*....|..
gi 685584907 401 PFGGVGASGMGQYHGKFSFDTF 422
Cdd:PRK11241 451 PFGGIKASGLGREGSKYGIEDY 472
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
12-416 |
5.45e-38 |
|
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: 144.46 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESElsevaisQGEITLALRNLR---AWmkdehvp 88
Cdd:cd07111 69 RTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESR-------DCDIPLVARHFYhhaGW------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 89 knlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVL 167
Cdd:cd07111 135 ---AQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 168 GGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 246
Cdd:cd07111 212 GNGSFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 247 PDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRALLGCGHvAIGGQSDESDR-------YIAP 318
Cdd:cd07111 292 GSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 319 TVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLA 398
Cdd:cd07111 371 TLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING--HNLFDA 448
|
410
....*....|....*...
gi 685584907 399 SLPFGGVGASGMGQYHGK 416
Cdd:cd07111 449 AAGFGGYRESGFGREGGK 466
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
98-423 |
1.58e-37 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 143.50 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETGQL 176
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 177 L--EHRFDYIFFTGSPRVGKIVMT-AAAKHLTPVTLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPDYVLC 252
Cdd:PRK09847 231 LsrHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 253 SPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALL----GCGHVAIGGQSDESDRYIAPTVLVDVQET 327
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQPGHPlDPATTMGTLIDCAHADSVHSFIregeSKGQLLLDGRNAGLAAAIGPTIFVDVDPN 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 328 EPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGG-FCG--NDGFMhmtlaSLPFGG 404
Cdd:PRK09847 391 ASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSvFVNnyNDGDM-----TVPFGG 465
|
330
....*....|....*....
gi 685584907 405 VGASGMGQYHGKFSFDTFS 423
Cdd:PRK09847 466 YKQSGNGRDKSLHALEKFT 484
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
5-411 |
2.32e-37 |
|
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: 142.00 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 5 EDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESElSEVAISQGEITLA----LRNLRA 80
Cdd:cd07147 24 EEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR-GEVARAIDTFRIAaeeaTRIYGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 81 WMKDEHVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LD 159
Cdd:cd07147 103 VLPLDISARGEGRQ---GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETgLP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 160 ESCFAVVLGGPQETGQLLEH-RFDYIFFTGSPRVG-KIVMTAAAKHltpVTLELGGKNPCYVDDNCDPQTVANRVAWFRY 237
Cdd:cd07147 180 KGAFSVLPCSRDDADLLVTDeRIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 238 FNAGQTCVAPDYVLCS----PEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLR-----ALLGCGHVAIGGQ 308
Cdd:cd07147 257 YQAGQSCISVQRVLVHrsvyDEFKSRLVARVKALKT---GDPKDDATDVGPMISESEAERVEgwvneAVDAGAKLLTGGK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 309 SDESdrYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCG 388
Cdd:cd07147 334 RDGA--LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVI 411
|
410 420
....*....|....*....|....*..
gi 685584907 389 ND--GFM--HMtlaslPFGGVGASGMG 411
Cdd:cd07147 412 NDvpTFRvdHM-----PYGGVKDSGIG 433
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-427 |
4.09e-36 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 139.94 E-value: 4.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----SMEKVLAEV-LPryldESCFAVVLG-GPQETGQL 176
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPlsalYAAKLLHEAgLP----PGVLNVVSGfGPTAGAAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 177 LEHR-FDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSP 254
Cdd:PLN02466 270 ASHMdVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 255 EM-QERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQR-LR---------ALLGCGhvaiGGQSDESDRYIAPTVLVD 323
Cdd:PLN02466 350 RVyDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKiLRyiksgvesgATLECG----GDRFGSKGYYIQPTVFSN 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 324 VQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGN--DGFMhmtlASLP 401
Cdd:PLN02466 426 VQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFD----AAIP 501
|
330 340
....*....|....*....|....*.
gi 685584907 402 FGGVGASGMGQYHGKFSFDTFSHHRA 427
Cdd:PLN02466 502 FGGYKMSGIGREKGIYSLNNYLQVKA 527
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
96-423 |
7.35e-35 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 135.78 E-value: 7.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 96 DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVlGGPQETG 174
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVV-QGDGRVG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 175 QLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQT------VANrvawfrYFNAGQTCVA 246
Cdd:PRK13252 213 AWLtEHpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRaadiamLAN------FYSSGQVCTN 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 247 PDYVLCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLR----------ALLGCGHVAIGGQSDESDRY 315
Cdd:PRK13252 287 GTRVFVQKSIKAAFEARLLERVERIRIGDPMDpATNFGPLVSFAHRDKVLgyiekgkaegARLLCGGERLTEGGFANGAF 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 316 IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSgGFC-----GNd 390
Cdd:PRK13252 367 VAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEA-GICwintwGE- 444
|
330 340 350
....*....|....*....|....*....|...
gi 685584907 391 gfmhmTLASLPFGGVGASGMGQYHGKFSFDTFS 423
Cdd:PRK13252 445 -----SPAEMPVGGYKQSGIGRENGIATLEHYT 472
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
18-430 |
2.25e-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: 134.12 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 18 GRTRSAEfRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESelsevaiSQGEITLALRNLRAWMKDEHVPKNLATQLDS 97
Cdd:cd07116 55 GKTSVAE-RANILNKIADRMEANLEMLAVAETWDNGKPVRET-------LAADIPLAIDHFRYFAGCIRAQEGSISEIDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 ---AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESCFAVVLGGPQETG 174
Cdd:cd07116 127 ntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 175 QLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNP-CYVDD--NCDPQTVANRVAWFRYF--NAGQTCVAP 247
Cdd:cd07116 207 KPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADvmDADDAFFDKALEGFVMFalNQGEVCTCP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 248 DYVLCSPEMQERLLP-ALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCG-----HVAIGGQ-----SDESDRYI 316
Cdd:cd07116 287 SRALIQESIYDRFMErALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGkeegaEVLTGGErnelgGLLGGGYY 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 317 APTVLVDVQETEpVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgFMHMT 396
Cdd:cd07116 367 VPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLY 443
|
410 420 430
....*....|....*....|....*....|....
gi 685584907 397 LASLPFGGVGASGMGQYHGKFSFDTFSHHRaCLL 430
Cdd:cd07116 444 PAHAAFGGYKQSGIGRENHKMMLDHYQQTK-NLL 476
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
99-412 |
3.42e-29 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 119.52 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETGQLL 177
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSLVGQRL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 178 EHRFDY--IFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSP 254
Cdd:cd07140 222 SDHPDVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 255 EMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRL-----RALLGCGHVAIGG-QSDESDRYIAPTVLVDVQET 327
Cdd:cd07140 302 SIHDEFVRRVVEEVKKMKIGDPlDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDH 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 328 EPVMQEEIFGPILPI--VNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGV 405
Cdd:cd07140 382 MFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT--YNKTDVAAPFGGF 459
|
....*..
gi 685584907 406 GASGMGQ 412
Cdd:cd07140 460 KQSGFGK 466
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-409 |
5.35e-29 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 118.91 E-value: 5.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 12 REAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESeLSEVAISQGEITLALR--NLRAWMKDEHVPK 89
Cdd:PRK09457 47 RAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEA-ATEVTAMINKIAISIQayHERTGEKRSEMAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 90 NlatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS-KSMEKVL---------AEVLpryld 159
Cdd:PRK09457 126 G------AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTpWVAELTVklwqqaglpAGVL----- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 160 escfAVVLGGPqETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHltP---VTLELGGKNPCYVDDNCDPQTVANRVAW 234
Cdd:PRK09457 195 ----NLVQGGR-ETGKaLAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 235 FRYFNAGQTCVAPDYVLCSPEMQ-ERLLPALQSTITRF----YGDDPQssPNLGRIINQKQFQRL----RALLGCGHVAI 305
Cdd:PRK09457 268 SAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLtvgrWDAEPQ--PFMGAVISEQAAQGLvaaqAQLLALGGKSL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 306 --GGQSDESDRYIAPTvLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSS 383
Cdd:PRK09457 346 leMTQLQAGTGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRA 424
|
410 420
....*....|....*....|....*...
gi 685584907 384 GGFCGNDgfmHMTLAS--LPFGGVGASG 409
Cdd:PRK09457 425 GIVNWNK---PLTGASsaAPFGGVGASG 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
2-422 |
4.44e-27 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 113.03 E-value: 4.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 2 DPFEDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESElSEVAISQgeitlalrNLRAW 81
Cdd:PRK13968 29 DDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAKSA--------NLCDW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 82 MKdEHVPKNLATQL-----DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPR 156
Cdd:PRK13968 100 YA-EHGPAMLKAEPtlvenQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 157 Y-LDESCFAVVLGGPQETGQLL-EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAW 234
Cdd:PRK13968 179 AgIPQGVYGWLNADNDGVSQMInDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 235 FRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPN-LGRI----INQKQFQRLRALLGCG-HVAIGGQ 308
Cdd:PRK13968 259 GRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENaLGPMarfdLRDELHHQVEATLAEGaRLLLGGE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 309 SDESD-RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG--- 384
Cdd:PRK13968 339 KIAGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGgvf 418
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 685584907 385 --GFCGNDgfmhmtlASLPFGGVGASGMGQYHGKFSFDTF 422
Cdd:PRK13968 419 inGYCASD-------ARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
98-411 |
1.45e-25 |
|
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: 108.66 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS----KSMEKVLAEV-LPrylDESCFAVVLGGPQE 172
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATplscLAFVDLLHEAgLP---EGWCQAVPCENAVA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 173 TGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHlTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC 252
Cdd:cd07148 195 EKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 253 SPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLR-----ALLGCGHVAIGGQSdESDRYIAPTVLVDVQE 326
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEewvneAVAAGARLLCGGKR-LSDTTYAPTVLLDPPR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 327 TEPVMQEEIFGPILPIVNVRSVDEAIEFINrrEKPLALYA--FSNSSQVVKRVLTQTSSGGFCGNDgfmHMTLAS--LPF 402
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQAN--SLPVAFQAavFTKDLDVALKAVRRLDATAVMVND---HTAFRVdwMPF 427
|
....*....
gi 685584907 403 GGVGASGMG 411
Cdd:cd07148 428 AGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
100-411 |
1.48e-25 |
|
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: 109.21 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVL-----PRYLdescFAVVLGGPQETG 174
Cdd:cd07125 163 LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheagvPRDV----LQLVPGDGEEIG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 175 Q-LLEH-RFDYIFFTGSPRVGKIVMTAAAKH---LTPVTLELGGKNPCYVDDNCDP-QTVANRVA-WFRyfNAGQTCVAP 247
Cdd:cd07125 239 EaLVAHpRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPeQAVKDVVQsAFG--SAGQRCSAL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 248 DyVLC-----SPEMQERLLPALQSTITrfygDDPQ-SSPNLGRIINQKQFQRLRAL--LGCGH---VAIGGQSDESDRYI 316
Cdd:cd07125 317 R-LLYlqeeiAERFIEMLKGAMASLKV----GDPWdLSTDVGPLIDKPAGKLLRAHteLMRGEawlIAPAPLDDGNGYFV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 317 APTVLVDVqeTEPVMQEEIFGPILPIV--NVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfmh 394
Cdd:cd07125 392 APGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRN--- 466
|
330 340
....*....|....*....|
gi 685584907 395 MTLA---SLPFGGVGASGMG 411
Cdd:cd07125 467 ITGAivgRQPFGGWGLSGTG 486
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-412 |
1.91e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 108.29 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 2 DPFEDTLRRLREAFHTGRTRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSafeselseVAISQGEITLALRNLRAW 81
Cdd:PRK09406 23 DEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT--------LASAKAEALKCAKGFRYY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 82 MkdEHVPKNLATQLDS--------AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV 153
Cdd:PRK09406 95 A--EHAEALLADEPADaaavgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 154 LPRY-LDESCFAVVL-GGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANR 231
Cdd:PRK09406 173 FRRAgFPDGCFQTLLvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAET 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 232 VAWFRYFNAGQTCVAPDYVLCSPEMQE---RLLPALQSTITrfYGD--DPQS-----SPNLGRIINQKQFQ---RLRALL 298
Cdd:PRK09406 253 AVTARVQNNGQSCIAAKRFIVHADVYDafaEKFVARMAALR--VGDptDPDTdvgplATEQGRDEVEKQVDdavAAGATI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 299 GCGhvaiGGQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVL 378
Cdd:PRK09406 331 LCG----GKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFI 406
|
410 420 430
....*....|....*....|....*....|....
gi 685584907 379 TQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGQ 412
Cdd:PRK09406 407 DDLEAGQVFING--MTVSYPELPFGGVKRSGYGR 438
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
104-356 |
2.28e-24 |
|
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: 105.37 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 104 PFGLVLIIAPWNYPL-----NLTLvplvgALAAGNCVVLKPSE----ISKSMEKVLAEVLPRY-LDESCFAVVLGGpQET 173
Cdd:cd07130 132 PLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttplTAIAVTKIVARVLEKNgLPGAIASLVCGG-ADV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 174 GQLLEH--RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL 251
Cdd:cd07130 206 GEALVKdpRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 252 cspeMQERLLPALQSTITRFYGD----DPQSSPNL-GRIINQKQFQRLRALL------GcGHVAIGGQS-DESDRYIAPT 319
Cdd:cd07130 286 ----VHESIYDEVLERLKKAYKQvrigDPLDDGTLvGPLHTKAAVDNYLAAIeeaksqG-GTVLFGGKViDGPGNYVEPT 360
|
250 260 270
....*....|....*....|....*....|....*..
gi 685584907 320 VlVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFIN 356
Cdd:cd07130 361 I-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
91-428 |
2.51e-22 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 99.52 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 91 LATQLDSAFIRKE-----------PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLK--PSE--ISKSMEKVLAEVLP 155
Cdd:PLN02315 130 LSRQLNGSIIPSErpnhmmmevwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIAMTKLVAEVLE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 156 RY-LDESCFAVVLGGpQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRV 232
Cdd:PLN02315 210 KNnLPGAIFTSFCGG-AEIGEAIakDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSV 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 233 AWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-------------QSSPNLGRIINQKQFQrlrallg 299
Cdd:PLN02315 289 LFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPlekgtllgplhtpESKKNFEKGIEIIKSQ------- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 300 CGHVAIGGQSDESD-RYIAPTVlVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVL 378
Cdd:PLN02315 362 GGKILTGGSAIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWI 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 685584907 379 TQTSSGgfCGndgfmhMTLASLP---------FGGVGASGMGQYHGKFSFDTFSHHRAC 428
Cdd:PLN02315 441 GPLGSD--CG------IVNVNIPtngaeiggaFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-411 |
3.06e-22 |
|
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: 99.21 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRY-LDESCFAVVLGGPQETGQLL--EH 179
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALtsDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 180 RFDYIFFTGSPRVGKIVMTAAAKHL---TPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEM 256
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 257 QERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRL----RALLGCG---HVAIGGQSDESDR--YIAPTV--LVDV 324
Cdd:TIGR01238 319 ADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEAKQNLlahiEHMSQTQkkiAQLTLDDSRACQHgtFVAPTLfeLDDI 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 325 QEtepvMQEEIFGPILPIV--NVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPF 402
Cdd:TIGR01238 399 AE----LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPF 474
|
....*....
gi 685584907 403 GGVGASGMG 411
Cdd:TIGR01238 475 GGQGLSGTG 483
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
26-411 |
1.88e-20 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 93.67 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 26 RAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESeLSEVAISQGEITLA----LRNLR--AWMKDEHVPKNLATQLdsAF 99
Cdd:PLN00412 77 RAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVRSGDLISYTaeegVRILGegKFLVSDSFPGNERNKY--CL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSeiSKSMEKVLAEVlpryldeSCF----------AVVLGG 169
Cdd:PLN00412 154 TSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPP--TQGAVAALHMV-------HCFhlagfpkgliSCVTGK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 170 PQETGQLL-EHR-FDYIFFTGsprvGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 246
Cdd:PLN00412 225 GSEIGDFLtMHPgVNCISFTG----GDTGIAISKKaGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 247 PDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGHVAIGGQSDESDR---YIAPTVLVD 323
Cdd:PLN00412 301 VKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIWPLLLDN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 324 VQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNS-------SQVVKRVLTQTSSGGFCGNDGFmhmt 396
Cdd:PLN00412 381 VRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDinkailiSDAMETGTVQINSAPARGPDHF---- 456
|
410
....*....|....*
gi 685584907 397 laslPFGGVGASGMG 411
Cdd:PLN00412 457 ----PFQGLKDSGIG 467
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
104-415 |
7.16e-20 |
|
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: 91.53 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP----SEISKSMEKVLAEVLprYLDESCFAVVLGGPQETGQLLEH 179
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPhtavSIVMQIMVRLLHYAG--LLPPEDVTLINGDGKTMQALLLH 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 180 -RFDYIFFTGSPRVGKIVmtAAAKHLTPVTLELGGKNPCYVDDNCDP-QTVANRVAWFRYFNAGQTCVAPD--YVLCSPE 255
Cdd:cd07084 178 pNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSGQKCTAQSmlFVPENWS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 256 MQeRLLPALQSTITRfygddpqSSPN---LGRIIN---QKQFQRLRALLgcGHVAIGGQSDESDRYI--------APTVL 321
Cdd:cd07084 256 KT-PLVEKLKALLAR-------RKLEdllLGPVQTfttLAMIAHMENLL--GSVLLFSGKELKNHSIpsiygacvASALF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 322 VDVQE---TEPVMQEEIFGPILPIVNVRSVDEA--IEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGfcgndgfmhMT 396
Cdd:cd07084 326 VPIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAG---------RT 396
|
330
....*....|....*....
gi 685584907 397 LASLPFGGVGAsgMGQYHG 415
Cdd:cd07084 397 YAILRGRTGVA--PNQNHG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
85-424 |
6.19e-19 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 89.42 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 85 EHVPkNLATQLDSAFIRkEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEV-LPRYLDESCF 163
Cdd:PLN02419 232 EYLP-NVSNGVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 164 AVVLGGPQETGQLLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:PLN02419 310 NIVHGTNDTVNAICDDEdIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQ 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 243 TCVAPDYVLC---SPEMQERLL---PALQSTItrfyGDDPQSspNLGRIINQKQFQRLRALLGCG------------HVA 304
Cdd:PLN02419 390 RCMALSTVVFvgdAKSWEDKLVeraKALKVTC----GSEPDA--DLGPVISKQAKERICRLIQSGvddgakllldgrDIV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 305 IGGQsdESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:PLN02419 464 VPGY--EKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAG 541
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 685584907 385 GFcGNDGFMHMTLASLPFGGVGASGMG--QYHGKFSFDTFSH 424
Cdd:PLN02419 542 QI-GINVPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-411 |
2.84e-16 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 81.94 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKSMEKVLAEVlpryldescfavvlGGPQETGQLL-- 177
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRILLEA--------------GVPAGVVQLLpg 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 178 -----------EHRFDYIFFTGSPRVGKIVMTAAAKHL------TPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:PRK11809 834 rgetvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 241 GQTCVAPDyVLCSPE-MQERLLPALQSTITRF-YGDDPQSSPNLGRIIN-------QKQFQRLRALLGCGHVAIGGQSDE 311
Cdd:PRK11809 914 GQRCSALR-VLCLQDdVADRTLKMLRGAMAECrMGNPDRLSTDIGPVIDaeakaniERHIQAMRAKGRPVFQAARENSED 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 312 SDR--YIAPTV--LVDVQEtepvMQEEIFGPILPIVNVRS--VDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGG 385
Cdd:PRK11809 993 WQSgtFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGN 1068
|
330 340
....*....|....*....|....*.
gi 685584907 386 FCGNDGFMHMTLASLPFGGVGASGMG 411
Cdd:PRK11809 1069 LYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
13-359 |
3.44e-14 |
|
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: 74.50 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 13 EAFHTGRTRSAEFRAAQLRGLGRFLhenkqllhDALAQDLHKSAF-ESELSEVAIsQGEIT-------LALRNLRA--WM 82
Cdd:cd07129 10 AAFESYRALSPARRAAFLEAIADEI--------EALGDELVARAHaETGLPEARL-QGELGrttgqlrLFADLVREgsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 83 K---DEHVPKnlATQLDSAFIRKE--PFGLVLIIAPWNYPLNLTLVplvG-----ALAAGNCVVLKP-------SEI-SK 144
Cdd:cd07129 81 DariDPADPD--RQPLPRPDLRRMlvPLGPVAVFGASNFPLAFSVA---GgdtasALAAGCPVVVKAhpahpgtSELvAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 145 SMEKVLAEV-LPryldESCFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLT--PVTLELGGKNPCYV 219
Cdd:cd07129 156 AIRAALRATgLP----AGVFSLLQGGGREVGVaLVKHpAIKAVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 220 DdncdPQTVANR--------VAWFRyFNAGQTCVAPDYVLC--SPEmQERLLPALQSTITRFygdDPQS--SPNLGRIIn 287
Cdd:cd07129 232 L----PGALAERgeaiaqgfVGSLT-LGAGQFCTNPGLVLVpaGPA-GDAFIAALAEALAAA---PAQTmlTPGIAEAY- 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685584907 288 QKQFQRLRALLGcGHVAIGGQSDESDRYIAPTVL-VDVQE--TEPVMQEEIFGPILPIVNVRSVDEAIEFINRRE 359
Cdd:cd07129 302 RQGVEALAAAPG-VRVLAGGAAAEGGNQAAPTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
106-409 |
6.21e-14 |
|
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: 73.77 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 106 GLVLIIAPWNYP---LNLTLVPlvgALAaGNCVVLKPSeiSKSM------EKVLAEV-LPryldescfAVVL-----GGP 170
Cdd:cd07123 172 GFVYAVSPFNFTaigGNLAGAP---ALM-GNVVLWKPS--DTAVlsnylvYKILEEAgLP--------PGVInfvpgDGP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 171 QETGQLLEHR-FDYIFFTGSPRVGKIVMTAAAKHLT-----P-VTLELGGKNPCYVDDNCDPQTVAN---RVAwFRYfnA 240
Cdd:cd07123 238 VVGDTVLASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTatvRGA-FEY--Q 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 241 GQTCVAPD--YVLCS--PEMQERLLPALqSTITrfYGDDPQSSPNLGRIINQKQFQRL-----RALLGCGH-VAIGGQSD 310
Cdd:cd07123 315 GQKCSAASraYVPESlwPEVKERLLEEL-KEIK--MGDPDDFSNFMGAVIDEKAFDRIkgyidHAKSDPEAeIIAGGKCD 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 311 ESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVnvrsVDEAIEFinrrEKPLAL------YA-----FSNSSQVVKRVL 378
Cdd:cd07123 392 DSVGYfVEPTVIETTDPKHKLMTEEIFGPVLTVY----VYPDSDF----EETLELvdttspYAltgaiFAQDRKAIREAT 463
|
330 340 350
....*....|....*....|....*....|...
gi 685584907 379 T--QTSSGGFCGNDGFMHMTLASLPFGGVGASG 409
Cdd:cd07123 464 DalRNAAGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
100-357 |
2.67e-13 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 72.54 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKSMEKVLAEV-LPryldESCFAVVLGGPQETG 174
Cdd:PRK11904 680 LRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEqtplIAAEAVKLLHEAgIP----KDVLQLLPGDGATVG 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 175 Q-LLEH-RFDYIFFTGSPRVGKIV-MTAAAKHLTPVTL--ELGGKNPCYVDDNCDPQTVANRV---AwFRyfNAGQTCVA 246
Cdd:PRK11904 756 AaLTADpRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVvtsA-FR--SAGQRCSA 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 247 PDyVLCSPE-MQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLRAllgcgHVA-------IGGQSDESDR--- 314
Cdd:PRK11904 833 LR-VLFVQEdIADRVIEMLKGAMAELKVGDPRLlSTDVGPVIDAEAKANLDA-----HIErmkrearLLAQLPLPAGten 906
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 685584907 315 --YIAPTvLVDVQETEpVMQEEIFGPILPIVNVRS--VDEAIEFINR 357
Cdd:PRK11904 907 ghFVAPT-AFEIDSIS-QLEREVFGPILHVIRYKAsdLDKVIDAINA 951
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
104-377 |
1.15e-12 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 69.81 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 104 PFGLVLIIA-----PWN-YPlnltlvPLVGALAAGNCVVLKPSEIS--------KSMEKVLAEVlprYLDESCFAVVLGG 169
Cdd:cd07127 193 PRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPHPAAilplaitvQVAREVLAEA---GFDPNLVTLAADT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 170 PQE--TGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLtpVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 246
Cdd:cd07127 264 PEEpiAQTLATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 247 PDYVLCSPE----MQERLLP-----ALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGHVAIGGQSDESDRYI- 316
Cdd:cd07127 342 PQNIYVPRDgiqtDDGRKSFdevaaDLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPd 421
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685584907 317 ----APTVLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINR--REK-PLALYAFSNSSQVVKRV 377
Cdd:cd07127 422 arvrTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERV 489
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
103-356 |
6.06e-12 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 67.97 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKSMEKVLAEV-LPRyldeSCFAVVLGGPQETGQLL 177
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEqtplIAARAVRLLHEAgVPK----DALQLLPGDGRTVGAAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 178 --EHRFDYIFFTGSPRVGKIVMTAAAKHLT-PVTL--ELGGKNPCYVDDNCDP-QTVANRVA-WFRyfNAGQTCVAPDyV 250
Cdd:PRK11905 751 vaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSALPeQVVADVIAsAFD--SAGQRCSALR-V 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 251 LC-----SPEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRA------LLGCG-HVAIGGQSDESDRYIAP 318
Cdd:PRK11905 828 LClqedvADRVLTMLKGAMDELRI---GDPWRLSTDVGPVIDAEAQANIEAhieamrAAGRLvHQLPLPAETEKGTFVAP 904
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 685584907 319 TVLvdvqETE--PVMQEEIFGPILPIVNVRS--VDEAIEFIN 356
Cdd:PRK11905 905 TLI----EIDsiSDLEREVFGPVLHVVRFKAdeLDRVIDDIN 942
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
8-383 |
9.84e-10 |
|
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: 60.75 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 8 LRRLreAFHTgrtrsaefRAAQLRGLGRFLHENKQLLHDaLAqdLHKSAFESElSEVAISQGEITLAL-----RNLrawM 82
Cdd:cd07128 53 LRAL--TFHE--------RAAMLKALAKYLMERKEDLYA-LS--AATGATRRD-SWIDIDGGIGTLFAyaslgRRE---L 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 83 KDEHV-PKNLATQL--DSAFIRKEPF----GLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP----SEISKSMEKVLA 151
Cdd:cd07128 116 PNAHFlVEGDVEPLskDGTFVGQHILtprrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPatatAYLTEAVVKDIV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 152 E--VLPryldESCFAVVLGGpqeTGQLLEH--RFDYIFFTGSPRVGKIVMT--AAAKHLTPVTLELGGKNPCYVDDNCDP 225
Cdd:cd07128 196 EsgLLP----EGALQLICGS---VGDLLDHlgEQDVVAFTGSAATAAKLRAhpNIVARSIRFNAEADSLNAAILGPDATP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 226 QT-----VANRVAWFRYFNAGQTCVAPDYVLCsPE-----MQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLR 295
Cdd:cd07128 269 GTpefdlFVKEVAREMTVKAGQKCTAIRRAFV-PEarvdaVIEALKARLAKVVV---GDPRLEGVRMGPLVSREQREDVR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 296 A----LLGCGHVAIGGQSDESDR--------YIAPTVLV--DVQETEPVMQEEIFGPILPIVNVRSVDEAIEFINRREKP 361
Cdd:cd07128 345 AavatLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGS 424
|
410 420
....*....|....*....|..
gi 685584907 362 LALYAFSNSSQVVKRVLTQTSS 383
Cdd:cd07128 425 LVASVVTNDPAFARELVLGAAP 446
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
90-356 |
3.13e-09 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 59.57 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKSMEKVLAEV-LPRyldeSCFA 164
Cdd:COG4230 666 AQARRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEqtplIAARAVRLLHEAgVPA----DVLQ 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 165 VVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIV-MTAAAKHLTPVTL--ELGGKNPCYVDDNCDPQTVANRV---AwFR 236
Cdd:COG4230 742 LLPGDGETVGAALvaDPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVlasA-FD 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 237 yfNAGQTCVAPDyVLCSPE-------------MQERLL--PALQSTitrfygDdpqsspnLGRIINQKQFQRLRAllgcg 301
Cdd:COG4230 821 --SAGQRCSALR-VLCVQEdiadrvlemlkgaMAELRVgdPADLST------D-------VGPVIDAEARANLEA----- 879
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685584907 302 H----------VAIGGQSDESDR--YIAPTV--LVDVQEtepvMQEEIFGPILPIVNVRS--VDEAIEFIN 356
Cdd:COG4230 880 HiermraegrlVHQLPLPEECANgtFVAPTLieIDSISD----LEREVFGPVLHVVRYKAdeLDKVIDAIN 946
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
87-384 |
1.21e-07 |
|
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: 54.04 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 87 VPKNLATQLDSAFirKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLK-PSEISKSMEKVLAEV----LPRyldES 161
Cdd:cd07126 127 VPGDHQGQQSSGY--RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKvDSKVSVVMEQFLRLLhlcgMPA---TD 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 162 CFAVVLGGPQETGQLLEHRFDYIFFTGSPRV---------GKIVMTAAA---KHLTPVTLELGgknpcYVDDNCDPQTva 229
Cdd:cd07126 202 VDLIHSDGPTMNKILLEANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA-- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 230 nrvawfrYFNAGQTCVAPDyVLCSPE--MQERLLPALQSTITRFYGDDPQSSPNLgRIINQKQFQRLRALLGC--GHVAI 305
Cdd:cd07126 275 -------YACSGQKCSAQS-ILFAHEnwVQAGILDKLKALAEQRKLEDLTIGPVL-TWTTERILDHVDKLLAIpgAKVLF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 306 GGQS----DESDRY--IAPT-VLVDVQ-----ETEPVMQEEIFGP--ILPIVNVRSVDEAIEFINRREKPLALYAFSNSS 371
Cdd:cd07126 346 GGKPltnhSIPSIYgaYEPTaVFVPLEeiaieENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDI 425
|
330
....*....|...
gi 685584907 372 QVVKRVLTQTSSG 384
Cdd:cd07126 426 RFLQEVLANTVNG 438
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
104-353 |
1.73e-06 |
|
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: 50.31 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLPRYLDESC----FAVVLGGP--QETGQLL 177
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGgpdnLVVTVEEPtiETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 178 EHR-FDYIFFTGSPRVGKIVMTAAAKhltpvTLELGGKNP-CYVDDNCDPQTVANRVAWFRYFNAGQTC----------- 244
Cdd:cd07121 177 AHPdINLLVVTGGPAVVKAALSSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVQGASFDNNLPCiaekeviavds 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 245 VAPD----------YVLCSPEMQERLLPALQstitrfygDDPQSSPNlgriinqKQF--QRLRALLGcghvAIGGQSDES 312
Cdd:cd07121 252 VADYliaamqrngaYVLNDEQAEQLLEVVLL--------TNKGATPN-------KKWvgKDASKILK----AAGIEVPAD 312
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 685584907 313 DRYIaptvLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIE 353
Cdd:cd07121 313 IRLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
103-394 |
3.21e-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: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKSMEKVLAEVLpryLDEscfAVVLGGPQ----------- 171
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLL---LQA---AVAAGAPEnligwidnpsi 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 172 ETGQLLEHR--FDYIFFTGSPRVGKivmtAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGqtcvapdy 249
Cdd:cd07081 168 ELAQRLMKFpgIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNG-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 250 VLCSPEMQERLLPALQSTITRFYGDDPqsspnlGRIINQKQFQRLRALL---GCGHVAIGGQSDESdryIAPTVLVDVQE 326
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEGQG------AYKLTAEELQQVQPVIlknGDVNRDIVGQDAYK---IAAAAGLKVPQ 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685584907 327 TEPVMqeeifgpilpIVNVRSVDEAIEFINRREKP-LALYAFSNSSQVVKRVLTQTSSGGfCGNDGFMH 394
Cdd:cd07081 307 ETRIL----------IGEVTSLAEHEPFAHEKLSPvLAMYRAANFADADAKALALKLEGG-CGHTSAMY 364
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
20-357 |
2.10e-05 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 46.67 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 20 TRSAEFRAAQLRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAIsqgeitlalrnLRAWMKDehvpknlatqlDSAF 99
Cdd:pfam05893 26 SKRHIETLAQITGYSEAMLNYLKSLMAFCRRRNLQNVLESELGQPFI-----------LDEWLPT-----------KPSY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 100 IRKEPFGLVLIIAPWNYPLnLTLVPLVGALAAGNCVVLKPSeiskSMEKVLAEVLPRYL---DESC-----FAVVL--GG 169
Cdd:pfam05893 84 EKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVS----SSDPFTAAALLASFadlDPTHpladsLSVVYwdGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 170 PQETGQLLEHRFDYIFFTGsprvGKIVMTAAAKHLTPVT--LELGGK-NPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 246
Cdd:pfam05893 159 STQLEDLIVANADVVIAWG----GEDAINAIRECLKPGKqwIDFGAKiSFAVVDREAALDKAAERAADDICVFDQQACLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 247 PDYVLCSP-------EMQERLLPALQSTITRFygddPQSSPNLG---RIINQKQFQRLRALLGcghvaiGGQSDESDRYI 316
Cdd:pfam05893 235 PQTVFVESddkitpdEFAERLAAALAKRARIL----PKAVLDIDeaaKISSDRAECKLDYAFA------GERGVWSDFHQ 304
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 685584907 317 APTVLVDVQetepvmQEEIFGPILPIVNVRSVDEAIEFINR 357
Cdd:pfam05893 305 RWTVIWSDG------QEELNSPLNRTVNVVPVPSLSDVVRY 339
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
23-232 |
4.83e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 45.68 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 23 AEFRAAQlRGLGRFLHENKQLLHDALAQDLHKSAFESELSEVAISQGEITLALRNLRAWM-------------------K 83
Cdd:cd07077 1 ESAKNAQ-RTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMgcsesklyknidtergitaS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 84 DEHVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGaLAAGNCVVLKPSEISKSMEKVLAEVLPRyldescf 163
Cdd:cd07077 80 VGHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQA------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 164 AVVLGGPQETGQLLEHR-------------FDYIFFTGSPRVGKivmtAAAKH--LTPVTLELGGKNPCYVDDNCDPQTV 228
Cdd:cd07077 152 ADAAHGPKILVLYVPHPsdelaeellshpkIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERA 227
|
....
gi 685584907 229 ANRV 232
Cdd:cd07077 228 SGSV 231
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
104-353 |
5.50e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 45.28 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKsmeKVLAEVLpRYLDESCFAVvlGGP------------Q 171
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAK---KVSLRAI-ELLNEAIVAA--GGPenlvvtvaeptiE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 172 ETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKhltpvTLELGGKNP-CYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:PRK15398 203 TAQRLMKHpGIALLVVTGGPAVVKAAMKSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVKGASFDNNLPCIAEKE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685584907 250 VLCSPEMQERLLPALQStitrfygddpqsspNLGRIINQKQFQRLRALL--GCGHV--------------AIGGQSDESD 313
Cdd:PRK15398 278 VIVVDSVADELMRLMEK--------------NGAVLLTAEQAEKLQKVVlkNGGTVnkkwvgkdaakileAAGINVPKDT 343
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 685584907 314 RYIaptvLVDVQETEPVMQEEIFGPILPIVNVRSVDEAIE 353
Cdd:PRK15398 344 RLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
|
|
| |
