|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
1-251 |
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: 527.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07132 193 MQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFIN 160
Cdd:cd07132 273 KESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFIN 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 161 RREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACLLRSPGME 240
Cdd:cd07132 353 SREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNME 432
|
250
....*....|.
gi 586946394 241 KLNALRYPPQS 251
Cdd:cd07132 433 KLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
1-233 |
2.05e-144 |
|
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: 411.53 E-value: 2.05e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07087 193 MEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFIN 160
Cdd:cd07087 273 KESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFIN 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586946394 161 RREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACL 233
Cdd:cd07087 353 SRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
1-258 |
1.04e-128 |
|
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: 372.61 E-value: 1.04e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07136 193 MEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFIN 160
Cdd:cd07136 273 LESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 161 RREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACLLRSPGME 240
Cdd:cd07136 353 SRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD 432
|
250
....*....|....*...
gi 586946394 241 klNALRYPPQSPRRLRML 258
Cdd:cd07136 433 --LPLRYPPYKGKKKKLK 448
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
1-263 |
3.22e-124 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 362.81 E-value: 3.22e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:PTZ00381 202 MQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDP 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNLGRIINQKQFQRLRALLGC--GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEF 158
Cdd:PTZ00381 282 KKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEF 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 159 INRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACLLRSPG 238
Cdd:PTZ00381 362 INSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTG 441
|
250 260
....*....|....*....|....*
gi 586946394 239 MEKLNALRYPPQSPRRLRMLLVAME 263
Cdd:PTZ00381 442 NSFDLSLRYPPYTSFKSWVLSFLLK 466
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
2-231 |
7.81e-113 |
|
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: 331.88 E-value: 7.81e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 2 TAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQ 81
Cdd:cd07135 202 EAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGAN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 82 SSPNLGRIINQKQFQRLRALLGC--GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFI 159
Cdd:cd07135 282 ASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVI 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586946394 160 NRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRA 231
Cdd:cd07135 362 NSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
1-233 |
8.48e-108 |
|
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: 318.79 E-value: 8.48e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07134 193 MAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 --QSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD 153
Cdd:cd07134 273 arKASPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 154 EAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACL 233
Cdd:cd07134 353 EVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
1-231 |
1.40e-104 |
|
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: 310.57 E-value: 1.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07133 194 MRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 qSSPNLGRIINQKQFQRLRALL------GCGRVAIG--GQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSL 152
Cdd:cd07133 274 -DNPDYTSIINERHYARLQGLLedarakGARVIELNpaGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSL 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRA 231
Cdd:cd07133 353 DEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
1-233 |
3.33e-100 |
|
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: 299.33 E-value: 3.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDD 79
Cdd:cd07137 194 MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGEN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSPNLGRIINQKQFQRLRALLGCGRVAI----GGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEA 155
Cdd:cd07137 274 PKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEES 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586946394 156 IEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACL 233
Cdd:cd07137 354 IEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-258 |
1.40e-89 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 273.91 E-value: 1.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVD---DNCDPQTVANRVAWFRYFN-AGQTCVAPDYVLCSPEMQERLLPALQSTITRFY 76
Cdd:PLN02203 201 MTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFF 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 77 GDDPQSSPNLGRIINQKQFQRLRALLGCGRVAI----GGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSL 152
Cdd:PLN02203 281 GENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKI 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRAC 232
Cdd:PLN02203 361 EDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
250 260
....*....|....*....|....*.
gi 586946394 233 LLRSPGMEKLnaLRYPPQSPRRLRML 258
Cdd:PLN02203 441 LRRSLLTEFE--FRYPPWNDFKLGFL 464
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
1-234 |
5.15e-77 |
|
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: 239.80 E-value: 5.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFY-GDD 79
Cdd:cd07078 192 MRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKvGNP 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQSDESD--RYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSL 152
Cdd:cd07078 272 LDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGkgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTlASLPFGGVGASGMGRYHGKFSFDTFSHHRAC 232
Cdd:cd07078 352 EEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAE-PSAPFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
..
gi 586946394 233 LL 234
Cdd:cd07078 431 TI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
1-258 |
1.04e-74 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 235.71 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDD 79
Cdd:PLN02174 205 MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSPNLGRIINQKQFQRLRALLG----CGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEA 155
Cdd:PLN02174 285 PMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEES 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 156 IEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACLLR 235
Cdd:PLN02174 365 FDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYR 444
|
250 260
....*....|....*....|...
gi 586946394 236 SpgMEKLNALRYPPQSPRRLRML 258
Cdd:PLN02174 445 S--LFGDSAVRYPPYSRGKLRLL 465
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-228 |
1.59e-58 |
|
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: 193.42 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC----SPEMQERLLPALQSTItrfY 76
Cdd:COG1012 237 AAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVhesiYDEFVERLVAAAKALK---V 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 77 GDDPQSSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQ--SDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNV 149
Cdd:COG1012 314 GDPLDPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPF 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586946394 150 QSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMtLASLPFGGVGASGMGRYHGKFSFDTFSH 228
Cdd:COG1012 394 DDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGREGGREGLEEYTE 471
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
1-234 |
9.34e-53 |
|
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: 175.50 E-value: 9.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQstitrfygddp 80
Cdd:cd06534 188 MKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 qsspnlgriinqkqfqrlrallgcgrvaiggqsdesdryiapTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFIN 160
Cdd:cd06534 257 ------------------------------------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALAN 294
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586946394 161 RREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTlASLPFGGVGASGMGRYHGKFSFDTFSHHRACLL 234
Cdd:cd06534 295 DTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVG-PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1-227 |
2.43e-48 |
|
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: 166.17 E-value: 2.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDD 79
Cdd:pfam00171 222 AEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQSDESD-RYIAPTVLVDV-QEMePVMQEEIFGPILPIVNVQSL 152
Cdd:pfam00171 302 LDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYFVEPTVLANVtPDM-RIAQEEIFGPVLSVIRFKDE 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHmTLASLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:pfam00171 381 EEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTG-DADGLPFGGFKQSGFGREGGPYGLEEYT 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
1-231 |
2.48e-46 |
|
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: 160.85 E-value: 2.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDD 79
Cdd:cd07099 213 MAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGAD 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSPNLGRIINQKQFQRLR-----ALLGCGRVAIGG-QSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD 153
Cdd:cd07099 293 DIGDADIGPMTTARQLDIVRrhvddAVAKGAKALTGGaRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADED 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586946394 154 EAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRA 231
Cdd:cd07099 373 EAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
1-226 |
1.23e-41 |
|
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: 148.35 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD--YVLCS--PEMQERLLPALQSTITrfy 76
Cdd:cd07103 213 MAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANriYVHESiyDEFVEKLVERVKKLKV--- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 77 GDDPQSSPNLGRIINQKQFQRLRAL----LGCG-RVAIGGQSDESD-RYIAPTVLVDV-QEMEpVMQEEIFGPILPIVNV 149
Cdd:cd07103 290 GNGLDEGTDMGPLINERAVEKVEALvedaVAKGaKVLTGGKRLGLGgYFYEPTVLTDVtDDML-IMNEETFGPVAPIIPF 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586946394 150 QSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG--GFcgNDGFmhMTLASLPFGGVGASGMGRYHGKFSFDTF 226
Cdd:cd07103 369 DTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGmvGI--NTGL--ISDAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
1-220 |
1.80e-40 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 145.52 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANrvAWFR--YFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YG 77
Cdd:cd07098 219 MAAAAESLTPVVLELGGKDPAIVLDDADLDQIAS--IIMRgtFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 78 DDPQSSPNLGRIINQKQFQRLRALLG----------CGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIV 147
Cdd:cd07098 297 PPLDGDVDVGAMISPARFDRLEELVAdavekgarllAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVM 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586946394 148 NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGND-GFMHMtLASLPFGGVGASGMGRYHGK 220
Cdd:cd07098 377 KASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDfGVNYY-VQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
1-220 |
1.14e-38 |
|
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: 140.36 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD--YVlcsPEMQ-ERLLPALQSTITRFY- 76
Cdd:cd07106 208 MASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKrlYV---HESIyDEFCEALVALAKAAVv 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 77 GDDPQSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQSDESDRY-IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQ 150
Cdd:cd07106 285 GDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYS 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586946394 151 SLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgfMHMTLA-SLPFGGVGASGMGRYHGK 220
Cdd:cd07106 365 DEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---THGALDpDAPFGGHKQSGIGVEFGI 432
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
3-228 |
7.94e-37 |
|
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: 134.97 E-value: 7.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGD--D 79
Cdd:cd07104 197 LAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVGDprD 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSpnLGRIINQKQFQRLRALL------GcGRVAIGGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD 153
Cdd:cd07104 277 PDTV--IGPLINERQVDRVHAIVedavaaG-ARLLTGGTYE--GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDE 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586946394 154 EAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHmTLASLPFGGVGASGMGRYHGKFSFDTFSH 228
Cdd:cd07104 352 EAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVN-DEPHVPFGGVKASGGGRFGGPASLEEFTE 425
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
3-227 |
1.03e-34 |
|
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: 129.76 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQ 81
Cdd:cd07150 217 KAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLkVGDPRD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 82 SSPNLGRIINQKQFQRLR-----ALLGCGRVAIGGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAI 156
Cdd:cd07150 297 PDTVIGPLISPRQVERIKrqvedAVAKGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEAL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 157 EFINRREKPLalyafsnSSQVVKRVLTQTSSGGFCGNDGFMHMTLASL------PFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07150 375 ELANDTEYGL-------SAAILTNDLQRAFKLAERLESGMVHINDPTIldeahvPFGGVKASGFGREGGEWSMEEFT 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
1-181 |
1.34e-34 |
|
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: 129.69 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD--YVLCS--PEMQERLLPALQSTItrfY 76
Cdd:cd07088 229 MEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAErvYVHEDiyDEFMEKLVEKMKAVK---V 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 77 GDDPQSSPNLGRIINQKQFQRL-----RALLGCGRVAIGGQSDESDR--YIAPTVLVDV-QEMEpVMQEEIFGPILPIVN 148
Cdd:cd07088 306 GDPFDAATDMGPLVNEAALDKVeemveRAVEAGATLLTGGKRPEGEKgyFYEPTVLTNVrQDME-IVQEEIFGPVLPVVK 384
|
170 180 190
....*....|....*....|....*....|...
gi 586946394 149 VQSLDEAIEFINRREKPLALYAFSNSSQVVKRV 181
Cdd:cd07088 385 FSSLDEAIELANDSEYGLTSYIYTENLNTAMRA 417
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
3-230 |
2.69e-33 |
|
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: 125.87 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS 82
Cdd:cd07152 208 AAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPAT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 83 SP-NLGRIINQKQFQRLRAL------LGcGRVAIGGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEA 155
Cdd:cd07152 288 GQvALGPLINARQLDRVHAIvddsvaAG-ARLEAGGTYD--GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEA 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586946394 156 IEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfmhmTLAS---LPFGGVGASGMG-RYHGKFSFDTFSHHR 230
Cdd:cd07152 365 VALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPFGGMGASGNGsRFGGPANWEEFTQWQ 439
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
3-229 |
1.15e-32 |
|
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: 124.28 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCvapdyvlCSPE-------MQERLLPALQSTITRF 75
Cdd:cd07102 213 AAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSC-------CSIEriyvhesIYDAFVEAFVAVVKGY 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 76 -YGDDPQSSPNLGRIINQKQFQRLR-----ALLGCGRVAIGGQ----SDESDRYIAPTVLVDV-QEMEpVMQEEIFGPIL 144
Cdd:cd07102 286 kLGDPLDPSTTLGPVVSARAADFVRaqiadAIAKGARALIDGAlfpeDKAGGAYLAPTVLTNVdHSMR-VMREETFGPVV 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 145 PIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGN-----DgfmhmtlASLPFGGVGASGMGRYHG 219
Cdd:cd07102 365 GIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcdylD-------PALAWTGVKDSGRGVTLS 437
|
250
....*....|....
gi 586946394 220 KFSFDTF----SHH 229
Cdd:cd07102 438 RLGYDQLtrpkSYH 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1-227 |
1.21e-32 |
|
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: 123.99 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPAL--QSTITRFyGD 78
Cdd:cd07118 215 AAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVvaRSRKVRV-GD 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 --DPQSspNLGRIINQKQFQRLRALLGCGR-----VAIGGQSDESD--RYIAPTVLVDVQEMEPVMQEEIFGPILPIVNV 149
Cdd:cd07118 294 plDPET--KVGAIINEAQLAKITDYVDAGRaegatLLLGGERLASAagLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 150 QSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGN---DGFmhmtlASLPFGGVGASGMGRYHGKFSFDTF 226
Cdd:cd07118 372 DTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNtflDGS-----PELPFGGFKQSGIGRELGRYGVEEY 446
|
.
gi 586946394 227 S 227
Cdd:cd07118 447 T 447
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
1-227 |
1.80e-32 |
|
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: 123.83 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCvapdyvLCSpemqERLLpaLQSTI-----TRF 75
Cdd:cd07093 213 MRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVC------LAG----SRIL--VQRSIydeflERF 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 76 --------YGDDPQSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQSDESDR-----YIAPTVLVDVQEMEPVMQE 137
Cdd:cd07093 281 verakalkVGDPLDPDTEVGPLISKEHLEKVLGYVELARaegatILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 138 EIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFM-HMTlasLPFGGVGASGMGR 216
Cdd:cd07093 361 EIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVrDLR---TPFGGVKASGIGR 437
|
250
....*....|.
gi 586946394 217 YHGKFSFDTFS 227
Cdd:cd07093 438 EGGDYSLEFYT 448
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
1-227 |
2.14e-32 |
|
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: 123.50 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07109 213 MRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPG 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQ----SDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQS 151
Cdd:cd07109 293 LEDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRiaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDD 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586946394 152 LDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLaSLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07109 373 EAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGI-ELPFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
1-227 |
6.34e-32 |
|
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: 122.05 E-value: 6.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDD 79
Cdd:cd07092 213 ARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIrVGDP 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSPNLGRIINQKQFQRLRALL----GCGRVAIGGQSDESDRY-IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDE 154
Cdd:cd07092 293 DDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDE 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586946394 155 AIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfmHMTLAS-LPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07092 373 AIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAAeMPHGGFKQSGYGKDLSIYALEDYT 443
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1-231 |
3.37e-31 |
|
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: 120.43 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGD- 78
Cdd:cd07089 219 MAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDp 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 -DPqsSPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNV 149
Cdd:cd07089 299 aDP--GTVMGPLISAAQRDRVEGYIARGRdegarlVTGGGRPAGLDKgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPY 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 150 QSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdGFMHMtLASLPFGGVGASGMGRYHGKFSFDTFSHH 229
Cdd:cd07089 377 DDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-GGGGY-GPDAPFGGYKQSGLGRENGIEGLEEFLET 454
|
..
gi 586946394 230 RA 231
Cdd:cd07089 455 KS 456
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
1-231 |
6.77e-31 |
|
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: 119.47 E-value: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07115 213 MQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDP 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 -QSSPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD 153
Cdd:cd07115 293 lDPKTQMGPLVSQAQFDRVLDYVDVGReegarlLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEE 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586946394 154 EAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRA 231
Cdd:cd07115 373 EALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT--YNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKS 448
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
1-226 |
4.58e-30 |
|
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: 117.22 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCD-----PQTVANRvawfrYFNAGQTCVAPDYVL----CSPEMQERLLPALQST 71
Cdd:cd07138 226 AEAAADTVKRVALELGGKSANIILDDADlekavPRGVAAC-----FANSGQSCNAPTRMLvprsRYAEAEEIAAAAAEAY 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 72 ITrfyGDDPQSSPNLGRIINQKQFQRLRALLGCG-----RVAIGG----QSDESDRYIAPTVLVDV-QEMEpVMQEEIFG 141
Cdd:cd07138 301 VV---GDPRDPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGGpgrpEGLERGYFVKPTVFADVtPDMT-IAREEIFG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 142 PILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMtlaSLPFGGVGASGMGRYHGKF 221
Cdd:cd07138 377 PVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRY 453
|
....*
gi 586946394 222 SFDTF 226
Cdd:cd07138 454 GLEEF 458
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
3-227 |
6.39e-30 |
|
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: 116.93 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFY-GD-- 78
Cdd:cd07112 223 SGQSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpGDpl 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 DPQSSpnLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQ 150
Cdd:cd07112 303 DPATR--MGALVSEAHFDKVLGYIESGkaegaRLVAGGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 151 SLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNDGFMhmtlaSLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07112 381 SEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVwvnCFDEGDI-----TTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
1-216 |
1.05e-29 |
|
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: 116.15 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANrVAWFR-YFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFY-G 77
Cdd:cd07091 237 MEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVE-WAAFGiFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 78 DDPQSSPNLGRIINQKQFQRL----------RALLGCGrvaiGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIV 147
Cdd:cd07091 316 DPFDPDTFQGPQVSKAQFDKIlsyiesgkkeGATLLTG----GERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTIL 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586946394 148 NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfmHMTLASLPFGGVGASGMGR 216
Cdd:cd07091 392 KFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTY--NVFDAAVPFGGFKQSGFGR 458
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
4-227 |
1.25e-29 |
|
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: 115.75 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 4 AAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQss 83
Cdd:cd07105 200 AAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV-- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 84 pnLGRIINQKQFQRLRAL----LGCG-RVAIGGQSDESDR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAI 156
Cdd:cd07105 278 --LGSLVSAAAADRVKELvddaLSKGaKLVVGGLADESPSgtSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAV 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 157 EFINRREKPLALYAFSNSSQVVKRVLTQTSSGGfcgndgfMH---MTL---ASLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07105 356 RIANDSEYGLSAAVFTRDLARALAVAKRIESGA-------VHingMTVhdePTLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
1-226 |
1.36e-29 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 116.33 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDD 79
Cdd:PLN02278 256 MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDG 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSPNLGRIINQKQFQRLRA------------LLGCGRVAIGGQsdesdrYIAPTVLVDVQEMEPVMQEEIFGPILPIV 147
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVEShvqdavskgakvLLGGKRHSLGGT------FYEPTVLGDVTEDMLIFREEVFGPVAPLT 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586946394 148 NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLAslPFGGVGASGMGRYHGKFSFDTF 226
Cdd:PLN02278 410 RFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
1-224 |
1.40e-29 |
|
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: 115.92 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYV--DDNCDpQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGD 78
Cdd:cd07108 212 YRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 DP-QSSPNLGRIINQKQFQRLRALLGCG------RVAIGGQSDESDR-----YIAPTVLVDVQEMEPVMQEEIFGPILPI 146
Cdd:cd07108 291 DPlDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPladgfFVQPTIFSGVDNEWRLAREEIFGPVLCA 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586946394 147 VNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMtlASLPFGGVGASGMGRyhgKFSFD 224
Cdd:cd07108 371 IPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQ--PGQSYGGFKQSGLGR---EASLE 443
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
1-226 |
4.03e-28 |
|
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: 111.90 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGD- 78
Cdd:cd07139 232 AAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALkVGDp 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 -DPqsSPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNV 149
Cdd:cd07139 312 lDP--ATQIGPLASARQRERVEGYIAKGRaegarlVTGGGRPAGLDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPY 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 150 QSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMtlaSLPFGGVGASGMGRYHGKFSFDTF 226
Cdd:cd07139 390 DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
1-227 |
4.31e-28 |
|
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: 112.02 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFY---G 77
Cdd:cd07119 230 MRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKlgnG 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 78 DDPqsSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDR-----YIAPTVLVDVQEMEPVMQEEIFGPILPIV 147
Cdd:cd07119 310 LDA--DTEMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKRPTGDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 148 NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07119 388 RFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
1-228 |
5.16e-28 |
|
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: 111.29 E-value: 5.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07110 216 MQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSP-NLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQS 151
Cdd:cd07110 296 LEEGvRLGPLVSQAQYEKVLSFIARGkeegaRLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 152 LDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNDGFMHmtlasLPFGGVGASGMGRYHGKFSFDTFSH 228
Cdd:cd07110 376 EDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVwinCSQPCFPQ-----APWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
3-226 |
9.24e-27 |
|
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: 107.55 E-value: 9.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAP----------DyvlcspEMQERLLPALQSTI 72
Cdd:cd07100 193 EAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAkrfivhedvyD------EFLEKFVEAMAALK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 73 TrfyGDD--------PQSSPNLGRIInQKQFQRlrALLGCGRVAIGGQSDESDR-YIAPTVLVDVQEMEPVMQEEIFGPI 143
Cdd:cd07100 267 V---GDPmdedtdlgPLARKDLRDEL-HEQVEE--AVAAGATLLLGGKRPDGPGaFYPPTVLTDVTPGMPAYDEELFGPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 144 LPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSF 223
Cdd:cd07100 341 AAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING--MVKSDPRLPFGGVKRSGYGRELGRFGI 418
|
...
gi 586946394 224 DTF 226
Cdd:cd07100 419 REF 421
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
1-231 |
1.13e-26 |
|
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: 108.00 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDD 79
Cdd:cd07143 240 MEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 P-QSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQSDESDRY-IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSL 152
Cdd:cd07143 320 PfAEDTFQGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNdgfmhMTLASLPFGGVGASGMGRYHGKFSFDTFSHH 229
Cdd:cd07143 400 EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVwvnCYN-----LLHHQVPFGGYKQSGIGRELGEYALENYTQI 474
|
..
gi 586946394 230 RA 231
Cdd:cd07143 475 KA 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
1-188 |
1.54e-26 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 106.74 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD--YVLCS--PEMQERLLPALQSTItrfY 76
Cdd:PRK10090 167 MAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAErvYVQKGiyDQFVNRLGEAMQAVQ---F 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 77 GDDPQ-SSPNLGRIINQKQFQRL-----RALLGCGRVAIGGQSDESDRYI-APTVLVDV-QEMEpVMQEEIFGPILPIVN 148
Cdd:PRK10090 244 GNPAErNDIAMGPLINAAALERVeqkvaRAVEEGARVALGGKAVEGKGYYyPPTLLLDVrQEMS-IMHEETFGPVLPVVA 322
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 586946394 149 VQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 188
Cdd:PRK10090 323 FDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
1-216 |
2.50e-26 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 106.92 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERL---LPALQSTITrfYG 77
Cdd:PRK13473 233 LSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLvakLAAAVATLK--VG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 78 DDPQSSPNLGRIINQKQFQRL-----RAL-LGCGRVAIGGQ-SDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQ 150
Cdd:PRK13473 311 DPDDEDTELGPLISAAHRDRVagfveRAKaLGHIRVVTGGEaPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFD 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 151 SLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMhmtLAS-LPFGGVGASGMGR 216
Cdd:PRK13473 391 DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM---LVSeMPHGGQKQSGYGK 454
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
4-216 |
2.61e-26 |
|
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: 106.66 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 4 AAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-QS 82
Cdd:cd07145 222 AGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPlDE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 83 SPNLGRIINQKQFQRL-----RALLGCGRVAIGGQSDESDrYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIE 157
Cdd:cd07145 302 STDLGPLISPEAVERMenlvnDAVEKGGKILYGGKRDEGS-FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 586946394 158 FINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfMHMTLASLPFGGVGASGMGR 216
Cdd:cd07145 381 IANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-TRFRWDNLPFGGFKKSGIGR 438
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
1-231 |
3.26e-26 |
|
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: 106.72 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFY--GD 78
Cdd:cd07144 240 MKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 DPQSSPNLGRIINQKQFQRLRALLGCGR------VAIG---GQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNV 149
Cdd:cd07144 320 PFDDDTVVGPQVSKTQYDRVLSYIEKGKkegaklVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 150 QSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNDGFMHMtlaslPFGGVGASGMGRYHGKFSFDTF 226
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSNDSDVGV-----PFGGFKMSGIGRELGEYGLETY 474
|
....*
gi 586946394 227 SHHRA 231
Cdd:cd07144 475 TQTKA 479
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
4-227 |
6.76e-26 |
|
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: 105.46 E-value: 6.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 4 AAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQS 82
Cdd:cd07151 230 AGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALpYGDPSDP 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 83 SPNLGRIINQKQFQRL-----RALLGCGRVAIGGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIE 157
Cdd:cd07151 310 DTVVGPLINESQVDGLldkieQAVEEGATLLVGGEAE--GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALE 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 158 FINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHmTLASLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEPHVPFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
2-235 |
7.60e-26 |
|
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: 105.60 E-value: 7.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 2 TAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQ 81
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 82 S-SPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDE 154
Cdd:cd07113 318 DeSVMFGPLANQPHFDKVCSYLDDARaegdeiVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 155 AIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgfMHMTL-ASLPFGGVGASGMGRYHGKFSFDTFSHHRACL 233
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLdPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
..
gi 586946394 234 LR 235
Cdd:cd07113 475 IR 476
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-216 |
1.32e-25 |
|
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: 104.60 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 8 LTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNL 86
Cdd:cd07149 224 LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDPLDEDTDV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 87 GRIINQKQFQRLR-----ALLGCGRVAIGGQSDEsdRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINR 161
Cdd:cd07149 304 GPMISEAEAERIEewveeAVEGGARLLTGGKRDG--AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAND 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 586946394 162 REKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDG----FMHMtlaslPFGGVGASGMGR 216
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALKAARELEVGGVMINDSstfrVDHM-----PYGGVKESGTGR 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
1-227 |
1.34e-25 |
|
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: 104.82 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKhLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07094 218 LRANAG-GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDP 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 -QSSPNLGRIINQKQFQRL-----RALLGCGRVAIGGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDE 154
Cdd:cd07094 297 lDEDTDVGPLISEEAAERVerwveEAVEAGARLLCGGERD--GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEE 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586946394 155 AIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfMHMTLASLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07094 375 AIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVGREGVPYAMEEMT 446
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
1-231 |
1.47e-25 |
|
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: 104.74 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07131 231 GETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNL-GRIINQKQFQRL-----------RALLGCGRVAIGGQSDESdRYIAPTVLVDVQEMEPVMQEEIFGPILPIVN 148
Cdd:cd07131 311 LDEETDmGPLINEAQLEKVlnyneigkeegATLLLGGERLTGGGYEKG-YFVEPTVFTDVTPDMRIAQEEIFGPVVALIE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 149 VQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfmhmTL---ASLPFGGVGASGMG-RYHGKFSFD 224
Cdd:cd07131 390 VSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAP----TIgaeVHLPFGGVKKSGNGhREAGTTALD 465
|
....*..
gi 586946394 225 TFSHHRA 231
Cdd:cd07131 466 AFTEWKA 472
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
3-227 |
2.59e-25 |
|
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: 103.78 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALqSTITRF--YGDDP 80
Cdd:cd07114 217 AAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERL-VARARAirVGDPL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNLGRIINQKQFQRLRALLGC-----GRVAIGGQ---SDESDR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQ 150
Cdd:cd07114 296 DPETQMGPLATERQLEKVERYVARareegARVLTGGErpsGADLGAgyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFD 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 151 SLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07114 376 DEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRALSPSSPFGGFKDSGIGRENGIEAIREYT 450
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
3-231 |
5.85e-25 |
|
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: 102.96 E-value: 5.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLP-ALQSTITRFYGDDPQ 81
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEkAKARALKRVVGDPFR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 82 SSPNLGRIINQKQFQRL----------RALLGCGRVAIGGQSdesdRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQS 151
Cdd:cd07142 320 KGVEQGPQVDKEQFEKIlsyiehgkeeGATLITGGDRIGSKG----YYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 152 LDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGN--DGFMhmtlASLPFGGVGASGMGRYHGKFSFDTFSHH 229
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFD----ASIPFGGYKMSGIGREKGIYALNNYLQV 471
|
..
gi 586946394 230 RA 231
Cdd:cd07142 472 KA 473
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
10-215 |
6.00e-25 |
|
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: 103.43 E-value: 6.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 10 PVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGR 88
Cdd:cd07083 265 RLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEnGTDLGP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 89 IINQKQFQRLRALLGCGR----VAIGGQSDESDRY-IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD--EAIEFINR 161
Cdd:cd07083 345 VIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANS 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 586946394 162 REKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMG 215
Cdd:cd07083 425 TPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTN 478
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
3-220 |
9.58e-25 |
|
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: 102.39 E-value: 9.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVAnRVAWFRYF-NAGQTCVAPD--YVLCS--PEMQERLLPALQSTITrfyG 77
Cdd:cd07101 214 RAGRRLIGCSLELGGKNPMIVLEDADLDKAA-AGAVRACFsNAGQLCVSIEriYVHESvyDEFVRRFVARTRALRL---G 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 78 DDPQSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQS--DESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQ 150
Cdd:cd07101 290 AALDYGPDMGSLISQAQLDRVTAHVDDAVakgatVLAGGRArpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVA 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586946394 151 SLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMhMTLASL--PFGGVGASGMGRYHGK 220
Cdd:cd07101 370 DDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYA-AAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
12-215 |
1.61e-24 |
|
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: 101.67 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 12 TLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRII 90
Cdd:cd07146 225 LLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 91 NQK---QFQR--LRALLGCGRVAIGGQSDESdrYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKP 165
Cdd:cd07146 305 DEEaaiQIENrvEEAIAQGARVLLGNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 586946394 166 LALYAFSNSSQVVKRVLTQTSSGGFCGNDGfMHMTLASLPFGGVGASGMG 215
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFGGVKDSGLG 431
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-226 |
1.84e-24 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 101.91 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFY-GDD 79
Cdd:PRK11241 242 MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHiGDG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQSSPNLGRIINQKQFQRLR-----ALLGCGRVAIGGQSDE-SDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD 153
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586946394 154 EAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLAslPFGGVGASGMGRYHGKFSFDTF 226
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGLGREGSKYGIEDY 472
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
1-228 |
5.63e-24 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 100.67 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDD 79
Cdd:PLN02766 254 MQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 P-QSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQS-DESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSL 152
Cdd:PLN02766 334 PfDPRARQGPQVDKQQFEKILSYIEHGKregatLLTGGKPcGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTlaSLPFGGVGASGMGRYHGKFSFDTFSH 228
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDP--DCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
6-215 |
4.98e-23 |
|
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: 97.68 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 6 KHLTPVTLELGGKNPCYVDDNCDPQTVANRV--AWFRYfnAGQTCVApdyvlCS---------PEMQERLLPALQSTITr 74
Cdd:cd07124 273 KWLKRVIAEMGGKNAIIVDEDADLDEAAEGIvrSAFGF--QGQKCSA-----CSrvivhesvyDEFLERLVERTKALKV- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 75 fyGDDPQSSPNLGRIINQKQFQRLR----ALLGCGRVAIGGQSDESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIV 147
Cdd:cd07124 345 --GDPEDPEVYMGPVIDKGARDRIRryieIGKSEGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVI 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586946394 148 NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMG 215
Cdd:cd07124 423 KAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
1-228 |
8.42e-23 |
|
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: 96.99 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP 80
Cdd:cd07090 211 MSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDP 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 -QSSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDR------YIAPTVLVDVQEMEPVMQEEIFGPILPIVN 148
Cdd:cd07090 291 lDEDTQMGALISEEHLEKVLGYIESAkqegaKVLCGGERVVPEDglengfYVSPCVLTDCTDDMTIVREEIFGPVMSILP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 149 VQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTFSH 228
Cdd:cd07090 371 FDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVPFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
3-227 |
1.03e-22 |
|
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: 96.55 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPAL-QSTITRFYGDDPQ 81
Cdd:cd07097 233 AAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALvERTKALKVGDALD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 82 SSPNLGRIINQKQFQR-LRAL-LG---CGRVAIGGQ---SDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD 153
Cdd:cd07097 313 EGVDIGPVVSERQLEKdLRYIeIArseGAKLVYGGErlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 154 EAIEFINRREkplalyaFSNSSQVVKRVL---------TQTssggfcgndGFMHMTLAS------LPFGGVGASGMG-RY 217
Cdd:cd07097 393 EALAIANDTE-------FGLSAGIVTTSLkhathfkrrVEA---------GVVMVNLPTagvdyhVPFGGRKGSSYGpRE 456
|
250
....*....|
gi 586946394 218 HGKFSFDTFS 227
Cdd:cd07097 457 QGEAALEFYT 466
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
1-228 |
1.83e-22 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 96.34 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDpqtVANRVAW--FRYF-NAGQTCVAPDYVLC----SPEMQERLLPALQStIT 73
Cdd:PLN02467 247 MTAAAQMVKPVSLELGGKSPIIVFDDVD---LDKAVEWamFGCFwTNGQICSATSRLLVheriASEFLEKLVKWAKN-IK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 74 rfYGDDPQSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQSDESDR---YIAPTVLVDVQEMEPVMQEEIFGPILP 145
Cdd:PLN02467 323 --ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKsegatILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLC 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 146 IVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNDGFmhmtlASLPFGGVGASGMGRYHGKFS 222
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVwinCSQPCF-----CQAPWGGIKRSGFGRELGEWG 475
|
....*.
gi 586946394 223 FDTFSH 228
Cdd:PLN02467 476 LENYLS 481
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
6-213 |
2.26e-22 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 95.77 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 6 KHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVApdyvlCS---------PEMQERLLpALQSTITrfY 76
Cdd:PRK03137 278 IWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA-----CSraivhedvyDEVLEKVV-ELTKELT--V 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 77 GDdPQSSPNLGRIINQKQFQRLRALL----GCGRVAIGGQSDESDRY-IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQS 151
Cdd:PRK03137 350 GN-PEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586946394 152 LDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASG 213
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 490
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
1-219 |
6.46e-22 |
|
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: 94.36 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANR-VAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDD 79
Cdd:cd07107 211 MRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAaVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGD 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PqSSPN--LGRIINQKQFQRLRALLGCGR------VAIGGQSD----ESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIV 147
Cdd:cd07107 291 P-TDPAttMGPLVSRQQYDRVMHYIDSAKregarlVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVL 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586946394 148 NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTlaSLPFGGVGASGMGRYHG 219
Cdd:cd07107 370 RWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-231 |
7.15e-22 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 94.49 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEM-QERLLPALQSTITRFYGDDPQ 81
Cdd:PLN02466 294 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVyDEFVEKAKARALKRVVGDPFK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 82 SSPNLGRIINQKQFQR-LR---------ALLGCGrvaiGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQS 151
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKiLRyiksgvesgATLECG----GDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKD 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 152 LDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGN--DGFMhmtlASLPFGGVGASGMGRYHGKFSFDTFSHH 229
Cdd:PLN02466 450 LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFD----AAIPFGGYKMSGIGREKGIYSLNNYLQV 525
|
..
gi 586946394 230 RA 231
Cdd:PLN02466 526 KA 527
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
1-228 |
7.68e-22 |
|
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: 94.33 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNP-------CYVDDNCDPQTVANRVAWFryFNAGQTCVAPDYVLCSPEMQERLLPALQSTIT 73
Cdd:cd07559 231 MQYAAENLIPVTLELGGKSPniffddaMDADDDFDDKAEEGQLGFA--FNQGEVCTCPSRALVQESIYDEFIERAVERFE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 74 RFYGDDPQ-SSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQSDESDR-----YIAPTVLVDVQEMEPVMQEEIFGP 142
Cdd:cd07559 309 AIKVGNPLdPETMMGAQVSKDQLEKILSYVDIGKeegaeVLTGGERLTLGGldkgyFYEPTLIKGGNNDMRIFQEEIFGP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 143 ILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFS 222
Cdd:cd07559 389 VLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNC--YHQYPAHAPFGGYKKSGIGRETHKMM 466
|
....*.
gi 586946394 223 FDTFSH 228
Cdd:cd07559 467 LDHYQQ 472
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
1-227 |
3.63e-21 |
|
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: 92.41 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC-SPEMQERLLPALQSTITRFYGD 78
Cdd:cd07141 241 QQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVqESIYDEFVKRSVERAKKRVVGN 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 DPQSSPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSL 152
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKkegaklECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 153 DEAIEFINRREKPLALYAFSNSsqvVKRVLTQTSS--GGFCGNDGFMHMTlASLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKD---IDKAITFSNAlrAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYT 473
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
3-219 |
3.89e-21 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 92.25 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD--YVLCS--PEMQERLLPALQS-TITRFYG 77
Cdd:PRK09407 250 QAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIEriYVHESiyDEFVRAFVAAVRAmRLGAGYD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 78 DDPQsspnLGRIINQKQFQRLRALLGCGR-----VAIGGQS--DESDRYIAPTVLVDV-QEMEpVMQEEIFGPILPIVNV 149
Cdd:PRK09407 330 YSAD----MGSLISEAQLETVSAHVDDAVakgatVLAGGKArpDLGPLFYEPTVLTGVtPDME-LAREETFGPVVSVYPV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586946394 150 QSLDEAIEFINrrEKPLALYA--FSNSSQVVKRVLTQTSSGGFCGNDGFMhMTLASL--PFGGVGASGMGRYHG 219
Cdd:PRK09407 405 ADVDEAVERAN--DTPYGLNAsvWTGDTARGRAIAARIRAGTVNVNEGYA-AAWGSVdaPMGGMKDSGLGRRHG 475
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
1-227 |
4.07e-21 |
|
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: 92.02 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC----SPEMQERLLPALQStITRFY 76
Cdd:cd07120 214 MAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVqrsiADEVRDRLAARLAA-VKVGP 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 77 GDDPQSspNLGRIINQKQFQRL-----RALLGCGRVAI-GGQSDESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIV 147
Cdd:cd07120 293 GLDPAS--DMGPLIDRANVDRVdrmveRAIAAGAEVVLrGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 148 NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfmHMTL-ASLPFGGVGASGMGRYHGKFSFDTF 226
Cdd:cd07120 371 TFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLfAEAEEGGYRQSGLGRLHGVAALEDF 447
|
.
gi 586946394 227 S 227
Cdd:cd07120 448 I 448
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
3-227 |
5.44e-21 |
|
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: 91.75 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS 82
Cdd:cd07117 233 AAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 83 -SPNLGRIINQKQFQRLRALLGCG-----RVAIGGQ---SDESDR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQS 151
Cdd:cd07117 313 pDTQMGAQVNKDQLDKILSYVDIAkeegaKILTGGHrltENGLDKgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586946394 152 LDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNT--YNQIPAGAPFGGYKKSGIGRETHKSMLDAYT 466
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
3-216 |
1.37e-20 |
|
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: 90.38 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHltpVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS----PEMQERLLPALQSTITrfyGD 78
Cdd:cd07147 221 AGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHrsvyDEFKSRLVARVKALKT---GD 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 DPQSSPNLGRIINQKQFQRLR-----ALLGCGRVAIGGQSDESdrYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD 153
Cdd:cd07147 295 PKDDATDVGPMISESEAERVEgwvneAVDAGAKLLTGGKRDGA--LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFD 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 154 EAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGND--GFM--HMtlaslPFGGVGASGMGR 216
Cdd:cd07147 373 EALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDvpTFRvdHM-----PYGGVKDSGIGR 434
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-226 |
2.42e-20 |
|
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: 89.88 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 4 AAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF---YGDDP 80
Cdd:cd07085 234 AAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkvgAGDDP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 qsSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDRY-----IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQ 150
Cdd:cd07085 314 --GADMGPVISPAAKERIEGLIESGveegaKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 151 SLDEAIEFINRREkplalYA-----FSNSSQVVKRVLTQTsSGGFCG-NDGfMHMTLASLPFGGVGASGMGRYH--GKFS 222
Cdd:cd07085 392 TLDEAIAIINANP-----YGngaaiFTRSGAAARKFQREV-DAGMVGiNVP-IPVPLAFFSFGGWKGSFFGDLHfyGKDG 464
|
....
gi 586946394 223 FDTF 226
Cdd:cd07085 465 VRFY 468
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-232 |
2.82e-19 |
|
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: 86.85 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS 82
Cdd:cd07086 234 TVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 83 SPNL-GRIINQKQFQR-LRAL-----LGcGRVAIGG---QSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSL 152
Cdd:cd07086 314 EGTLvGPLINQAAVEKyLNAIeiaksQG-GTVLTGGkriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGgfCG----NDGfmhmTL---ASLPFGGVGASGMGRYHGKFSFDT 225
Cdd:cd07086 393 EEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSD--CGivnvNIP----TSgaeIGGAFGGEKETGGGRESGSDAWKQ 466
|
....*..
gi 586946394 226 FSHHRAC 232
Cdd:cd07086 467 YMRRSTC 473
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
10-216 |
1.79e-18 |
|
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: 84.55 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 10 PVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGR 88
Cdd:cd07082 244 RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPwDNGVDITP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 89 IINQKQFQRLRALL------GcGRVAIGGQSdESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRR 162
Cdd:cd07082 324 LIDPKSADFVEGLIddavakG-ATVLNGGGR-EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKS 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586946394 163 EKPLALYAFSNSSQVVKRVLTQTSSG-----GFC--GNDGFmhmtlaslPFGGVGASGMGR 216
Cdd:cd07082 402 NYGLQASIFTKDINKARKLADALEVGtvninSKCqrGPDHF--------PFLGRKDSGIGT 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-227 |
1.01e-17 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 82.24 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNPCYVDDNCDPQT------VANrvawfrYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITR 74
Cdd:PRK13252 237 MAAAAASLKEVTMELGGKSPLIVFDDADLDRaadiamLAN------FYSSGQVCTNGTRVFVQKSIKAAFEARLLERVER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 75 FYGDDPQS-SPNLGRIINQKQFQRLR----------ALLGCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPI 143
Cdd:PRK13252 311 IRIGDPMDpATNFGPLVSFAHRDKVLgyiekgkaegARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPV 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 144 LPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSgGFC-----GNdgfmhmTLASLPFGGVGASGMGRYH 218
Cdd:PRK13252 391 MSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEA-GICwintwGE------SPAEMPVGGYKQSGIGREN 463
|
....*....
gi 586946394 219 GKFSFDTFS 227
Cdd:PRK13252 464 GIATLEHYT 472
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
11-220 |
1.08e-17 |
|
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: 82.06 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 11 VTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRI 89
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 90 INQKQFQRLRALLGCGRvAIGGQSDESDR-------YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRR 162
Cdd:cd07111 332 VDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 586946394 163 EKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGK 220
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWING--HNLFDAAAGFGGYRESGFGREGGK 466
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
13-216 |
1.99e-17 |
|
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: 81.16 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 13 LELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQ-ERLLPALQSTITRFYGDDPQSSPN--LGRI 89
Cdd:cd07095 205 LEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPfmGPLI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 90 INQKQFQRLRA---LLGCGRVAIGGQS--DESDRYIAPTvLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK 164
Cdd:cd07095 285 IAAAAARYLLAqqdLLALGGEPLLAMErlVAGTAFLSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRF 363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 586946394 165 PLALYAFSNSSQVVKRVLTQTSSGGFCGNdgfMHMTLAS--LPFGGVGASGMGR 216
Cdd:cd07095 364 GLSAGLLSDDEALFERFLARIRAGIVNWN---RPTTGASstAPFGGVGLSGNHR 414
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
3-227 |
3.56e-17 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 80.71 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 3 AAAKHLTPVTLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP- 80
Cdd:PRK09847 256 AGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPl 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNLGRIINQKQFQRLRALL----GCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAI 156
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIregeSKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586946394 157 EFINRREKPLALYAFSNSSQVVKRVLTQTSSGG-FCG--NDGFMhmtlaSLPFGGVGASGMGRYHGKFSFDTFS 227
Cdd:PRK09847 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSvFVNnyNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFT 484
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
1-236 |
4.12e-16 |
|
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: 77.49 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 1 MTAAAKHLTPVTLELGGKNP-CYVDD--NCDPQTVANRVAWFRYF--NAGQTCVAPDYVLCSPEMQERLLP-ALQSTITR 74
Cdd:cd07116 231 MQYASENIIPVTLELGGKSPnIFFADvmDADDAFFDKALEGFVMFalNQGEVCTCPSRALIQESIYDRFMErALERVKAI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 75 FYGDDPQSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQ-----SDESDRYIAPTVLVDVQEMEpVMQEEIFGPIL 144
Cdd:cd07116 311 KQGNPLDTETMIGAQASLEQLEKILSYIDIGKeegaeVLTGGErnelgGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 145 PIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgFMHMTLASLPFGGVGASGMGRYHGKFSFD 224
Cdd:cd07116 390 AVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIGRENHKMMLD 467
|
250
....*....|..
gi 586946394 225 TFSHHRaCLLRS 236
Cdd:cd07116 468 HYQQTK-NLLVS 478
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
9-215 |
8.62e-14 |
|
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: 70.53 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 9 TPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLG 87
Cdd:cd07148 226 TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLvVGDPTDPDTEVG 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 88 RIINQKQFQRLR-----ALLGCGRVAIGGQSdESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINrr 162
Cdd:cd07148 306 PLIRPREVDRVEewvneAVAAGARLLCGGKR-LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQAN-- 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 163 EKPLALYA--FSNSSQVVKRVLTQTSSGGFCGNDgfmHMTLAS--LPFGGVGASGMG 215
Cdd:cd07148 383 SLPVAFQAavFTKDLDVALKAVRRLDATAVMVND---HTAFRVdwMPFAGRRQSGYG 436
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
4-226 |
3.43e-13 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 68.73 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 4 AAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSS 83
Cdd:PRK13968 224 AGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 84 PN-LGRI----INQKQFQRLRALLGCG-RVAIGGQSDESD-RYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAI 156
Cdd:PRK13968 304 ENaLGPMarfdLRDELHHQVEATLAEGaRLLLGGEKIAGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHAL 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586946394 157 EFINRREKPLALYAFSNSSQVVKRVLTQTSSG-----GFCGNDgfmhmtlASLPFGGVGASGMGRYHGKFSFDTF 226
Cdd:PRK13968 384 ELANDSEFGLSATIFTTDETQARQMAARLECGgvfinGYCASD-------ARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
14-213 |
6.72e-13 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 68.00 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 14 ELGGKNPCYVDDNCDPQTVAN---RVAwFRYfnAGQTCVAPD--YVLCS--PEMQERLLPALqSTITrfYGDDPQSSPNL 86
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTatvRGA-FEY--QGQKCSAASraYVPESlwPEVKERLLEEL-KEIK--MGDPDDFSNFM 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 87 GRIINQKQFQRLRALLGCGR------VAIGGQSDESDRY-IAPTVLVDVQEMEPVMQEEIFGPILpivNVQSLDEAiEFi 159
Cdd:cd07123 358 GAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL---TVYVYPDS-DF- 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586946394 160 nrrEKPLAL------YA-----FSNSSQVVKRVLT--QTSSGGFCGNDGFMHMTLASLPFGGVGASG 213
Cdd:cd07123 433 ---EETLELvdttspYAltgaiFAQDRKAIREATDalRNAAGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
2-216 |
4.62e-12 |
|
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: 65.59 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 2 TAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP- 80
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPl 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 QSSPNLGRIINQKQFQRL-----RALLGCGRVAIGG-QSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQS--L 152
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGR 216
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT--YNKTDVAAPFGGFKQSGFGK 466
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
4-216 |
6.03e-12 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 65.14 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 4 AAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQE---RLLPALQSTITrfYGD-- 78
Cdd:PRK09406 221 AGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDafaEKFVARMAALR--VGDpt 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 79 DPQS-----SPNLGRIINQKQFQRlrALLGCGRVAIGGQS-DESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSL 152
Cdd:PRK09406 299 DPDTdvgplATEQGRDEVEKQVDD--AVAAGATILCGGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADI 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586946394 153 DEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGR 216
Cdd:PRK09406 377 DEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFGGVKRSGYGR 438
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
13-213 |
2.32e-11 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 63.44 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 13 LELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQ-ERLLPALQSTITRF----YGDDPQssPNLG 87
Cdd:PRK09457 242 LEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLtvgrWDAEPQ--PFMG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 88 RIINQKQFQRL----RALLGCGRVAI--GGQSDESDRYIAPTvLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINR 161
Cdd:PRK09457 320 AVISEQAAQGLvaaqAQLLALGGKSLleMTQLQAGTGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANN 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 586946394 162 REKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfmHMTLAS--LPFGGVGASG 213
Cdd:PRK09457 399 TRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNK---PLTGASsaAPFGGVGASG 449
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-232 |
2.92e-11 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 63.31 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 13 LELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP------------ 80
Cdd:PLN02315 265 LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPlekgtllgplht 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 81 -QSSPNLGRIINQKQFQrlrallgCGRVAIGGQSDESD-RYIAPTVlVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEF 158
Cdd:PLN02315 345 pESKKNFEKGIEIIKSQ-------GGKILTGGSAIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEI 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 159 INRREKPLALYAFSNSSQVVKRVLTQTSSGgfCGndgfmhMTLASLP---------FGGVGASGMGRYHGKFSFDTFSHH 229
Cdd:PLN02315 417 NNSVPQGLSSSIFTRNPETIFKWIGPLGSD--CG------IVNVNIPtngaeiggaFGGEKATGGGREAGSDSWKQYMRR 488
|
...
gi 586946394 230 RAC 232
Cdd:PLN02315 489 STC 491
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-215 |
8.80e-10 |
|
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: 58.75 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 2 TAAAKH-----------LTPVTLELGGKNPCYVDDNCDP-QTVANRVA-WFRyfNAGQTCVAPDyVLC-----SPEMQER 63
Cdd:cd07125 256 TETAKLinralaerdgpILPLIAETGGKNAMIVDSTALPeQAVKDVVQsAFG--SAGQRCSALR-LLYlqeeiAERFIEM 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 64 LLPALQSTITrfygDDPQS-SPNLGRIINQKQFQRLRALL----GCGRVAIGGQSDESD-RYIAPTVLVDVQEmePVMQE 137
Cdd:cd07125 333 LKGAMASLKV----GDPWDlSTDVGPLIDKPAGKLLRAHTelmrGEAWLIAPAPLDDGNgYFVAPGIIEIVGI--FDLTT 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 138 EIFGPILPIV--NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfmhMTLA---SLPFGGVGAS 212
Cdd:cd07125 407 EVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRN---ITGAivgRQPFGGWGLS 483
|
...
gi 586946394 213 GMG 215
Cdd:cd07125 484 GTG 486
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
10-215 |
9.86e-10 |
|
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: 58.77 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 10 PVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGR 88
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPhLLTTDVGP 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 89 IINQKQFQRL----RALLGCGR-----VAIGGQSDESDRYIAPTV--LVDVQEMepvmQEEIFGPILPIV--NVQSLDEA 155
Cdd:TIGR01238 348 VIDAEAKQNLlahiEHMSQTQKkiaqlTLDDSRACQHGTFVAPTLfeLDDIAEL----SEEVFGPVLHVVryKARELDQI 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 156 IEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMG 215
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTG 483
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
15-228 |
1.98e-08 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 54.75 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 15 LGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC---SPEMQERLL---PALQSTItrfyGDDPQSspNLGR 88
Cdd:PLN02419 358 MGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVeraKALKVTC----GSEPDA--DLGP 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 89 IINQKQFQRLRALLGCG-----RVAIGGQS-----DESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEF 158
Cdd:PLN02419 432 VISKQAKERICRLIQSGvddgaKLLLDGRDivvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586946394 159 INRREKPLALYAFSNSSQVVKRVLTQTSSGGFcGNDGFMHMTLASLPFGGVGASGMG--RYHGKFSFDTFSH 228
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQI-GINVPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
8-215 |
4.09e-08 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 53.61 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 8 LTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLG 87
Cdd:PLN00412 258 MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDIT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 88 RIINQKQFQRLRALLGCGRVAIGGQSDESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK 164
Cdd:PLN00412 338 PVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNF 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 586946394 165 PLALYAFSNS-------SQVVKRVLTQTSSGGFCGNDGFmhmtlaslPFGGVGASGMG 215
Cdd:PLN00412 418 GLQGCVFTRDinkailiSDAMETGTVQINSAPARGPDHF--------PFQGLKDSGIG 467
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
14-181 |
4.67e-08 |
|
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: 53.64 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 14 ELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPE----MQERLLP-----ALQSTITRFYGDDPQSSP 84
Cdd:cd07127 305 EKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtDDGRKSFdevaaDLAAAIDGLLADPARAAA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 85 NLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYI-----APTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFI 159
Cdd:cd07127 385 LLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPdarvrTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
170 180
....*....|....*....|....*
gi 586946394 160 NR--REK-PLALYAFSNSSQVVKRV 181
Cdd:cd07127 465 REsvREHgAMTVGVYSTDPEVVERV 489
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
13-160 |
1.46e-06 |
|
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: 48.74 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 13 LELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLcspeMQERLLPALQSTITRFYGD----DPQSSPNL-G 87
Cdd:cd07130 243 LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI----VHESIYDEVLERLKKAYKQvrigDPLDDGTLvG 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 88 RIINQKQFQRLRALL------GcGRVAIGGQS-DESDRYIAPTVlVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFIN 160
Cdd:cd07130 319 PLHTKAAVDNYLAAIeeaksqG-GTVLFGGKViDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
7-219 |
3.39e-05 |
|
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: 44.54 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 7 HLTPVTLELGGKNPCYVDDNCDP-QTVANRVAWFRYFNAGQTCVAPD--YVLCSPEMQeRLLPALQSTITRfygddpqSS 83
Cdd:cd07084 200 KQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSGQKCTAQSmlFVPENWSKT-PLVEKLKALLAR-------RK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 84 PN---LGRIIN---QKQFQRLRALLGcgRVAIGGQSDESDRYI--------APTVLVDVQE---MEPVMQEEIFGPILPI 146
Cdd:cd07084 272 LEdllLGPVQTfttLAMIAHMENLLG--SVLLFSGKELKNHSIpsiygacvASALFVPIDEilkTYELVTEEIFGPFAIV 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586946394 147 VNVQSLDEA--IEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGfcgndgfmhMTLASLPFGGVGASGMgrYHG 219
Cdd:cd07084 350 VEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAG---------RTYAILRGRTGVAPNQ--NHG 413
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
10-163 |
5.48e-05 |
|
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: 44.07 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 10 PVTLELGGKNPCYVDdncdPQTVANR--------VAWFRyFNAGQTCVAPDYVLC--SPEmQERLLPALQSTITRFygdD 79
Cdd:cd07129 218 PFYAELGSVNPVFIL----PGALAERgeaiaqgfVGSLT-LGAGQFCTNPGLVLVpaGPA-GDAFIAALAEALAAA---P 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 80 PQS--SPNLGRIInQKQFQRLRALLGcGRVAIGGQSDESDRYIAPTVL-VDVQEM--EPVMQEEIFGPILPIVNVQSLDE 154
Cdd:cd07129 289 AQTmlTPGIAEAY-RQGVEALAAAPG-VRVLAGGAAAEGGNQAAPTLFkVDAAAFlaDPALQEEVFGPASLVVRYDDAAE 366
|
....*....
gi 586946394 155 AIEFINRRE 163
Cdd:cd07129 367 LLAVAEALE 375
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
44-187 |
2.79e-04 |
|
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: 41.87 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 44 AGQTCVAPDYVLCsPE-----MQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRA----LLGCGRVAIGGQSD 114
Cdd:cd07128 288 AGQKCTAIRRAFV-PEarvdaVIEALKARLAKVVV---GDPRLEGVRMGPLVSREQREDVRAavatLLAEAEVVFGGPDR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 115 ESDR--------YIAPTVLVDVQEMEP--VMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQ 184
Cdd:cd07128 364 FEVVgadaekgaFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLG 443
|
...
gi 586946394 185 TSS 187
Cdd:cd07128 444 AAP 446
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
4-161 |
4.62e-04 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 41.34 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 4 AAKHLTPVTL--ELGGKNPCYVDDNCDPQTVANRV---AwFRyfNAGQTCVAPDyVLCSPE-MQERLLPALQSTITRFYG 77
Cdd:PRK11904 784 AARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVvtsA-FR--SAGQRCSALR-VLFVQEdIADRVIEMLKGAMAELKV 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586946394 78 DDPQS-SPNLGRIINQKQFQRLRA----------LLGcgRVAIGGQSDESDrYIAPTvLVDVQEMEpVMQEEIFGPILPI 146
Cdd:PRK11904 860 GDPRLlSTDVGPVIDAEAKANLDAhiermkrearLLA--QLPLPAGTENGH-FVAPT-AFEIDSIS-QLEREVFGPILHV 934
|
170
....*....|....*..
gi 586946394 147 V--NVQSLDEAIEFINR 161
Cdd:PRK11904 935 IryKASDLDKVIDAINA 951
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
108-157 |
3.07e-03 |
|
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: 38.76 E-value: 3.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 586946394 108 AIGGQSDESDRYIaptvLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIE 157
Cdd:cd07121 304 AAGIEVPADIRLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| |
