|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-431 |
0e+00 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 675.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 5 QTLLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFE-QLFEITVPLGVIDYYRRHLVDLMAP 83
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEaYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 84 QQVEIPpgLEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEA 163
Cdd:cd07087 81 RRVSVP--LLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 164 VTVVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQ 243
Cdd:cd07087 159 VAVVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 244 WCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQPEKVVHGGRFDIPGRYVEPTVLY 323
Cdd:cd07087 239 TCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 324 PSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDSLPF 403
Cdd:cd07087 319 DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPF 398
|
410 420
....*....|....*....|....*...
gi 502316442 404 GGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07087 399 GGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-447 |
0e+00 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 567.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 5 QTLLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFE-QLFEITVPLGVIDYYRRHLVDLMAP 83
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEaYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 84 QQVEIPpgLEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEA 163
Cdd:cd07136 81 KRVKTP--LLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 164 VTVVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGH--NAis 241
Cdd:cd07136 159 VAVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKflNA-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 242 GQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQPEKVVHGGRFDIPGRYVEPTV 321
Cdd:cd07136 237 GQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 322 LYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDSL 401
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYL 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 502316442 402 PFGGVGLSGMGKYYGQAGFDALSNTKSLLiGNPDKvLDV---FPPYAGK 447
Cdd:cd07136 397 PFGGVGNSGMGSYHGKYSFDTFSHKKSIL-KKSTW-FDLplrYPPYKGK 443
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
5-444 |
2.64e-172 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 492.62 E-value: 2.64e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 5 QTLLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFE-QLFEITVPLGVIDYYRRHLVDLMAP 83
Cdd:PTZ00381 10 PPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFEtKMTEVLLTVAEIEHLLKHLDEYLKP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 84 QQVEIP----PGleaEGYrgmIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYF 159
Cdd:PTZ00381 90 EKVDTVgvfgPG---KSY---IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 160 APEAVTVVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNA 239
Cdd:PTZ00381 164 DPSYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 240 ISGQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQPE--KVVHGGRFDIPGRYV 317
Cdd:PTZ00381 244 NAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHggKVVYGGEVDIENKYV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 318 EPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCW 397
Cdd:PTZ00381 324 APTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLL 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 502316442 398 IDSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLIGNPDKVLDV---FPPY 444
Cdd:PTZ00381 404 NPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLslrYPPY 453
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
7-445 |
1.36e-170 |
|
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: 486.34 E-value: 1.36e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 7 LLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFE-QLFEITVPLGVIDYYRRHLVDLMAPQQ 85
Cdd:cd07132 3 AVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEaVLSEILLVKNEIKYAISNLPEWMKPEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 86 VEIP-PGLEAEGYrgmIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV 164
Cdd:cd07132 83 VKKNlATLLDDVY---IYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 165 TVVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG--HNAisG 242
Cdd:cd07132 160 PVVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGkfINA--G 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 243 QWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQPEKVVHGGRFDIPGRYVEPTVL 322
Cdd:cd07132 238 QTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 323 YPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDSLP 402
Cdd:cd07132 318 TDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 502316442 403 FGGVGLSGMGKYYGQAGFDALSNTKSLLIG--NPDKVLDV-FPPYA 445
Cdd:cd07132 398 FGGVGNSGMGAYHGKYSFDTFSHKRSCLVKslNMEKLNSLrYPPYS 443
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
7-430 |
1.94e-162 |
|
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: 465.54 E-value: 1.94e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 7 LLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLF-EITVPLGVIDYYRRHLVDLMAPQQ 85
Cdd:cd07135 10 IHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLtEVSGVKNDILHMLKNLKKWAKDEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 86 VEIPPGLEAEGyRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVT 165
Cdd:cd07135 90 VKDGPLAFMFG-KPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWC 245
Cdd:cd07135 169 VVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQIC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 246 IAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQ--PEKVVHGGRFDIPGRYVEPTVLY 323
Cdd:cd07135 249 VAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIPPTIVS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 324 PSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDSLPF 403
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPF 408
|
410 420
....*....|....*....|....*..
gi 502316442 404 GGVGLSGMGKYYGQAGFDALSNTKSLL 430
Cdd:cd07135 409 GGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
5-431 |
2.43e-156 |
|
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: 449.75 E-value: 2.43e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 5 QTLLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFE-QLFEITVPLGVIDYYRRHLVDLMAP 83
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEvDLTEILPVLSEINHAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 84 QQVEIPPGLEaeGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEA 163
Cdd:cd07134 81 KRVRTPLLLF--GTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 164 VTVVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQ 243
Cdd:cd07134 159 VAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 244 WCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSR--SPDFARMISAHDAQRVANYIQPE-----KVVHGGRFDIPGRY 316
Cdd:cd07134 239 TCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARkaSPDLARIVNDRHFDRLKGLLDDAvakgaKVEFGGQFDAAQRY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHC 396
Cdd:cd07134 319 IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHF 398
|
410 420 430
....*....|....*....|....*....|....*
gi 502316442 397 WIDSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07134 399 LNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
5-430 |
7.99e-144 |
|
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: 418.04 E-value: 7.99e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 5 QTLLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDF-RKPPFEQLF-EITVPLGVIDYYRRHLVDLMA 82
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLaEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 83 PQQVEIPPGLEaeGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPE 162
Cdd:cd07133 81 PSRRHVGLLFL--PAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 163 AVTVVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISG 242
Cdd:cd07133 159 EVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 243 QWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSrSPDFARMISAHDAQRVANYIQPEK--------VVHGGRFDIPG 314
Cdd:cd07133 239 QTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLAD-NPDYTSIINERHYARLQGLLEDARakgarvieLNPAGEDFAAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 315 RYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNL 394
Cdd:cd07133 318 RKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 502316442 395 HCWIDSLPFGGVGLSGMGKYYGQAGFDALSNTKSLL 430
Cdd:cd07133 398 HVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVF 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
7-430 |
1.17e-135 |
|
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: 397.17 E-value: 1.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 7 LLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLF-EITVPLGVIDYYRRHLVDLMAPQQ 85
Cdd:cd07137 4 LVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRdEVSVLVSSCKLAIKELKKWMAPEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 86 VEIPpgLEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVT 165
Cdd:cd07137 84 VKTP--LTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIA---WGHNAisG 242
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAggkWGCNN--G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 243 QWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQP----EKVVHGGRFDIPGRYVE 318
Cdd:cd07137 240 QACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDpsvaDKIVHGGERDEKNLYIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 319 PTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWI 398
Cdd:cd07137 320 PTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAI 399
|
410 420 430
....*....|....*....|....*....|..
gi 502316442 399 DSLPFGGVGLSGMGKYYGQAGFDALSNTKSLL 430
Cdd:cd07137 400 DTLPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
8-431 |
1.41e-130 |
|
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: 384.25 E-value: 1.41e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 8 LDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVE 87
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 88 IPPGLEAegyrgMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TV 166
Cdd:cd07078 84 PDPGELA-----IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVlNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 167 VTGGREEIS-ALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQW 244
Cdd:cd07078 159 VTGDGDEVGaALASHPrVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 245 CIAPGYVYVHHSIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYI-----QPEKVVHGGRFD--IPGRY 316
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPlDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLegGKGYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHC 396
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA 398
|
410 420 430
....*....|....*....|....*....|....*
gi 502316442 397 wIDSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07078 399 -EPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
12-430 |
1.77e-110 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 334.77 E-value: 1.77e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLF-EITVPLGVIDYYRRHLVDLMAPQQVEIPp 90
Cdd:PLN02203 16 RETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRdEVGVLTKSANLALSNLKKWMAPKKAKLP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 91 gLEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVTVVTGG 170
Cdd:PLN02203 95 -LVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 171 REEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVD---ATANLDIAIDRIA---WGhnAISGQW 244
Cdd:PLN02203 174 PAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVggkWG--SCAGQA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 245 CIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQPEKV----VHGGRFDIPGRYVEPT 320
Cdd:PLN02203 252 CIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVaasiVHGGSIDEKKLFIEPT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 321 VLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDS 400
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDS 411
|
410 420 430
....*....|....*....|....*....|
gi 502316442 401 LPFGGVGLSGMGKYYGQAGFDALSNTKSLL 430
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
9-431 |
9.59e-107 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 321.10 E-value: 9.59e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 9 DRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVEI 88
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 89 PPGLEAegyrgMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPE-AVTVV 167
Cdd:cd06534 81 DPGGEA-----YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPgVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 168 TGGREEIS-ALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWC 245
Cdd:cd06534 156 PGGGDEVGaALLSHPrVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 246 IAPGYVYVHHSIADDFIARIKrsltamygedpsrspdfarmisahdaqrvanyiqpekvvhggrfdipgryvepTVLYPS 325
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 326 SWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCwIDSLPFGG 405
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GPEAPFGG 341
|
410 420
....*....|....*....|....*.
gi 502316442 406 VGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
19-431 |
2.73e-104 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 318.61 E-value: 2.73e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 19 ATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYrrhlVDLMAPQQVEIPPgLEAEGYR 98
Cdd:COG1012 60 AATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYY----AGEARRLYGETIP-SDAPGTR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 99 GMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLI-----PkyfaPEAVTVVTGGREE 173
Cdd:COG1012 135 AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLeeaglP----AGVLNVVTGDGSE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 174 IS-ALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYV 251
Cdd:COG1012 211 VGaALVAHPdVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 252 YVHHSIADDFIARIK---RSLTAMYGEDPSrsPDFARMISAHDAQRVANYIQP-----EKVVHGGRF--DIPGRYVEPTV 321
Cdd:COG1012 291 LVHESIYDEFVERLVaaaKALKVGDPLDPG--TDMGPLISEAQLERVLAYIEDavaegAELLTGGRRpdGEGGYFVEPTV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 322 LYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCwIDSL 401
Cdd:COG1012 369 LADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQA 447
|
410 420 430
....*....|....*....|....*....|
gi 502316442 402 PFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:COG1012 448 PFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-428 |
4.78e-94 |
|
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: 291.74 E-value: 4.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 19 ATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLvDLMAPQQVEIPPGleaegYR 98
Cdd:pfam00171 46 RKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLA-RRLDGETLPSDPG-----RL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 99 GMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTGGREEIS-A 176
Cdd:pfam00171 120 AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGeA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 177 LLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHH 255
Cdd:pfam00171 200 LVEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIARIK---RSLTAMYGEDPsrSPDFARMISAHDAQRVANYIQPE-----KVVHGGRFD-IPGRYVEPTVLYPSS 326
Cdd:pfam00171 280 SIYDEFVEKLVeaaKKLKVGDPLDP--DTDMGPLISKAQLERVLKYVEDAkeegaKLLTGGEAGlDNGYFVEPTVLANVT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 327 WDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCwIDSLPFGGV 406
Cdd:pfam00171 358 PDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGD-ADGLPFGGF 436
|
410 420
....*....|....*....|..
gi 502316442 407 GLSGMGKYYGQAGFDALSNTKS 428
Cdd:pfam00171 437 KQSGFGREGGPYGLEEYTEVKT 458
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
7-445 |
2.23e-91 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 285.79 E-value: 2.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 7 LLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFE-QLFEITVPLGVIDYYRRHLVDLMAPQQ 85
Cdd:PLN02174 15 LVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELEsSVYEVSLLRNSIKLALKQLKNWMAPEK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 86 VEIppGLEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVT 165
Cdd:PLN02174 95 AKT--SLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTGGREEISALLELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRI---AWGHNaiSG 242
Cdd:PLN02174 173 VVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIiagKWGCN--NG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 243 QWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQ----PEKVVHGGRFDIPGRYVE 318
Cdd:PLN02174 251 QACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 319 PTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWI 398
Cdd:PLN02174 331 PTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAL 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 502316442 399 DSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLIGN--PDKVLDvFPPYA 445
Cdd:PLN02174 411 HTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSlfGDSAVR-YPPYS 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
26-431 |
2.77e-90 |
|
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: 281.80 E-value: 2.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 26 RLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQqvEIPPGLEAEGYRGMIYKEP 105
Cdd:cd07099 42 RAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVLAPR--KVPTGLLMPNKKATVEYRP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 106 YGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALLELPFDF 184
Cdd:cd07099 120 YGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVlQVVTGDGATGAALIDAGVDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 185 IFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIADDFIAR 264
Cdd:cd07099 200 VAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVAR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 265 IKRSLTAM-YGEDPSRSPDFARMISAHDAQRVANYIQPE-----KVVHGG-RFDIPGRYVEPTVLYPSSWDDPAMQQEIF 337
Cdd:cd07099 280 LVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDDAvakgaKALTGGaRSNGGGPFYEPTVLTDVPHDMDVMREETF 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 338 GPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDSLPFGGVGLSGMGKYYGQ 417
Cdd:cd07099 360 GPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGA 439
|
410
....*....|....
gi 502316442 418 AGFDALSNTKSLLI 431
Cdd:cd07099 440 EGLREFCRPKAIAR 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
7-413 |
1.76e-68 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 225.17 E-value: 1.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 7 LLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITvplGVIDYYR------RHLVDL 80
Cdd:cd07149 26 AIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD---RAIETLRlsaeeaKRLAGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 81 MAPqqVEIPPGleAEGYRGMIYKEPYGPTLVIGPFNAPVLLL---LDPAIAAlaaGNPVTLKPANTTPTVAALL-QTLIP 156
Cdd:cd07149 103 TIP--FDASPG--GEGRIGFTIREPIGVVAAITPFNFPLNLVahkVGPAIAA---GNAVVLKPASQTPLSALKLaELLLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 157 KYFAPEAVTVVTGGREEI-SALLELP-FDFIFFTGSAAVGKVVMRAAAehLTPVILELGGQNPTVVDATANLDIAIDRIA 234
Cdd:cd07149 176 AGLPKGALNVVTGSGETVgDALVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 235 WGHNAISGQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYIQpE------KVVHG 307
Cdd:cd07149 254 SGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPlDEDTDVGPMISEAEAERIEEWVE-EaveggaRLLTG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 308 GRFDipGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGG 387
Cdd:cd07149 333 GKRD--GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGV 410
|
410 420
....*....|....*....|....*.
gi 502316442 388 CVNQTNLHcWIDSLPFGGVGLSGMGK 413
Cdd:cd07149 411 MINDSSTF-RVDHMPYGGVKESGTGR 435
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
12-431 |
7.95e-66 |
|
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: 218.26 E-value: 7.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATK-SAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRrHLVDLMAPQQveIPP 90
Cdd:cd07109 29 RRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYG-GAADKLHGET--IPL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 91 GleaEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTP-TVAALLQTLIPKYFAPEAVTVVTG 169
Cdd:cd07109 106 G---PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPlTALRLAELAEEAGLPAGALNVVTG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 170 -GREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG--HNAisGQWC 245
Cdd:cd07109 183 lGAEAGAALVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAiiQNA--GQTC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 246 IAPGYVYVHHSIADDFIARIK---RSLTAMYGEDpsrSPDFARMISAHDAQRVANYIQPEK-----VVHGGRF--DIP-- 313
Cdd:cd07109 261 SAGSRLLVHRSIYDEVLERLVerfRALRVGPGLE---DPDLGPLISAKQLDRVEGFVARARargarIVAGGRIaeGAPag 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 314 GRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDqraIDRFL--------GSVS-- 383
Cdd:cd07109 338 GYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD---GDRALrvarrlraGQVFvn 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 502316442 384 --FGGGCVnqtnlhcwidSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07109 415 nyGAGGGI----------ELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
54-419 |
2.78e-64 |
|
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: 215.55 E-value: 2.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 54 KPPFEQLFEITVPLGVIDYYRRHLVDLmAPQQVEIPPGlEAEGYRgmiYkEPYGPTLVIGPFNAPVLLLLDPAIAALAAG 133
Cdd:cd07124 121 KNWAEADADVAEAIDFLEYYAREMLRL-RGFPVEMVPG-EDNRYV---Y-RPLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 134 NPVTLKPANTTPTVAALL-QTLIPKYFAPEAVTVVTGGREEIS-ALLELP-FDFIFFTGSAAVGKVVMRAAA------EH 204
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKLvEILEEAGLPPGVVNFLPGPGEEVGdYLVEHPdVRFIAFTGSREVGLRIYERAAkvqpgqKW 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 205 LTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIADDFIARIK---RSLTAMYGEDPSrsp 281
Cdd:cd07124 275 LKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVertKALKVGDPEDPE--- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 282 dfARM---ISAHDAQRVANYI----QPEKVVHGGRFDIP---GRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDE 351
Cdd:cd07124 352 --VYMgpvIDKGARDRIRRYIeigkSEGRLLLGGEVLELaaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502316442 352 VIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDSLPFGGVGLSGMGkyyGQAG 419
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTG---SKAG 494
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
11-427 |
3.17e-62 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 208.15 E-value: 3.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 11 QREFFLTDATKSAAWrldqLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIdyyrRHLVDLMAPQQVEIPP 90
Cdd:cd07104 13 QKAWAATPPQERAAI----LRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAIL----REAAGLPRRPEGEILP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 91 GlEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLqtlIPKYFA----PEAV-T 165
Cdd:cd07104 85 S-DVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLL---IAEIFEeaglPKGVlN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTGGREEI-SALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG---Hnai 240
Cdd:cd07104 161 VVPGGGSEIgDALVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGaflH--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 241 SGQWCIAPGYVYVHHSIADDFIARIK---RSLTamYGeDPsRSPD--FARMISAHDAQRVANYIQPE-----KVVHGGRF 310
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVakaKALP--VG-DP-RDPDtvIGPLINERQVDRVHAIVEDAvaagaRLLTGGTY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 311 DipGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAidrflgsVSFG---- 385
Cdd:cd07104 314 E--GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlERA-------MAFAerle 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 502316442 386 -GGC-VNQTNLHcwiDS--LPFGGVGLSGMGKYYGQAGFDALSNTK 427
Cdd:cd07104 385 tGMVhINDQTVN---DEphVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
96-431 |
8.92e-62 |
|
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: 207.42 E-value: 8.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 96 GYRGMIYKEPYGPTLVIGPFNAPvLLLLDPAIA-ALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTG-GRE 172
Cdd:cd07093 108 GALNYVLRQPVGVAGLITPWNLP-LMLLTWKIApALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVvNVVHGfGPE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 173 EISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYV 251
Cdd:cd07093 187 AGAALVAHPdVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 252 YVHHSIADDFIARIKRSLTAMYGEDPsRSPD--FARMISAHDAQRVANYIQPEK-----VVHGGRFDIP-----GRYVEP 319
Cdd:cd07093 267 LVQRSIYDEFLERFVERAKALKVGDP-LDPDteVGPLISKEHLEKVLGYVELARaegatILTGGGRPELpdlegGYFVEP 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 320 TVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNqtnlhCWI- 398
Cdd:cd07093 346 TVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVN-----CWLv 420
|
330 340 350
....*....|....*....|....*....|....*
gi 502316442 399 -D-SLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07093 421 rDlRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
7-431 |
1.02e-61 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 207.29 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 7 LLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVI----DYYRRHlvdlma 82
Cdd:cd07094 26 ALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLrlaaEEAERI------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 83 pQQVEIPPGLEA--EGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVA-ALLQTLIPKYF 159
Cdd:cd07094 100 -RGEEIPLDATQgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSAlELAKILVEAGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 160 APEAVTVVTGGREEISALLEL--PFDFIFFTGSAAVGKVVMRAAAehLTPVILELGGQNPTVVDATANLDIAIDRIAWGH 237
Cdd:cd07094 179 PEGVLQVVTGEREVLGDAFAAdeRVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLDAAIEALAKGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 238 NAISGQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRS-PDFARMISAHDAQRVANYIQpEKVVHGGRFdIPGRY 316
Cdd:cd07094 257 FYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEdTDVGPLISEEAAERVERWVE-EAVEAGARL-LCGGE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDPAM-----QQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQ 391
Cdd:cd07094 335 RDGALFKPTVLEDVPRdtklsTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVND 414
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 502316442 392 TNlHCWIDSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07094 415 SS-AFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
88-431 |
1.17e-61 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 207.28 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 88 IPPglEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTP-TVAALLQTLIPKYFAPEAVTV 166
Cdd:cd07103 102 IPS--PAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPlSALALAELAEEAGLPAGVLNV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 167 VTGGREEIS-ALLElpfDF----IFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAIS 241
Cdd:cd07103 180 VTGSPAEIGeALCA---SPrvrkISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 242 GQWCIAPGYVYVHHSIADDFIARIK---RSLTAMYGEDPsrSPDFARMISAHDAQRVANYIQPE-----KVVHGG-RFDI 312
Cdd:cd07103 257 GQTCVCANRIYVHESIYDEFVEKLVervKKLKVGNGLDE--GTDMGPLINERAVEKVEALVEDAvakgaKVLTGGkRLGL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 313 PGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFG--GgcVN 390
Cdd:cd07103 335 GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGmvG--IN 412
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 502316442 391 QTNLHCwiDSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07103 413 TGLISD--AEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
81-431 |
5.05e-61 |
|
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: 205.12 E-value: 5.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 81 MAPQQVE--IPPglEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALL-QTLIPK 157
Cdd:cd07105 74 LITQIIGgsIPS--DKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIgRVFHEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 158 YFAPEAVTVVTGGREE----ISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDR 232
Cdd:cd07105 152 GLPKGVLNVVTHSPEDapevVEALIAHPaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 233 IAWGHNAISGQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSPdfarMISAHDAQRVANYI-----QPEKVVHG 307
Cdd:cd07105 232 ALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLGS----LVSAAAADRVKELVddalsKGAKLVVG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 308 G--RFDIPGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRaidRFL---GSV 382
Cdd:cd07105 308 GlaDESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLA---RALavaKRI 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502316442 383 SFGGGCVNQTNLHcwiD--SLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07105 385 ESGAVHINGMTVH---DepTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
94-431 |
6.52e-61 |
|
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: 205.25 E-value: 6.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 94 AEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVTVVTGGREE 173
Cdd:cd07092 107 LPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGAS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 174 ISALL---ELPfDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGY 250
Cdd:cd07092 187 AGDALvahPRV-RMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 251 VYVHHSIADDFIARIKRSLTAM-YGEDPSRSPDFARMISAHDAQRVANYI----QPEKVVHGG-RFDIPGRYVEPTVLYP 324
Cdd:cd07092 266 VYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGrRAEGPGYFYEPTVVAG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 325 SSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFggGCVnqtnlhcWIDS---- 400
Cdd:cd07092 346 VAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDF--GTV-------WVNThipl 416
|
330 340 350
....*....|....*....|....*....|....
gi 502316442 401 ---LPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07092 417 aaeMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
12-429 |
1.52e-60 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 204.40 E-value: 1.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPF-EQLFEITVPLGVIDYYRRHLvdLMAPQQVEIP- 89
Cdd:cd07089 30 RAFDTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQVDGPIGHLRYFADLA--DSFPWEFDLPv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 90 PGLEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVT 168
Cdd:cd07089 108 PALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVvNVVT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 169 GGREEISALLEL-P-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIA--WGHNaiSGQW 244
Cdd:cd07089 188 GSDNAVGEALTTdPrVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVgvCMHN--AGQG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 245 CIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPsRSPD--FARMISAHDAQRVANYI-----QPEKVVHGG----RFDiP 313
Cdd:cd07089 266 CALTTRLLVPRSRYDEVVEALAAAFEALPVGDP-ADPGtvMGPLISAAQRDRVEGYIargrdEGARLVTGGgrpaGLD-K 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 314 GRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQ---RAIDRFL--GSVSFGGGC 388
Cdd:cd07089 344 GFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVdraYRVARRIrtGSVGINGGG 423
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 502316442 389 VNQTNlhcwidsLPFGGVGLSGMGKYYGQAGFDALSNTKSL 429
Cdd:cd07089 424 GYGPD-------APFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
103-431 |
2.39e-60 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 203.75 E-value: 2.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 103 KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTP----TVAALLQTLIPkyfaPEAVTVVTG-GREEISAL 177
Cdd:cd07108 115 REPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPlavlLLAEILAQVLP----AGVLNVITGyGEECGAAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 178 LELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHN-AISGQWCIAPGYVYVHH 255
Cdd:cd07108 191 VDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMRfTRQGQSCTAGSRLFVHE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYI------QPEKVVHGGR-----FDIPGRYVEPTVLY 323
Cdd:cd07108 271 DIYDAFLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKVCGYIdlglstSGATVLRGGPlpgegPLADGFFVQPTIFS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 324 PSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTnlHCWIDSLPF 403
Cdd:cd07108 351 GVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSY 428
|
330 340
....*....|....*....|....*....
gi 502316442 404 GGVGLSGMGKYYGQAG-FDALSNTKSLLI 431
Cdd:cd07108 429 GGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
99-431 |
2.62e-60 |
|
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: 203.72 E-value: 2.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 99 GMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPE-AVTVVTGGREEI-SA 176
Cdd:cd07118 113 GLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAgVVNIVTGYGATVgQA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 177 LLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHH 255
Cdd:cd07118 193 MTEHPdVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYIQPEK-----VVHGG-RFDI-PGRYVEPTVLYPSSW 327
Cdd:cd07118 273 SIADAFVAAVVARSRKVRVGDPlDPETKVGAIINEAQLAKITDYVDAGRaegatLLLGGeRLASaAGLFYQPTIFTDVTP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 328 DDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDqraIDRFLGS---VSFGGGCVNqtnlhCWIDS---L 401
Cdd:cd07118 353 DMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD---IDTALTVarrIRAGTVWVN-----TFLDGspeL 424
|
330 340 350
....*....|....*....|....*....|
gi 502316442 402 PFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07118 425 PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
97-431 |
2.16e-59 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 201.24 E-value: 2.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 97 YRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTGGREEIS 175
Cdd:cd07114 111 YLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAgFPPGVVNVVTGFGPETG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 176 -ALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYV 253
Cdd:cd07114 191 eALVEHPlVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 254 HHSIADDFIARI-KRSLTAMYGeDPSR-SPDFARMISAHDAQRVANYI-----QPEKVVHGG-RFDIP----GRYVEPTV 321
Cdd:cd07114 271 QRSIYDEFVERLvARARAIRVG-DPLDpETQMGPLATERQLEKVERYVarareEGARVLTGGeRPSGAdlgaGYFFEPTI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 322 LYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGggcvnqtnlHCWID-- 399
Cdd:cd07114 350 LADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAG---------TVWVNty 420
|
330 340 350
....*....|....*....|....*....|....*..
gi 502316442 400 -----SLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07114 421 ralspSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
22-413 |
1.06e-58 |
|
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: 199.39 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 22 SAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQ-VEIPPGleAEGYRGM 100
Cdd:cd07147 41 PAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIYGEVLpLDISAR--GEGRQGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 101 IYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALL-QTLIPKYFAPEAVTVVTGGREEISALLE 179
Cdd:cd07147 119 VRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILgEVLAETGLPKGAFSVLPCSRDDADLLVT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 180 LP-FDFIFFTGSAAVG-KVVMRAAAEHltpVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSI 257
Cdd:cd07147 199 DErIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 258 ADDFIARIKRSLTAMYGEDPS-RSPDFARMISAHDAQRVANYIQpEKVVHGGRFDIPGR----YVEPTVLYPSSWDDPAM 332
Cdd:cd07147 276 YDEFKSRLVARVKALKTGDPKdDATDVGPMISESEAERVEGWVN-EAVDAGAKLLTGGKrdgaLLEPTILEDVPPDMEVN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 333 QQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQtnLHCW-IDSLPFGGVGLSGM 411
Cdd:cd07147 355 CEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND--VPTFrVDHMPYGGVKDSGI 432
|
..
gi 502316442 412 GK 413
Cdd:cd07147 433 GR 434
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
22-413 |
1.09e-57 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 196.80 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 22 SAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVI----DYYRRHlvdlmapqQVEIPPgLEAEGY 97
Cdd:cd07145 41 PAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFklaaEEAKVL--------RGETIP-VDAYEY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 98 --RGMIY--KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTGGRE 172
Cdd:cd07145 112 neRRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 173 EI-SALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGY 250
Cdd:cd07145 192 EVgDEIVTNPkVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 251 VYVHHSIADDFIARIKRSLTAMYGEDPSR-SPDFARMISAHDAQRVANYI-----QPEKVVHGGRFDiPGRYVEPTVLYP 324
Cdd:cd07145 272 ILVEEEVYDKFLKLLVEKVKKLKVGDPLDeSTDLGPLISPEAVERMENLVndaveKGGKILYGGKRD-EGSFFPPTVLEN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 325 SSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWiDSLPFG 404
Cdd:cd07145 351 DTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRFRW-DNLPFG 429
|
....*....
gi 502316442 405 GVGLSGMGK 413
Cdd:cd07145 430 GFKKSGIGR 438
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
18-428 |
1.75e-57 |
|
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: 196.37 E-value: 1.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 18 DATKSA--AWRLDQLDRMERLLR-------ENQEAFCNALYQDFRKPPFEQLF-EITVPLGVIDYYRRHLVDLMAPQQVe 87
Cdd:cd07098 25 AAARAAqrEWAKTSFAERRKVLRsllkyilENQEEICRVACRDTGKTMVDASLgEILVTCEKIRWTLKHGEKALRPESR- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 88 ipPGLEAEGYRG-MIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFA-----P 161
Cdd:cd07098 104 --PGGLLMFYKRaRVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAacghdP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 162 EAVTVVTGGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAI 240
Cdd:cd07098 182 DLVQLVTCLPETAEALTSHPvIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 241 SGQWCIAPGYVYVHHSIADDFIARIK---RSLTAMYGEDpsRSPDFARMISAHDAQRVANYI-----QPEKVVHGG-RFD 311
Cdd:cd07098 262 SGQNCIGIERVIVHEKIYDKLLEILTdrvQALRQGPPLD--GDVDVGAMISPARFDRLEELVadaveKGARLLAGGkRYP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 312 IP----GRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGG 387
Cdd:cd07098 340 HPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMV 419
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 502316442 388 CVNQTNLHCWIDSLPFGGVGLSGMGKYYGQAGFDALSNTKS 428
Cdd:cd07098 420 AINDFGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKS 460
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
18-393 |
4.48e-57 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 195.56 E-value: 4.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 18 DATKSA--AW-------RLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYY----RRHlvdlmapq 84
Cdd:cd07088 42 DAAEAAqkAWerlpaieRAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMaewaRRI-------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 85 QVEIPPGlEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV 164
Cdd:cd07088 114 EGEIIPS-DRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 165 -TVVTG-GREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAIS 241
Cdd:cd07088 193 lNIVTGrGSVVGDALVAHPkVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINC 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 242 GQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYI-----QPEKVVHGG-RFDI-P 313
Cdd:cd07088 273 GQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPfDAATDMGPLVNEAALDKVEEMVeraveAGATLLTGGkRPEGeK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 314 GRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTN 393
Cdd:cd07088 353 GYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINREN 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-423 |
5.56e-57 |
|
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: 195.47 E-value: 5.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 3 QYQTLLDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYY---RRHLVD 79
Cdd:cd07086 36 DVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYAvglSRMLYG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 80 LMAPQqvEIPpgleaeGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLI---- 155
Cdd:cd07086 116 LTIPS--ERP------GHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILaevl 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 156 PKYFAPEAV-TVVTGGREeISALLELP--FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDR 232
Cdd:cd07086 188 EKNGLPPGVvNLVTGGGD-GGELLVHDprVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 233 IAWGHNAISGQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSR-SPDFARMISAHDAQRVANYI-----QPEKVVH 306
Cdd:cd07086 267 VLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDeGTLVGPLINQAAVEKYLNAIeiaksQGGTVLT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 307 GGRF---DIPGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVS 383
Cdd:cd07086 347 GGKRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKG 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 502316442 384 FGGGCVNqTNLHCwidS-----LPFGGVGLSGMGKyygQAGFDAL 423
Cdd:cd07086 427 SDCGIVN-VNIPT---SgaeigGAFGGEKETGGGR---ESGSDAW 464
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
11-427 |
7.25e-57 |
|
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: 194.48 E-value: 7.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 11 QREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYR---RHlvdlMAPQQVE 87
Cdd:cd07120 29 RRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAglaRT----EAGRMIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 88 IPPGLeaegyRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTV-AALLQTL--IPkYFAPEAV 164
Cdd:cd07120 105 PEPGS-----FSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQInAAIIRILaeIP-SLPAGVV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 165 TVVTGGREEISALL-ELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISG 242
Cdd:cd07120 179 NLFTESGSEGAAHLvASPdVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 243 QWCIAPGYVYVHHSIADDFIARIKRSLTAMY---GEDPSRspDFARMISAHDAQRVANYIQ------PEKVVHGGRFD-- 311
Cdd:cd07120 259 QFCMAGSRVLVQRSIADEVRDRLAARLAAVKvgpGLDPAS--DMGPLIDRANVDRVDRMVEraiaagAEVVLRGGPVTeg 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 312 -IPGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRA--IDRFL--GSVsfg 385
Cdd:cd07120 337 lAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDlARAmrVARAIraGTV--- 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 502316442 386 ggcvnqtnlhcWI-------DSLPFGGVGLSGMGKYYGQAGFDALSNTK 427
Cdd:cd07120 414 -----------WIndwnklfAEAEEGGYRQSGLGRLHGVAALEDFIEYK 451
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
18-431 |
1.17e-56 |
|
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: 193.90 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 18 DATKSA--AW-------RLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIdyyrRHLVDLMAPQQVEI 88
Cdd:cd07106 26 AAAKAAfpGWsatpleeRRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWL----RYTASLDLPDEVIE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 89 ppglEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVTVVT 168
Cdd:cd07106 102 ----DDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 169 GGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG--HNaiSGQWC 245
Cdd:cd07106 178 GGDELGPALTSHPdIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGafIN--SGQVC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 246 IAPGYVYVHHSIADDFIARIKRSLTAMY---GEDPsrSPDFARMISAHDAQRVANYI-----QPEKVVHGGRF-DIPGRY 316
Cdd:cd07106 256 AAIKRLYVHESIYDEFCEALVALAKAAVvgdGLDP--GTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPlDGPGYF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQ---RAIDRFL--GSVsfgggcvnq 391
Cdd:cd07106 334 IPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLeraEAVARRLeaGTV--------- 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 502316442 392 tnlhcWIDS-------LPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07106 405 -----WINThgaldpdAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
103-431 |
1.52e-56 |
|
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: 194.55 E-value: 1.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 103 KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTG-GREEISALLEL 180
Cdd:cd07144 142 HEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGyGAVAGSALAEH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 181 P-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDriaWGHNAI---SGQWCIAPGYVYVHHS 256
Cdd:cd07144 222 PdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVK---WAAAGImynSGQNCTATSRIYVQES 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 257 IADDFIARIKR------SLTAMYGEDPSRSPdfarMISAHDAQRVANYIQP-----EKVVHGGRFDIP----GRYVEPTV 321
Cdd:cd07144 299 IYDKFVEKFVEhvkqnyKVGSPFDDDTVVGP----QVSKTQYDRVLSYIEKgkkegAKLVYGGEKAPEglgkGYFIPPTI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 322 LYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWidSL 401
Cdd:cd07144 375 FTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GV 452
|
330 340 350
....*....|....*....|....*....|
gi 502316442 402 PFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07144 453 PFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
22-423 |
2.00e-56 |
|
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: 194.10 E-value: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 22 SAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYR---RHLVDLMAPQqvEIPPGLeaegyr 98
Cdd:cd07131 57 PAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAgegRRLFGETVPS--ELPNKD------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 99 GMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVA-ALLQTLIPKYFAPEAVTVVTGGREEI-SA 176
Cdd:cd07131 129 AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACAlKLVELFAEAGLPPGVVNVVHGRGEEVgEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 177 LLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHH 255
Cdd:cd07131 209 LVEHPdVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIARIKRSLTAMYGEDPSRSP-DFARMISAHDAQRVANYI---QPE--KVVHGG-RFD----IPGRYVEPTVLYP 324
Cdd:cd07131 289 SVYDEFLKRFVERAKRLRVGDGLDEEtDMGPLINEAQLEKVLNYNeigKEEgaTLLLGGeRLTgggyEKGYFVEPTVFTD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 325 SSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIdSLPFG 404
Cdd:cd07131 369 VTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFG 447
|
410
....*....|....*....
gi 502316442 405 GVGLSGMGkyYGQAGFDAL 423
Cdd:cd07131 448 GVKKSGNG--HREAGTTAL 464
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
17-413 |
3.37e-56 |
|
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: 192.98 E-value: 3.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 17 TDATKSA--AWRL-------DQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRrHLVDLMAPQQve 87
Cdd:cd07107 25 VAAARAAfpEWRAttpleraRMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFA-GLVTELKGET-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 88 IPPGLEAEGYRgmiYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVTVV 167
Cdd:cd07107 102 IPVGGRNLHYT---LREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 168 TGGREEI-SALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHN-AISGQW 244
Cdd:cd07107 179 PGDGATAgAALVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGMNfTWCGQS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 245 CIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSrSPD--FARMISAHDAQRVANYIQPEK-----VVHGGRfdIP---- 313
Cdd:cd07107 259 CGSTSRLFVHESIYDEVLARVVERVAAIKVGDPT-DPAttMGPLVSRQQYDRVMHYIDSAKregarLVTGGG--RPegpa 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 314 ---GRYVEPTVLypsswDDPAM-----QQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFG 385
Cdd:cd07107 336 legGFYVEPTVF-----ADVTPgmriaREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAG 410
|
410 420
....*....|....*....|....*...
gi 502316442 386 GGCVNQTNLHCWidSLPFGGVGLSGMGK 413
Cdd:cd07107 411 YVWINGSSRHFL--GAPFGGVKNSGIGR 436
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
8-428 |
2.29e-55 |
|
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: 189.98 E-value: 2.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 8 LDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVE 87
Cdd:cd07100 5 LDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADEPIE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 88 IPPGleaegyRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPE-AVTV 166
Cdd:cd07100 85 TDAG------KAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEgVFQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 167 VTGGREEISALLELPF-DFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG--HNAisGQ 243
Cdd:cd07100 159 LLIDSDQVEAIIADPRvRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGrlQNA--GQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 244 WCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPS-RSPDFARMISAHDAQRVANYIQPE-----KVVHGG-RFDIPGRY 316
Cdd:cd07100 237 SCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMdEDTDLGPLARKDLRDELHEQVEEAvaagaTLLLGGkRPDGPGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQtnlHC 396
Cdd:cd07100 317 YPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING---MV 393
|
410 420 430
....*....|....*....|....*....|...
gi 502316442 397 WID-SLPFGGVGLSGMGKYYGQAGFDALSNTKS 428
Cdd:cd07100 394 KSDpRLPFGGVKRSGYGRELGRFGIREFVNIKT 426
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
103-428 |
4.25e-55 |
|
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: 190.50 E-value: 4.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 103 KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTG-GREEISALLEL 180
Cdd:cd07091 139 REPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGfGPTAGAAISSH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 181 P-FDFIFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVVDATANLDIAIDriaWGHNAI---SGQWCIAPGYVYVHH 255
Cdd:cd07091 219 MdVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVE---WAAFGIffnQGQCCCAGSRIFVQE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIARIKRSLTAMYGEDPSRSPDF-ARMISAHDAQRVANYIQPEK-----VVHGG-RFDIPGRYVEPTVLYPSSWD 328
Cdd:cd07091 296 SIYDEFVEKFKARAEKRVVGDPFDPDTFqGPQVSKAQFDKILSYIESGKkegatLLTGGeRHGSKGYFIQPTVFTDVKDD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 329 DPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCwiDSLPFGGVGL 408
Cdd:cd07091 376 MKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFD--AAVPFGGFKQ 453
|
330 340
....*....|....*....|
gi 502316442 409 SGMGKYYGQAGFDALSNTKS 428
Cdd:cd07091 454 SGFGRELGEEGLEEYTQVKA 473
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-431 |
1.30e-54 |
|
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: 188.94 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 22 SAAWRLDQLDRMERLLRENQEAFCNALYQDFRKP-PFEQLFEITVPLGVIDYYRRhLVDLMAPQQVEIPPGleaeGYRGM 100
Cdd:cd07139 58 SPAERAAVLRRLADALEARADELARLWTAENGMPiSWSRRAQGPGPAALLRYYAA-LARDFPFEERRPGSG----GGHVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 101 IYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALLE 179
Cdd:cd07139 133 VRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVvNVVPADREVGEYLVR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 180 LP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIA 258
Cdd:cd07139 213 HPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 259 DDFIARIKRSLTAMYGEDPS-RSPDFARMISAHDAQRVANYIQPEK------VVHGGRFDIPGR--YVEPTVLYPSSWDD 329
Cdd:cd07139 293 DEVVEALAAAVAALKVGDPLdPATQIGPLASARQRERVEGYIAKGRaegarlVTGGGRPAGLDRgwFVEPTLFADVDNDM 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 330 PAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAID--RFLGSVSFGggcVNQTnlhcWID-SLPFGG 405
Cdd:cd07139 373 RIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADvERGLAvaRRIRTGTVG---VNGF----RLDfGAPFGG 445
|
410 420
....*....|....*....|....*.
gi 502316442 406 VGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07139 446 FKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
12-430 |
1.35e-54 |
|
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: 188.71 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVEIPpg 91
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQLDAKAERAVP-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 92 LEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTP-TVAALLQTLIPKYFAPEAVTVVTGG 170
Cdd:cd07110 107 LPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSlTELELAEIAAEAGLPPGVLNVVTGT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 171 REEISA-LLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAP 248
Cdd:cd07110 187 GDEAGApLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 249 GYVYVHHSIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYIQPEK-----VVHGGR---FDIPGRYVEP 319
Cdd:cd07110 267 SRLLVHESIADAFLERLATAAEAIRVGDPlEEGVRLGPLVSQAQYEKVLSFIARGKeegarLLCGGRrpaHLEKGYFIAP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 320 TVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGggcvnqtnlHCWID 399
Cdd:cd07110 347 TVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAG---------IVWIN 417
|
410 420 430
....*....|....*....|....*....|....*...
gi 502316442 400 S-------LPFGGVGLSGMGKYYGQAGFDALSNTKSLL 430
Cdd:cd07110 418 CsqpcfpqAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
26-412 |
2.21e-54 |
|
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: 188.55 E-value: 2.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 26 RLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITvplGVIDYYRRHLVDL--MAPQQVEIPPGLEAEGYRGMIYK 103
Cdd:cd07082 63 RIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVD---RTIDYIRDTIEELkrLDGDSLPGDWFPGTKGKIAQVRR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 104 EPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAA-LLQTLIPKYFAPEAVTVVTG-GREEISALLELP 181
Cdd:cd07082 140 EPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIpLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 182 -FDFIFFTGSAAVGKVVMRAAaeHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIADD 260
Cdd:cd07082 220 rIDVISFTGSTEVGNRLKKQH--PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 261 FIARIKRSLTAMYGEDP-SRSPDFARMISahdaQRVANYIQP---------EKVVHGGRFDIpGRYVEPTVLYPsswDDP 330
Cdd:cd07082 298 LVELLKEEVAKLKVGMPwDNGVDITPLID----PKSADFVEGliddavakgATVLNGGGREG-GNLIYPTLLDP---VTP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 331 AMQ---QEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAID---RFL--GSVSFGGGCVNQtnlhcwIDSLP 402
Cdd:cd07082 370 DMRlawEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARklaDALevGTVNINSKCQRG------PDHFP 443
|
410
....*....|
gi 502316442 403 FGGVGLSGMG 412
Cdd:cd07082 444 FLGRKDSGIG 453
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
90-431 |
4.82e-54 |
|
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: 187.65 E-value: 4.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 90 PGLEAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTP-TVAALLQTLIPKYFAPEAVTVVT 168
Cdd:cd07113 127 PSMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPlTLLRVAELAKEAGIPDGVLNVVN 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 169 GGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIA 247
Cdd:cd07113 207 GKGAVGAQLISHPdVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 248 PGYVYVHHSIADDFIARIKRSLTAMYGEDP----------SRSPDFARMISAHDAQRVANyiqpEKVVHGGR-FDIPGRY 316
Cdd:cd07113 287 PERFYVHRSKFDELVTKLKQALSSFQVGSPmdesvmfgplANQPHFDKVCSYLDDARAEG----DEIVRGGEaLAGEGYF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVnqtNLHC 396
Cdd:cd07113 363 VQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWV---NMHT 439
|
330 340 350
....*....|....*....|....*....|....*.
gi 502316442 397 WID-SLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07113 440 FLDpAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
93-427 |
1.63e-53 |
|
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: 185.61 E-value: 1.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 93 EAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGR 171
Cdd:cd07150 107 DSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVfNVVTGGG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 172 EEISALL--ELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPG 249
Cdd:cd07150 187 AEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSAS 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 250 YVYVHHSIADDFIARIKRSLTAMYGEDPsRSPD--FARMISAHDAQRVANYIQPE-----KVVHGGRFDipGRYVEPTVL 322
Cdd:cd07150 267 RIIVEEPVYDEFVKKFVARASKLKVGDP-RDPDtvIGPLISPRQVERIKRQVEDAvakgaKLLTGGKYD--GNFYQPTVL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 323 YPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAIdrFLGSVSFGGGC-VNQTNLHCWIdS 400
Cdd:cd07150 344 TDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDlQRAF--KLAERLESGMVhINDPTILDEA-H 420
|
330 340
....*....|....*....|....*..
gi 502316442 401 LPFGGVGLSGMGKYYGQAGFDALSNTK 427
Cdd:cd07150 421 VPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
26-428 |
5.28e-53 |
|
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: 184.37 E-value: 5.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 26 RLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVEippglEAEGYRGMIYKEP 105
Cdd:cd07102 42 RKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVP-----EKDGFERYIRREP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 106 YGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALLELP-FD 183
Cdd:cd07102 117 LGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVfQVLHLSHETSAALIADPrID 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 184 FIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIADDFIA 263
Cdd:cd07102 197 HVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 264 RIKrSLTAMY--GEDPSRSPDFARMISAHDAQRVANYIQPE------KVVHGGRFDIP---GRYVEPTVLYPSSWDDPAM 332
Cdd:cd07102 277 AFV-AVVKGYklGDPLDPSTTLGPVVSARAADFVRAQIADAiakgarALIDGALFPEDkagGAYLAPTVLTNVDHSMRVM 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 333 QQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNlhcWID-SLPFGGVGLSGM 411
Cdd:cd07102 356 REETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCD---YLDpALAWTGVKDSGR 432
|
410
....*....|....*..
gi 502316442 412 GKYYGQAGFDALSNTKS 428
Cdd:cd07102 433 GVTLSRLGYDQLTRPKS 449
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
21-431 |
7.76e-53 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 184.44 E-value: 7.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 21 KSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRhLVDLMAPQQVEIPPGLEAegyrgM 100
Cdd:cd07119 56 LPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAG-LATKETGEVYDVPPHVIS-----R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 101 IYKEPYGPTLVIGPFNAPvLLLLDPAIA-ALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEI-SAL 177
Cdd:cd07119 130 TVREPVGVCGLITPWNYP-LLQAAWKLApALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVvNLVTGSGATVgAEL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 178 LELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDriaWGHNAI---SGQWCIAPGYVYV 253
Cdd:cd07119 209 AESPdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVD---QALNGVffnAGQVCSAGSRLLV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 254 HHSIADDFIARIKRSLTAM---YGEDPsrSPDFARMISAHDAQRVANYIQ-----PEKVVHGG-RFDIP----GRYVEPT 320
Cdd:cd07119 286 EESIHDKFVAALAERAKKIklgNGLDA--DTEMGPLVSAEHREKVLSYIQlgkeeGARLVCGGkRPTGDelakGYFVEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 321 VLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNqtNLHCWIDS 400
Cdd:cd07119 364 IFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN--DYHPYFAE 441
|
410 420 430
....*....|....*....|....*....|.
gi 502316442 401 LPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07119 442 APWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
103-431 |
5.60e-52 |
|
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: 181.48 E-value: 5.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 103 KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVA-ALLQTLIPKYFAPEAVTVVTG-GREEISALLEL 180
Cdd:cd07115 115 REPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAlRIAELMAEAGFPAGVLNVVTGfGEVAGAALVEH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 181 P-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG--HNAisGQWCIAPGYVYVHHSI 257
Cdd:cd07115 195 PdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGifYNQ--GQMCTAGSRLLVHESI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 258 ADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYI-----QPEKVVHGG-RFDIPGRYVEPTVLYPSSWDDP 330
Cdd:cd07115 273 YDEFLERFTSLARSLRPGDPlDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGkRPGARGFFVEPTIFAAVPPEMR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 331 AMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGggcvnqtnlHCWIDS-------LPF 403
Cdd:cd07115 353 IAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAG---------TVWINTynrfdpgSPF 423
|
330 340
....*....|....*....|....*...
gi 502316442 404 GGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07115 424 GGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
11-416 |
8.15e-52 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 180.95 E-value: 8.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 11 QREFFLTDATKSAAwrldQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVplgVIDYYRRHLVDLMAPQQVEIPP 90
Cdd:cd07152 26 QRAWAATPPRERAA----VLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGA---AIGELHEAAGLPTQPQGEILPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 91 gleAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLqtlIPKYFA----PEAV-T 165
Cdd:cd07152 99 ---APGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV---IARLFEeaglPAGVlH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTGGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQW 244
Cdd:cd07152 173 VLPGGADAGEALVEDPnVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 245 CIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSRSP-DFARMISAHDAQRVANYIQPE-----KVVHGGRFDipGRYVE 318
Cdd:cd07152 253 CMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIVDDSvaagaRLEAGGTYD--GLFYR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 319 PTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAIDrfLG-SVSFGGGCVN-QTNLH 395
Cdd:cd07152 331 PTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDvGRAMA--LAdRLRTGMLHINdQTVND 408
|
410 420
....*....|....*....|.
gi 502316442 396 CWIDslPFGGVGLSGMGKYYG 416
Cdd:cd07152 409 EPHN--PFGGMGASGNGSRFG 427
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
103-431 |
4.71e-50 |
|
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: 177.15 E-value: 4.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 103 KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTG-GREEISALLEL 180
Cdd:cd07141 143 HEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGyGPTAGAAISSH 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 181 P-FDFIFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVVDATANLDIAIDriaWGHNAI---SGQWCIAPGYVYVHH 255
Cdd:cd07141 223 PdIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVE---QAHEALffnMGQCCCAGSRTFVQE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIAR-IKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQPEK------VVHGGRFDIPGRYVEPTVLYPSSWD 328
Cdd:cd07141 300 SIYDEFVKRsVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKkegaklECGGKRHGDKGYFIQPTVFSDVTDD 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 329 DPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDqraIDR---FLGSVSFGGGCVNQTNlhCWIDSLPFGG 405
Cdd:cd07141 380 MRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKaitFSNALRAGTVWVNCYN--VVSPQAPFGG 454
|
330 340
....*....|....*....|....*.
gi 502316442 406 VGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07141 455 YKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
95-413 |
5.19e-50 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 176.64 E-value: 5.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 95 EGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVTVVTG-GREE 173
Cdd:PRK13473 128 EGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGrGATV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 174 ISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG--HNAisGQWCIAPGY 250
Cdd:PRK13473 208 GDALVGHPkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFgyYNA--GQDCTAACR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 251 VYVHHSIADDFIARIK---RSLTAMYGEDPSRspDFARMISAHDAQRVANYI-----QPE-KVVHGGR-FDIPGRYVEPT 320
Cdd:PRK13473 286 IYAQRGIYDDLVAKLAaavATLKVGDPDDEDT--ELGPLISAAHRDRVAGFVerakaLGHiRVVTGGEaPDGKGYYYEPT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 321 VLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAIdRFLGSVSFggGCVnqtnlhcWID 399
Cdd:PRK13473 364 LLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDvGRAH-RVSARLQY--GCT-------WVN 433
|
330 340
....*....|....*....|.
gi 502316442 400 S-------LPFGGVGLSGMGK 413
Cdd:PRK13473 434 ThfmlvseMPHGGQKQSGYGK 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
12-431 |
5.95e-50 |
|
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: 176.34 E-value: 5.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLmAPQQVEIPPG 91
Cdd:cd07090 29 KAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTL-SGEHVPLPGG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 92 LEAEGYRgmiykEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGG 170
Cdd:cd07090 108 SFAYTRR-----EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVfNVVQGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 171 REEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIdRIAWGHNAIS-GQWCIAP 248
Cdd:cd07090 183 GETGQLLCEHPdVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAV-NGAMMANFLSqGQVCSNG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 249 GYVYVHHSIADDFIARIKRSLTAMYGEDPSRS-PDFARMISAHDAQRVANYI-----QPEKVVHGGRFDIP------GRY 316
Cdd:cd07090 262 TRVFVQRSIKDEFTERLVERTKKIRIGDPLDEdTQMGALISEEHLEKVLGYIesakqEGAKVLCGGERVVPedglenGFY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAiDRFLGSVSFGggcvnqtnlH 395
Cdd:cd07090 342 VSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDlQRA-HRVIAQLQAG---------T 411
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 502316442 396 CWIDS-------LPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07090 412 CWINTynispveVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
4-427 |
7.52e-50 |
|
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: 176.34 E-value: 7.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 4 YQTLLDRQREFfltdATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIdyyrRHLVDLMAP 83
Cdd:cd07151 38 YRAAAAAQKEW----AATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAIT----REAATFPLR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 84 QQVEIPPGLeAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLqtlIPKYFA--- 160
Cdd:cd07151 110 MEGRILPSD-VPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLL---LAKIFEeag 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 161 -PEAV-TVVTGGREEI-SALLELPF-DFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG 236
Cdd:cd07151 186 lPKGVlNVVVGAGSEIgDAFVEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 237 HNAISGQWCIAPGYVYVHHSIADDFIARIKRSLTAM-YGeDPSrSPD--FARMISAHDAQRVANYIQPEK-----VVHGG 308
Cdd:cd07151 266 KFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALpYG-DPS-DPDtvVGPLINESQVDGLLDKIEQAVeegatLLVGG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 309 rfDIPGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAIdRFLGSVSFGGG 387
Cdd:cd07151 344 --EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDlERGV-QFARRIDAGMT 420
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 502316442 388 CVNQTNLHcwiDS--LPFGGVGLSGMGKYYGQAGFDALSNTK 427
Cdd:cd07151 421 HINDQPVN---DEphVPFGGEKNSGLGRFNGEWALEEFTTDK 459
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
8-433 |
2.18e-49 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 175.65 E-value: 2.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 8 LDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYY----RRHLVDLmap 83
Cdd:PLN02278 68 IASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFaeeaKRVYGDI--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 84 qqveIPPGLeAEGyRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTL-----IPky 158
Cdd:PLN02278 145 ----IPSPF-PDR-RLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELalqagIP-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 159 faPEAVTVVTGGREEI-SALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWG 236
Cdd:PLN02278 217 --PGVLNVVMGDAPEIgDALLASPkVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALAS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 237 HNAISGQWCIAPGYVYVHHSIADDFIARIKRSLTAM-----YGEDPSRSPdfarMISAHDAQRVANYIQPE-----KVVH 306
Cdd:PLN02278 295 KFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvvgdgFEEGVTQGP----LINEAAVQKVESHVQDAvskgaKVLL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 307 GG-RFDIPGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFG 385
Cdd:PLN02278 371 GGkRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYG 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 502316442 386 GGCVNQTnlhcWI--DSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLIGN 433
Cdd:PLN02278 451 IVGVNEG----LIstEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLGN 496
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
12-410 |
2.75e-49 |
|
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: 174.00 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVEIPPG 91
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGERATPMAQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 92 leaegyRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALL-QTLIPKYFAPEAVTVVTGG 170
Cdd:cd07095 90 ------RAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMvELWEEAGLPPGVLNLVQGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 171 REEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHlTPVIL--ELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIA 247
Cdd:cd07095 164 RETGEALAAHEgIDGLLFTGSAATGLLLHRQFAGR-PGKILalEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 248 PGYVYVHHS-IADDFIARIKRSLTAMYGEDPSRSPDFarMISAHDAQRVANYI--QPEKVVHGG-------RFDIPGRYV 317
Cdd:cd07095 243 ARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPF--MGPLIIAAAAARYLlaQQDLLALGGepllameRLVAGTAFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 318 EPTVLYPSSWDDPAmQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSfgGGCVN---QTNL 394
Cdd:cd07095 321 SPGIIDVTDAADVP-DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR--AGIVNwnrPTTG 397
|
410
....*....|....*.
gi 502316442 395 HCwiDSLPFGGVGLSG 410
Cdd:cd07095 398 AS--STAPFGGVGLSG 411
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
87-431 |
4.73e-49 |
|
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: 173.94 E-value: 4.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 87 EIPPglEAEGYRGMIYKEPYGptlVIG---PFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEA 163
Cdd:cd07112 108 EVAP--TGPDALALITREPLG---VVGavvPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 164 V-TVVTG-GREEISAL-LELPFDFIFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVV-DATANLDIAIDRIAWG-- 236
Cdd:cd07112 183 VlNVVPGfGHTAGEALgLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVfADAPDLDAAAEAAAAGif 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 237 HNAisGQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYIQPEK-----VVHGG-- 308
Cdd:cd07112 263 WNQ--GEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPlDPATRMGALVSEAHFDKVLGYIESGKaegarLVAGGkr 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 309 -RFDIPGRYVEPTVLypsswDD--PAM---QQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSV 382
Cdd:cd07112 341 vLTETGGFFVEPTVF-----DGvtPDMriaREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRL 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502316442 383 SFGGGCVNqtnlhCWID---SLPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07112 416 RAGTVWVN-----CFDEgdiTTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
26-410 |
6.14e-49 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 174.74 E-value: 6.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 26 RLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVEIPPGLEAEgyrgMIYkEP 105
Cdd:PRK03137 97 RARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNR----YFY-IP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 106 YGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISA-LLELP-F 182
Cdd:PRK03137 172 LGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVvNFVPGSGSEVGDyLVDHPkT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 183 DFIFFTGSAAVGKVVMRAAAE------HLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHS 256
Cdd:PRK03137 252 RFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHED 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 257 IADDFIARIKRSLTAMYGEDPSRSPDFARMISAHDAQRVANYIQPEK-----VVHGGRFDIPGRYVEPTVLYPSSWDDPA 331
Cdd:PRK03137 332 VYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKeegrlVLGGEGDDSKGYFIQPTIFADVDPKARI 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 332 MQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDR-----FLGSVSFGGGCVNQTnlhcwIDSLPFGGV 406
Cdd:PRK03137 412 MQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKarrefHVGNLYFNRGCTGAI-----VGYHPFGGF 486
|
....
gi 502316442 407 GLSG 410
Cdd:PRK03137 487 NMSG 490
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-430 |
1.42e-48 |
|
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: 172.69 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKP-PFEQLFEITVPLGVIDYYRrhlvDLMAPQQVEIPP 90
Cdd:cd07138 46 RRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPiTLARAAQVGLGIGHLRAAA----DALKDFEFEERR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 91 GleaegyRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTG 169
Cdd:cd07138 122 G------NSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVfNLVNG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 170 GREEI-SALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIA 247
Cdd:cd07138 196 DGPVVgEALSAHPdVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 248 PGYVYVHHSIADDFIARIKRSLTAMYGEDPS-RSPDFARMISAHDAQRVANYIQ---PE--KVVHGGrfdiPGR------ 315
Cdd:cd07138 276 PTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRdPATTLGPLASAAQFDRVQGYIQkgiEEgaRLVAGG----PGRpegler 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 316 --YVEPTVLypsSWDDPAM---QQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQ---RAIDRFL--GSVSFG 385
Cdd:cd07138 352 gyFVKPTVF---ADVTPDMtiaREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPeraRAVARRLraGQVHIN 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 502316442 386 GGCVNQtnlhcwidSLPFGGVGLSGMGKYYGQAGFDALSNTKSLL 430
Cdd:cd07138 429 GAAFNP--------GAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
19-423 |
3.05e-48 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 172.05 E-value: 3.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 19 ATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVEIPPGLEAEgyr 98
Cdd:cd07097 54 RRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVE--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 99 gmIYKEPYGPTLVIGPFNAPVLLlldPA--IA-ALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTG-GREE 173
Cdd:cd07097 131 --TTREPLGVVGLITPWNFPIAI---PAwkIApALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVfNLVMGsGSEV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 174 ISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVY 252
Cdd:cd07097 206 GQALVEHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 253 VHHSIADDFIARIKRSLTAM-YGEDPSRSPDFARMISAHDAQRVANYI-----QPEKVVHGGR---FDIPGRYVEPTVLY 323
Cdd:cd07097 286 VTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGErlkRPDEGYYLAPALFA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 324 PSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQ----TNLHcwid 399
Cdd:cd07097 366 GVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptagVDYH---- 441
|
410 420
....*....|....*....|....
gi 502316442 400 sLPFGGVGLSGMGkyYGQAGFDAL 423
Cdd:cd07097 442 -VPFGGRKGSSYG--PREQGEAAL 462
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
19-419 |
1.06e-47 |
|
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: 170.18 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 19 ATKSAAWRLDQLDRMERLLRENQEAFCNaLYQ----DFRKPPFEQLFEITVplgVIDYYRRHLVDLMAPQQVEIP-PGLE 93
Cdd:cd07101 35 AARPFAERAAVFLRFHDLVLERRDELLD-LIQletgKARRHAFEEVLDVAI---VARYYARRAERLLKPRRRRGAiPVLT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 94 aegyRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTP-----TVAALLQTLIPKyfapEAVTVVT 168
Cdd:cd07101 111 ----RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAltalwAVELLIEAGLPR----DLWQVVT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 169 G-GREEISALLElPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIA 247
Cdd:cd07101 183 GpGSEVGGAIVD-NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 248 PGYVYVHHSIADDFIARIKRSLTAM-YGEDPSRSPDFARMISAHDAQRVANYI-----QPEKVVHGG--RFDIPGRYVEP 319
Cdd:cd07101 262 IERIYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVddavaKGATVLAGGraRPDLGPYFYEP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 320 TVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCW-- 397
Cdd:cd07101 342 TVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWas 421
|
410 420
....*....|....*....|..
gi 502316442 398 IDSlPFGGVGLSGMGKYYGQAG 419
Cdd:cd07101 422 IDA-PMGGMKDSGLGRRHGAEG 442
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
19-419 |
3.76e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 170.06 E-value: 3.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 19 ATKSAAWRLDQLDRMERLLRENQEAFCNaLYQ----DFRKPPFEqlfEITVPLGVIDYYRRHLVDLMAPQQVeippglea 94
Cdd:PRK09407 71 AATPVRERAAVLLRFHDLVLENREELLD-LVQletgKARRHAFE---EVLDVALTARYYARRAPKLLAPRRR-------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 95 egyRGMI--------YKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTP-TVAALLQTLIPKYFAPEAVT 165
Cdd:PRK09407 139 ---AGALpvltktteLRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPlTALAAVELLYEAGLPRDLWQ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTG-GREEISALLELPfDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQW 244
Cdd:PRK09407 216 VVTGpGPVVGTALVDNA-DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 245 CIAPGYVYVHHSIADDFIARIKRSLTAM-YGEDPSRSPDFARMISAHDAQRVANYIQP-----EKVVHGG--RFDIPGRY 316
Cdd:PRK09407 295 CISIERIYVHESIYDEFVRAFVAAVRAMrLGAGYDYSADMGSLISEAQLETVSAHVDDavakgATVLAGGkaRPDLGPLF 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHC 396
Cdd:PRK09407 375 YEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAA 454
|
410 420
....*....|....*....|....*
gi 502316442 397 W--IDSlPFGGVGLSGMGKYYGQAG 419
Cdd:PRK09407 455 WgsVDA-PMGGMKDSGLGRRHGAEG 478
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
105-380 |
6.56e-47 |
|
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: 168.54 E-value: 6.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 105 PYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYF----APEAV-TVVTGGREEISALLE 179
Cdd:cd07130 132 PLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLekngLPGAIaSLVCGGADVGEALVK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 180 LP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIA 258
Cdd:cd07130 212 DPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 259 DDFIARikrsLTAMYGE----DPsRSPDfARMISAHDAQRVANYI--------QPEKVVHGG-RFDIPGRYVEPTVLYPS 325
Cdd:cd07130 292 DEVLER----LKKAYKQvrigDP-LDDG-TLVGPLHTKAAVDNYLaaieeaksQGGTVLFGGkVIDGPGNYVEPTIVEGL 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 502316442 326 SwDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLG 380
Cdd:cd07130 366 S-DAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLG 419
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-431 |
1.26e-46 |
|
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: 167.91 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 8 LDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLfEITVPLgVIDYYRRHLVDLMApqqve 87
Cdd:cd07559 44 VDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETL-AADIPL-AIDHFRYFAGVIRA----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 88 ippgleAEGYRGMI--------YKEPYGPTLVIGPFNAPVLLL---LDPAiaaLAAGNPVTLKPANTTPTVAALLQTLIP 156
Cdd:cd07559 117 ------QEGSLSEIdedtlsyhFHEPLGVVGQIIPWNFPLLMAawkLAPA---LAAGNTVVLKPASQTPLSILVLMELIG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 157 KYFAPEAVTVVTG-GREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPT-----VVDATANLDIA 229
Cdd:cd07559 188 DLLPKGVVNVVTGfGSEAGKPLASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNiffddAMDADDDFDDK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 230 IDRIAWGHNAISGQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSrspDFARMI----SAHDAQRVANYIQPEK-- 303
Cdd:cd07559 268 AEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL---DPETMMgaqvSKDQLEKILSYVDIGKee 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 304 ----VVHGGRFDIP----GRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAI 375
Cdd:cd07559 345 gaevLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRA 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 502316442 376 DRFLGSVSFGGGCVNQTNL---HCwidslPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07559 425 LRVARGIQTGRVWVNCYHQypaHA-----PFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
104-431 |
5.92e-46 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 166.16 E-value: 5.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 104 EPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTG-GREEISALLELP 181
Cdd:cd07143 143 EPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGyGRTCGNAISSHM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 182 -FDFIFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIAD 259
Cdd:cd07143 223 dIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYD 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 260 DFIARIKRSLTAM-----YGEDPSRSPDfarmISAHDAQRVANYIQPEK------VVHGGRFDIPGRYVEPTVLYPSSWD 328
Cdd:cd07143 303 KFVKRFKEKAKKLkvgdpFAEDTFQGPQ----VSQIQYERIMSYIESGKaegatvETGGKRHGNEGYFIEPTIFTDVTED 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 329 DPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAIdRFLGSVSFGGGCVNQTNLhcwID-SLPFGGV 406
Cdd:cd07143 379 MKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNiNNAI-RVANALKAGTVWVNCYNL---LHhQVPFGGY 454
|
330 340
....*....|....*....|....*
gi 502316442 407 GLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07143 455 KQSGIGRELGEYALENYTQIKAVHI 479
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
100-393 |
2.69e-45 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 162.60 E-value: 2.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 100 MIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALL 178
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVfNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 179 --ELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHS 256
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 257 IADDFIARIKRSLTAMYGEDPSRSPDFAR--MISAHDAQRVANYI-----QPEKVVHGG-RFDIPGRYVEPTVLYPSSWD 328
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFGNPAERNDIAMgpLINAAALERVEQKVaraveEGARVALGGkAVEGKGYYYPPTLLLDVRQE 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502316442 329 DPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTN 393
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREN 370
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
30-425 |
7.90e-45 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 163.05 E-value: 7.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 30 LDRMERLLRENQEAFCNALYQDFRKPpFEQLFEITVPL--GVIDYYRRHLVDLmapQQVEIPpgleAEG-YRGMIYKEPY 106
Cdd:cd07142 71 LLRFADLLEKHADELAALETWDNGKP-YEQARYAEVPLaaRLFRYYAGWADKI---HGMTLP----ADGpHHVYTLHEPI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 107 GPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALL--ELPFD 183
Cdd:cd07142 143 GVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVlNIVTGFGPTAGAAIasHMDVD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 184 FIFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVVDATANLDIAIDRiawGHNAI---SGQWCIAPGYVYVHHSIAD 259
Cdd:cd07142 223 KVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVEL---AHFALffnQGQCCCAGSRTFVHESIYD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 260 DFIARIK-RSLTAMYGeDPSRSP-DFARMISAHDAQRVANYIQPEK------VVHGGRFDIPGRYVEPTVLYPSSWDDPA 331
Cdd:cd07142 300 EFVEKAKaRALKRVVG-DPFRKGvEQGPQVDKEQFEKILSYIEHGKeegatlITGGDRIGSKGYYIQPTIFSDVKDDMKI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 332 MQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLhcWIDSLPFGGVGLSGM 411
Cdd:cd07142 379 ARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDV--FDASIPFGGYKMSGI 456
|
410
....*....|....
gi 502316442 412 GKyygQAGFDALSN 425
Cdd:cd07142 457 GR---EKGIYALNN 467
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
8-412 |
1.64e-44 |
|
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: 161.43 E-value: 1.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 8 LDRQREFFLTDATKSAAW-RLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMApqqV 86
Cdd:cd07148 27 LDTAHALFLDRNNWLPAHeRIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGG---R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 87 EIPPGLEA--EGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEA- 163
Cdd:cd07148 104 EIPMGLTPasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGw 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 164 VTVVTGGREEISALLELP-FDFIFFTGSAAVGkVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISG 242
Cdd:cd07148 184 CQAVPCENAVAEKLVTDPrVAFFSFIGSARVG-WMLRSKLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 243 QWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSR-SPDFARMISAHDAQRVANYIQpEKVVHGGRFDIPGRYV---- 317
Cdd:cd07148 263 QVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDpDTEVGPLIRPREVDRVEEWVN-EAVAAGARLLCGGKRLsdtt 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 318 -EPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDqraIDRFLGSVSFGGGCVNQTNLHC 396
Cdd:cd07148 342 yAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKD---LDVALKAVRRLDATAVMVNDHT 418
|
410
....*....|....*...
gi 502316442 397 W--IDSLPFGGVGLSGMG 412
Cdd:cd07148 419 AfrVDWMPFAGRRQSGYG 436
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
103-432 |
8.15e-44 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 160.43 E-value: 8.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 103 KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALLELP 181
Cdd:PRK13252 140 REPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVfNVVQGDGRVGAWLTEHP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 182 -FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIADD 260
Cdd:PRK13252 220 dIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 261 FIARIKRSLTAMYGEDPS-RSPDFARMISAHDAQRVANYIQPEK-----VVHGGRFDIP-----GRYVEPTVLYPSSWDD 329
Cdd:PRK13252 300 FEARLLERVERIRIGDPMdPATNFGPLVSFAHRDKVLGYIEKGKaegarLLCGGERLTEggfanGAFVAPTVFTDCTDDM 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 330 PAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD----QRAIDRFLGSVsfgggcvnqtnlhCWIDS----- 400
Cdd:PRK13252 380 TIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVIHQLEAGI-------------CWINTwgesp 446
|
330 340 350
....*....|....*....|....*....|....
gi 502316442 401 --LPFGGVGLSGMGKYYGQAGFDALSNTKSLLIG 432
Cdd:PRK13252 447 aeMPVGGYKQSGIGRENGIATLEHYTQIKSVQVE 480
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
94-431 |
1.45e-43 |
|
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: 159.06 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 94 AEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTGGRE 172
Cdd:cd07146 109 GKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 173 EI-SALLELP-FDFIFFTGSAAVGKVVmrAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGY 250
Cdd:cd07146 189 EIgDELITHPdVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 251 VYVHHSIADDFIARI-KRSLTAMYGeDPSR-SPDFARMISAHDAQRVANYI-----QPEKVVHGGRFDipGRYVEPTVLY 323
Cdd:cd07146 267 ILVHESVADEFVDLLvEKSAALVVG-DPMDpATDMGTVIDEEAAIQIENRVeeaiaQGARVLLGNQRQ--GALYAPTVLD 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 324 PSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNlHCWIDSLPF 403
Cdd:cd07146 344 HVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVP-GFRSELSPF 422
|
330 340
....*....|....*....|....*....
gi 502316442 404 GGVGLSGMGKYYG-QAGFDALSNTKSLLI 431
Cdd:cd07146 423 GGVKDSGLGGKEGvREAMKEMTNVKTYSL 451
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-431 |
3.12e-43 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 158.39 E-value: 3.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLfEITVPLGvIDYYRRHLVDLMAP--QQVEIP 89
Cdd:cd07117 48 QEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETR-AVDIPLA-ADHFRYFAGVIRAEegSANMID 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 90 pgleaEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTP----TVAALLQTLIPKyfapEAVT 165
Cdd:cd07117 126 -----EDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSlsllELAKIIQDVLPK----GVVN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTG-GREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQ 243
Cdd:cd07117 197 IVTGkGSKSGEYLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 244 WCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYIQPEK------VVHGGRFD----I 312
Cdd:cd07117 277 VCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPlDPDTQMGAQVNKDQLDKILSYVDIAKeegakiLTGGHRLTenglD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 313 PGRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAIdRFLGSVSFGG---GC 388
Cdd:cd07117 357 KGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDiNRAL-RVARAVETGRvwvNT 435
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 502316442 389 VNQTNLHCwidslPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07117 436 YNQIPAGA-----PFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
70-412 |
2.22e-42 |
|
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: 156.97 E-value: 2.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 70 ID---YYRRHLVDLMAPQQVEIPPGlEAEGYRgmiyKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPT 146
Cdd:cd07125 134 IDfcrYYAAQARELFSDPELPGPTG-ELNGLE----LHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 147 VAALLQTL-----IPKyfapEAVTVVTGGREEI-SALLELP-FDFIFFTGSAAVGKVVMRAAAEH---LTPVILELGGQN 216
Cdd:cd07125 209 IAARAVELlheagVPR----DVLQLVPGDGEEIgEALVAHPrIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 217 PTVVDATANLDIAIDRI---AWGHnaiSGQWCIAPGYVYVHHSIADDFIARIKRSLTAMYGEDPS-RSPDFARMISAHDA 292
Cdd:cd07125 285 AMIVDSTALPEQAVKDVvqsAFGS---AGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWdLSTDVGPLIDKPAG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 293 QRVANYIQ----PEKVVHGGRFDIP-GRYVEPTVLY-PSSWDdpaMQQEIFGPVLPVLPYD--DLDEVIETIKRKPKSLA 364
Cdd:cd07125 362 KLLRAHTElmrgEAWLIAPAPLDDGnGYFVAPGIIEiVGIFD---LTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLT 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502316442 365 AYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDSLPFGGVGLSGMG 412
Cdd:cd07125 439 LGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTG 486
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-421 |
6.15e-41 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 152.58 E-value: 6.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 19 ATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQqvEIPPGLEAEGYR 98
Cdd:PLN02467 67 ARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQ--KAPVSLPMETFK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 99 GMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPAN-TTPTVAALLQTLIPKYFAPEAVTVVTG-GREEISA 176
Cdd:PLN02467 145 GYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSElASVTCLELADICREVGLPPGVLNVVTGlGTEAGAP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 177 LLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHH 255
Cdd:PLN02467 225 LASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIARIKRSLTAMYGEDPsRSPD--FARMISAHDAQRVANYIQPEK-----VVHGGrfDIP-----GRYVEPTVLY 323
Cdd:PLN02467 305 RIASEFLEKLVKWAKNIKISDP-LEEGcrLGPVVSEGQYEKVLKFISTAKsegatILCGG--KRPehlkkGFFIEPTIIT 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 324 PSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFlgSVSFGGGCVnqtnlhcWID---- 399
Cdd:PLN02467 382 DVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERV--SEAFQAGIV-------WINcsqp 452
|
410 420
....*....|....*....|....*
gi 502316442 400 ---SLPFGGVGLSGMGKYYGQAGFD 421
Cdd:PLN02467 453 cfcQAPWGGIKRSGFGRELGEWGLE 477
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
36-412 |
1.65e-40 |
|
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: 151.58 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 36 LLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQ--VEIPPGLEAEGYRGMiykepyGPTLVIG 113
Cdd:cd07083 89 LLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVevVPYPGEDNESFYVGL------GAGVVIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 114 PFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTV-AALLQTLIPKYFAPEAVTVVTGGREEI-SALLELP-FDFIFFTGS 190
Cdd:cd07083 163 PWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVgYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHErIRGINFTGS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 191 AAVGKVVMRAAAEHLT------PVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIADDFIAR 264
Cdd:cd07083 243 LETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLER 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 265 IKRSLTAMYGEDPSR-SPDFARMISAHDAQRVANYIQPEK-----VVHGGRFDIPGRYVEPTVLYPSSWDDPAMQQEIFG 338
Cdd:cd07083 323 LLKRAERLSVGPPEEnGTDLGPVIDAEQEAKVLSYIEHGKnegqlVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFG 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502316442 339 PVLPVLPY--DDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWIDSLPFGGVGLSGMG 412
Cdd:cd07083 403 PVLSVIRYkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTN 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
104-425 |
1.17e-38 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 146.88 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 104 EPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTG-GREEISALLE-L 180
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVlNVVSGfGPTAGAALAShM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 181 PFDFIFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVVDATANLDIAIDriaWGHNAI---SGQWCIAPGYVYVHHS 256
Cdd:PLN02466 274 DVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVE---LAHFALffnQGQCCCAGSRTFVHER 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 257 IADDFIARIK-RSLTAMYGeDPSRSP-DFARMISAHDAQRVANYIQ------PEKVVHGGRFDIPGRYVEPTVLYPSSWD 328
Cdd:PLN02466 351 VYDEFVEKAKaRALKRVVG-DPFKKGvEQGPQIDSEQFEKILRYIKsgvesgATLECGGDRFGSKGYYIQPTVFSNVQDD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 329 DPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNqtnlhCW--ID-SLPFGG 405
Cdd:PLN02466 430 MLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN-----CFdvFDaAIPFGG 504
|
330 340
....*....|....*....|
gi 502316442 406 VGLSGMGKyygQAGFDALSN 425
Cdd:PLN02466 505 YKMSGIGR---EKGIYSLNN 521
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
103-431 |
9.64e-38 |
|
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: 143.79 E-value: 9.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 103 KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTG-GREEISALLEL 180
Cdd:cd07140 145 REPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGsGSLVGQRLSDH 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 181 PfDF--IFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVVDATANLDIAIDRiawGHNAI---SGQWCIAPGYVYVH 254
Cdd:cd07140 225 P-DVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRM---GMSSVffnKGENCIAAGRLFVE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 255 HSIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYIQP-----EKVVHGG-RFDIPGRYVEPTVLYPSSW 327
Cdd:cd07140 301 ESIHDEFVRRVVEEVKKMKIGDPlDRSTDHGPQNHKAHLDKLVEYCERgvkegATLVYGGkQVDRPGFFFEPTVFTDVED 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 328 DDPAMQQEIFGPVLPVLPYD--DLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLhcwID-SLPFG 404
Cdd:cd07140 381 HMFIAKEESFGPIMIISKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNK---TDvAAPFG 457
|
330 340
....*....|....*....|....*..
gi 502316442 405 GVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07140 458 GFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
97-435 |
1.32e-37 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 143.42 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 97 YRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEIS 175
Cdd:PLN02766 150 LQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGViNVVTGFGPTAG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 176 ALL--ELPFDFIFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVY 252
Cdd:PLN02766 230 AAIasHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVY 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 253 VHHSIADDFIARIKRSLTAMYGEDPSRSPdfARMISAHDAQ---RVANYIQPEK-----VVHGGR--FDiPGRYVEPTVL 322
Cdd:PLN02766 310 VQEGIYDEFVKKLVEKAKDWVVGDPFDPR--ARQGPQVDKQqfeKILSYIEHGKregatLLTGGKpcGD-KGYYIEPTIF 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 323 YPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNqtnlhCWI---D 399
Cdd:PLN02766 387 TDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN-----CYFafdP 461
|
330 340 350
....*....|....*....|....*....|....*.
gi 502316442 400 SLPFGGVGLSGMGKYYGQAGFDALSNTKSLLIGNPD 435
Cdd:PLN02766 462 DCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPLYN 497
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
22-432 |
2.81e-35 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 136.58 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 22 SAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMApqqvEIPPGLEAEGyRGMI 101
Cdd:PRK11241 68 TAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG----DTIPGHQADK-RLIV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 102 YKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISAllEL 180
Cdd:PRK11241 143 IKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVfNVVTGSAGAVGG--EL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 181 PFDFIF----FTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHS 256
Cdd:PRK11241 221 TSNPLVrklsFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 257 IADDFIARIKRSLTAMY-GEDPSRSPDFARMISAHDAQRVANYI-----QPEKVVHGGR-FDIPGRYVEPTVLYPSSWDD 329
Cdd:PRK11241 301 VYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEEHIadaleKGARVVCGGKaHELGGNFFQPTILVDVPANA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 330 PAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCwiDSLPFGGVGLS 409
Cdd:PRK11241 381 KVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISN--EVAPFGGIKAS 458
|
410 420
....*....|....*....|...
gi 502316442 410 GMGKYYGQAGFDALSNTKSLLIG 432
Cdd:PRK11241 459 GLGREGSKYGIEDYLEIKYMCIG 481
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
80-427 |
1.04e-34 |
|
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: 134.95 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 80 LMAPQQVEIPPGLEAEGYRgmiykEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYF 159
Cdd:cd07085 116 LKGEYLENVARGIDTYSYR-----QPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 160 APEAV-TVVTGGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGH 237
Cdd:cd07085 191 LPDGVlNVVHGGKEAVNALLDHPdIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 238 NAISGQWCIAPGYVYVHHSIADDFIARIK---RSLTAMYGEDPSrsPDFARMISAHDAQRVANYIQP-----EKVVHGGR 309
Cdd:cd07085 271 FGAAGQRCMALSVAVAVGDEADEWIPKLVeraKKLKVGAGDDPG--ADMGPVISPAAKERIEGLIESgveegAKLVLDGR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 310 -FDIP----GRYVEPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSF 384
Cdd:cd07085 349 gVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDA 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502316442 385 GGGCVNqtnlhcwI------DSLPFGGVGLS--GMGKYYGQAGFDALSNTK 427
Cdd:cd07085 429 GMVGIN-------VpipvplAFFSFGGWKGSffGDLHFYGKDGVRFYTQTK 472
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
102-431 |
1.00e-32 |
|
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: 129.49 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 102 YKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAVTVVTGGREEISALLELP 181
Cdd:cd07116 133 FHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 182 FDF--IFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVV--DATANLDIAIDRIAWGHNAI---SGQWCIAPGYVYVH 254
Cdd:cd07116 213 KRIakVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFfaDVMDADDAFFDKALEGFVMFalnQGEVCTCPSRALIQ 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 255 HSIADDFIARIKRSLTAMYGEDPSrspDFARMISAHDAQ----RVANYIQPEK-----VVHGGR-----FDIPGRYVEPT 320
Cdd:cd07116 293 ESIYDRFMERALERVKAIKQGNPL---DTETMIGAQASLeqleKILSYIDIGKeegaeVLTGGErnelgGLLGGGYYVPT 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 321 VLYPSSwDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQtnLHCWIDS 400
Cdd:cd07116 370 TFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNC--YHLYPAH 446
|
330 340 350
....*....|....*....|....*....|.
gi 502316442 401 LPFGGVGLSGMGKYYGQAGFDALSNTKSLLI 431
Cdd:cd07116 447 AAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
106-419 |
1.48e-32 |
|
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: 129.05 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 106 YGPTLVIG---PFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALLELP 181
Cdd:cd07111 145 WKPVGVVGqivPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVlNIVTGNGSFGSALANHP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 182 -FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAwghNAI---SGQWCIAPGYVYVHHSI 257
Cdd:cd07111 225 gVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIV---DAIwfnQGQVCCAGSRLLVQESV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 258 ADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYIQPEKVVHGGRF----DIP--GRYVEPTVLYPSSWDDP 330
Cdd:cd07111 302 AEELIRKLKERMSHLRVGDPlDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFqpgaDLPskGPFYPPTLFTNVPPASR 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 331 AMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLhcwID-SLPFGGVGLS 409
Cdd:cd07111 382 IAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNL---FDaAAGFGGYRES 458
|
330
....*....|
gi 502316442 410 GMGKYYGQAG 419
Cdd:cd07111 459 GFGREGGKEG 468
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
87-386 |
1.70e-31 |
|
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: 125.43 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 87 EIPPGLEAEGYRgmiYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFA--PEAV 164
Cdd:cd07084 85 HLGQGLKQQSHG---YRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlpPEDV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 165 TVVTGGREEISALLELP-FDFIFFTGSAAVGKVVmrAAAEHLTPVILELGGQNPTVVDATAN-LDIAIDRIAWGHNAISG 242
Cdd:cd07084 162 TLINGDGKTMQALLLHPnPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 243 QWCIAPGYVYVHH--------SIADDFIARIKRSLTAMygeDPSRSPDFARMISAHDAQRVANYIQPEKVVHGGRFD-IP 313
Cdd:cd07084 240 QKCTAQSMLFVPEnwsktplvEKLKALLARRKLEDLLL---GPVQTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPsIY 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502316442 314 GRYVEPTVLYPSSWDD---PAMQQEIFGPVLPVLPYDDLDE--VIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGG 386
Cdd:cd07084 317 GACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAG 394
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
8-432 |
1.86e-31 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 125.62 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 8 LDRQREFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQqve 87
Cdd:PRK09406 29 IARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALLADE--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 88 iPPGLEAEG-YRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPE-AVT 165
Cdd:PRK09406 106 -PADAAAVGaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDgCFQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTGGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQW 244
Cdd:PRK09406 185 TLLVGSGAVEAILRDPrVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 245 CIAPGYVYVHHSIADDFIARIKRSLTAMYGEDP-SRSPDFARMISAHDAQRVANYI-----QPEKVVHGG-RFDIPGRYV 317
Cdd:PRK09406 265 CIAAKRFIVHADVYDAFAEKFVARMAALRVGDPtDPDTDVGPLATEQGRDEVEKQVddavaAGATILCGGkRPDGPGWFY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 318 EPTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVN-QTNLHc 396
Cdd:PRK09406 345 PPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINgMTVSY- 423
|
410 420 430
....*....|....*....|....*....|....*.
gi 502316442 397 wiDSLPFGGVGLSGMGKYYGQAGFDALSNTKSLLIG 432
Cdd:PRK09406 424 --PELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
13-412 |
3.08e-31 |
|
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: 125.41 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 13 EFFLTDATKSAAwrldQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVEippgl 92
Cdd:TIGR01238 89 TWNATPAKERAA----KLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVE----- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 93 eaegyrgmiykePYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKY-FAPEAVTVVTGGR 171
Cdd:TIGR01238 160 ------------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 172 EEISALL--ELPFDFIFFTGSAAVGKVVMRAAAEHL---TPVILELGGQNPTVVDATANLD-IAIDRIAWGHNAiSGQWC 245
Cdd:TIGR01238 228 ADVGAALtsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEqVVRDVLRSAFDS-AGQRC 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 246 IAPGYVYVHHSIADDFIARIKRSLTAMYGEDPSR-SPDFARMISAHDAQRVANYIQP----EKVVHGGRFDIP-----GR 315
Cdd:TIGR01238 307 SALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLlTTDVGPVIDAEAKQNLLAHIEHmsqtQKKIAQLTLDDSracqhGT 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 316 YVEPTVLYPSSWDdpAMQQEIFGPVLPVLPY--DDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTN 393
Cdd:TIGR01238 387 FVAPTLFELDDIA--ELSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQ 464
|
410
....*....|....*....
gi 502316442 394 LHCWIDSLPFGGVGLSGMG 412
Cdd:TIGR01238 465 VGAVVGVQPFGGQGLSGTG 483
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-410 |
4.60e-31 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 124.69 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 12 REFFLTDATKSAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVID-----YYRRhlvdlMAPQQV 86
Cdd:PRK09457 47 RAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINKIAisiqaYHER-----TGEKRS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 87 EIPPGleaegyRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-T 165
Cdd:PRK09457 122 EMADG------AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVlN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 166 VVTGGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVI-LELGGQNPTVVDATANLDIAIdriawgHNAI--- 240
Cdd:PRK09457 196 LVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQPEKILaLEMGGNNPLVIDEVADIDAAV------HLIIqsa 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 241 ---SGQWCIAPGYVYVHHSI-ADDFIARIKRSLTAM----YGEDPSrsPDFARMISAHDAQRVANyIQPEKVVHGGRFDI 312
Cdd:PRK09457 270 fisAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLtvgrWDAEPQ--PFMGAVISEQAAQGLVA-AQAQLLALGGKSLL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 313 PGRYVEP--TVLYPSSWDDPAMQ----QEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSfgG 386
Cdd:PRK09457 347 EMTQLQAgtGLLTPGIIDVTGVAelpdEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIR--A 424
|
410 420
....*....|....*....|....*..
gi 502316442 387 GCVN---QTNLHCwiDSLPFGGVGLSG 410
Cdd:PRK09457 425 GIVNwnkPLTGAS--SAAPFGGVGASG 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
22-429 |
1.53e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 120.35 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 22 SAAWRLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHlvdlmAPQQVEIPPGLeAEGYRGMI 101
Cdd:PRK13968 49 NIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEH-----GPAMLKAEPTL-VENQQAVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 102 YKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPAnttPTVAALLQtLIPKYFA----PEAV-TVVTGGREEISA 176
Cdd:PRK13968 123 EYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA---PNVMGCAQ-LIAQVFKdagiPQGVyGWLNADNDGVSQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 177 LLELP-FDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHH 255
Cdd:PRK13968 199 MINDSrIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIARIKRSLTAMYGEDPSRSPDFARMISAHD------AQRVANYIQPEKVVHGG-RFDIPGRYVEPTVLYPSSWD 328
Cdd:PRK13968 279 GIASAFTERFVAAAAALKMGDPRDEENALGPMARFDlrdelhHQVEATLAEGARLLLGGeKIAGAGNYYAPTVLANVTPE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 329 DPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQtnlHCWIDS-LPFGGVG 407
Cdd:PRK13968 359 MTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFING---YCASDArVAFGGVK 435
|
410 420
....*....|....*....|..
gi 502316442 408 LSGMGKYYGQAGFDALSNTKSL 429
Cdd:PRK13968 436 KSGFGRELSHFGLHEFCNIQTV 457
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
100-413 |
1.76e-29 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 120.39 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 100 MIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTG-GREEISAL 177
Cdd:PRK09847 152 MIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVlNVVTGfGHEAGQAL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 178 LELP-FDFIFFTGSAAVGKVVMRAAAE-HLTPVILELGGQNPTVVDATA-NLDIAIDRIAWGHNAISGQWCIAPGYVYVH 254
Cdd:PRK09847 232 SRHNdIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 255 HSIADDFIARIKRSLTAMYGEDPsRSPD--FARMISAHDAQRVANYIqpEKVVHGGRFDIPGR------YVEPTVLYPSS 326
Cdd:PRK09847 312 ESIADEFLALLKQQAQNWQPGHP-LDPAttMGTLIDCAHADSVHSFI--REGESKGQLLLDGRnaglaaAIGPTIFVDVD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 327 WDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNlhcwiD---SLPF 403
Cdd:PRK09847 389 PNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYN-----DgdmTVPF 463
|
330
....*....|
gi 502316442 404 GGVGLSGMGK 413
Cdd:PRK09847 464 GGYKQSGNGR 473
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
104-412 |
4.00e-27 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 114.96 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 104 EPYGPTLVIGPFNAPVlllldpAI------AALAAGNPVTLKPANTTPTVAA-----LLQTLIPKyfapEAVTVVTG-GR 171
Cdd:PRK11905 675 KPLGPVVCISPWNFPL------AIftgqiaAALVAGNTVLAKPAEQTPLIAAravrlLHEAGVPK----DALQLLPGdGR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 172 EEISALLELP-FDFIFFTGSAAVGKVVMRAAAEHL---TPVILELGGQNPTVVDATANLDIAI-DRIAWGHNAiSGQWCI 246
Cdd:PRK11905 745 TVGAALVADPrIAGVMFTGSTEVARLIQRTLAKRSgppVPLIAETGGQNAMIVDSSALPEQVVaDVIASAFDS-AGQRCS 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 247 APGYVYVHHSIADDFIARIKRSLTAMYGEDPSR-SPDFARMISAHDAQRVANYIQPEK----VVHggRFDIP-----GRY 316
Cdd:PRK11905 824 ALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRlSTDVGPVIDAEAQANIEAHIEAMRaagrLVH--QLPLPaetekGTF 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 317 VEPTVLYPSSWDDpaMQQEIFGPVLPVLPY--DDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNL 394
Cdd:PRK11905 902 VAPTLIEIDSISD--LEREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNII 979
|
330
....*....|....*...
gi 502316442 395 HCWIDSLPFGGVGLSGMG 412
Cdd:PRK11905 980 GAVVGVQPFGGEGLSGTG 997
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-434 |
2.85e-26 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 111.00 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 21 KSAAW-RLDQLDRMERLLRENQEAFCNALYQDFRKPPFEQLFEITVPLGVIDYYRRHLVDLMAPQQVEIP---PGLEAEG 96
Cdd:PLN00412 71 KTPLWkRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGKFLVSdsfPGNERNK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 97 YrGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPAnTTPTVAAL--LQTLIPKYFAPEAVTVVTGGREEI 174
Cdd:PLN00412 151 Y-CLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPP-TQGAVAALhmVHCFHLAGFPKGLISCVTGKGSEI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 175 SALLEL--PFDFIFFTGsAAVGKVVMRAAAehLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVY 252
Cdd:PLN00412 229 GDFLTMhpGVNCISFTG-GDTGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 253 VHHSIADDFIARIKRSLTAMYGEDPSRSPDFARMISahdaQRVANYIQ---PEKVVHGGRFDIPGRYvEPTVLYPSSWDD 329
Cdd:PLN00412 306 VMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVS----ESSANFIEglvMDAKEKGATFCQEWKR-EGNLIWPLLLDN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 330 --PAMQ---QEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD-QRAI---DRF-LGSVSFGGGCVNQTnlhcwiD 399
Cdd:PLN00412 381 vrPDMRiawEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAIlisDAMeTGTVQINSAPARGP------D 454
|
410 420 430
....*....|....*....|....*....|....*
gi 502316442 400 SLPFGGVGLSGMGKYYGQAGFDALSNTKSLLIGNP 434
Cdd:PLN00412 455 HFPFQGLKDSGIGSQGITNSINMMTKVKSTVINLP 489
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
105-412 |
8.86e-26 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 111.22 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 105 PYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAA-----LLQTLIPkyfaPEAVTVVTGGREEISALL- 178
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAqavriLLEAGVP----AGVVQLLPGRGETVGAALv 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 179 -ELPFDFIFFTGSAAVGKVVMRAAAEHL------TPVILELGGQNPTVVDATANLD-IAIDRIAWGHNAiSGQWCIAPGY 250
Cdd:PRK11809 844 aDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEqVVADVLASAFDS-AGQRCSALRV 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 251 VYVHHSIADDFIARIKRSLTAMYGEDPSR-SPDFARMISAHDAQRVANYIQPEK--------VVHGGRFDIP-GRYVEPT 320
Cdd:PRK11809 923 LCLQDDVADRTLKMLRGAMAECRMGNPDRlSTDIGPVIDAEAKANIERHIQAMRakgrpvfqAARENSEDWQsGTFVPPT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 321 VLYPSSWDDpaMQQEIFGPVLPVLPY--DDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWI 398
Cdd:PRK11809 1003 LIELDSFDE--LKREVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVV 1080
|
330
....*....|....
gi 502316442 399 DSLPFGGVGLSGMG 412
Cdd:PRK11809 1081 GVQPFGGEGLSGTG 1094
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
112-412 |
3.51e-24 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 106.05 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 112 IGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAA-----LLQTLIPKyfapEAVTVVTGGREEI-SALLELP-FDF 184
Cdd:PRK11904 691 ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAeavklLHEAGIPK----DVLQLLPGDGATVgAALTADPrIAG 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 185 IFFTGSAAVGKVVMRAAAEH---LTPVILELGGQNPTVVDATANLDIAIDriawghNAIS------GQWCIAPGYVYVHH 255
Cdd:PRK11904 767 VAFTGSTETARIINRTLAARdgpIVPLIAETGGQNAMIVDSTALPEQVVD------DVVTsafrsaGQRCSALRVLFVQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 256 SIADDFIARIKRSLTAMYGEDPSR---------SPDFARMISAHdaqrVANYIQPEKVVHggRFDIP-----GRYVEPTV 321
Cdd:PRK11904 841 DIADRVIEMLKGAMAELKVGDPRLlstdvgpviDAEAKANLDAH----IERMKREARLLA--QLPLPagtenGHFVAPTA 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 322 LYPSSWDDpaMQQEIFGPVLPVLPY--DDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVNQTNLHCWID 399
Cdd:PRK11904 915 FEIDSISQ--LEREVFGPILHVIRYkaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVG 992
|
330
....*....|...
gi 502316442 400 SLPFGGVGLSGMG 412
Cdd:PRK11904 993 VQPFGGQGLSGTG 1005
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
105-390 |
6.64e-23 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 101.06 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 105 PYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVA----ALLQTLIPKYFAPEAV-TVVTGGREEISAL-L 178
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITiamtKLVAEVLEKNNLPGAIfTSFCGGAEIGEAIaK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 179 ELPFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSIA 258
Cdd:PLN02315 234 DTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIY 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 259 DDFIARIKRSLTAMYGEDPSRSPDFARMIsaHDAQRVANYIQPEKVV--HGGRF-------DIPGRYVEPTVLYPSSwDD 329
Cdd:PLN02315 314 DDVLEQLLTVYKQVKIGDPLEKGTLLGPL--HTPESKKNFEKGIEIIksQGGKIltggsaiESEGNFVQPTIVEISP-DA 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502316442 330 PAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGGGCVN 390
Cdd:PLN02315 391 DVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVN 451
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
62-410 |
6.72e-22 |
|
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: 98.04 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 62 EITVPLGVIDYYR---RHLVDLMAPQQVEIPPG----LEaegYRGMiykEpyGPTLVIGPFNAPvlllldpAIAA-LAA- 132
Cdd:cd07123 128 EIDAACELIDFLRfnvKYAEELYAQQPLSSPAGvwnrLE---YRPL---E--GFVYAVSPFNFT-------AIGGnLAGa 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 133 ----GNPVTLKPANTtptvAALLQTLIPKYFA-----PEAVTVVTGGREEIS-ALLELP-FDFIFFTGSAAVGKVVMRAA 201
Cdd:cd07123 193 palmGNVVLWKPSDT----AVLSNYLVYKILEeaglpPGVINFVPGDGPVVGdTVLASPhLAGLHFTGSTPTFKSLWKQI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 202 AEHLT-----PVIL-ELGGQNPTVVDATANLD---IAIDRIAWGHnaiSGQWCIAPGYVYVHHSIADdfiaRIKRSLTAM 272
Cdd:cd07123 269 GENLDryrtyPRIVgETGGKNFHLVHPSADVDslvTATVRGAFEY---QGQKCSAASRAYVPESLWP----EVKERLLEE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 273 YGE----DPSrspDFARMISA--HDA--QRVANYI-----QPE-KVVHGGRFD-IPGRYVEPTVLYPSSWDDPAMQQEIF 337
Cdd:cd07123 342 LKEikmgDPD---DFSNFMGAviDEKafDRIKGYIdhaksDPEaEIIAGGKCDdSVGYFVEPTVIETTDPKHKLMTEEIF 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 338 GPVLPVLPYDD--LDEVIETI-KRKPKSLAAYIFSKDQRAI-----------------DRFLGSVsfgggcVNQTnlhcw 397
Cdd:cd07123 419 GPVLTVYVYPDsdFEETLELVdTTSPYALTGAIFAQDRKAIreatdalrnaagnfyinDKPTGAV------VGQQ----- 487
|
410
....*....|...
gi 502316442 398 idslPFGGVGLSG 410
Cdd:cd07123 488 ----PFGGARASG 496
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
103-455 |
3.98e-21 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 96.35 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 103 KEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALLE-L 180
Cdd:PLN02419 247 REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVlNIVHGTNDTVNAICDdE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 181 PFDFIFFTGSAAVGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPG---YVYVHHSI 257
Cdd:PLN02419 327 DIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALStvvFVGDAKSW 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 258 ADDFIARIKrSLTAMYGEDPSrsPDFARMISAHDAQRVANYIQP-----EKVVHGGRfDI------PGRYVEPTVLYPSS 326
Cdd:PLN02419 407 EDKLVERAK-ALKVTCGSEPD--ADLGPVISKQAKERICRLIQSgvddgAKLLLDGR-DIvvpgyeKGNFIGPTILSGVT 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 327 WDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQRAIDRFLGSVSFGggcvnQTNLHCWID-SLPF-- 403
Cdd:PLN02419 483 PDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAG-----QIGINVPIPvPLPFfs 557
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 502316442 404 ---GGVGLSGMGKYYGQAGFDALSNTKSLlignpdkvldvfpPYAGKDIATSLAL 455
Cdd:PLN02419 558 ftgNKASFAGDLNFYGKAGVDFFTQIKLV-------------TQKQKDIHSPFSL 599
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
104-356 |
8.98e-21 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 95.78 E-value: 8.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 104 EPYGPTLVIGPFNAPVlllldpAI------AALAAGNPVTLKPANTTPTVAA-----LLQTLIPKyfapEAVTVVTGGRE 172
Cdd:COG4230 679 RGRGVFVCISPWNFPL------AIftgqvaAALAAGNTVLAKPAEQTPLIAAravrlLHEAGVPA----DVLQLLPGDGE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 173 EI-SALLELP-FDFIFFTGSAAVGKVVMRAAAEH---LTPVILELGGQNPTVVDATAnL------DI---AIDriawghN 238
Cdd:COG4230 749 TVgAALVADPrIAGVAFTGSTETARLINRTLAARdgpIVPLIAETGGQNAMIVDSSA-LpeqvvdDVlasAFD------S 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 239 AisGQWCIAPGYVYVHHSIADDFIARIKRsltAMyGE----DPSR-SPDF-------AR-MISAH------DAQRVANYI 299
Cdd:COG4230 822 A--GQRCSALRVLCVQEDIADRVLEMLKG---AM-AElrvgDPADlSTDVgpvidaeARaNLEAHiermraEGRLVHQLP 895
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 502316442 300 QPEKVVHggrfdipGRYVEPTVLYPSSWDDpaMQQEIFGPVLPVLPY--DDLDEVIETI 356
Cdd:COG4230 896 LPEECAN-------GTFVAPTLIEIDSISD--LEREVFGPVLHVVRYkaDELDKVIDAI 945
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
112-371 |
1.14e-20 |
|
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: 94.26 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 112 IGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVA-ALLQTLIPKYFAPE-AVTVVTGGREEISALLElPFDFIFFTG 189
Cdd:cd07128 151 INAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTeAVVKDIVESGLLPEgALQLICGSVGDLLDHLG-EQDVVAFTG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 190 SAAVGK-------VVMRAA-----AEHLTPVILelggqNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYVHHSI 257
Cdd:cd07128 230 SAATAAklrahpnIVARSIrfnaeADSLNAAIL-----GPDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEAR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 258 ADDFIARIKRSLTAMYGEDPSRspDFARMIS-AHDAQR------VANYIQPEKVVHGG--RFDIP------GRYVEPTVL 322
Cdd:cd07128 305 VDAVIEALKARLAKVVVGDPRL--EGVRMGPlVSREQRedvraaVATLLAEAEVVFGGpdRFEVVgadaekGAFFPPTLL 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502316442 323 Y--PSSWDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKD 371
Cdd:cd07128 383 LcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
102-372 |
2.59e-18 |
|
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: 86.83 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 102 YKEPYGPTLVIGPFNAPvlllL-------DPAiAALAAGNPVTLK--PA--NTTPTVAALLQTLIPKYFAPEAV-TVVTG 169
Cdd:cd07129 102 MLVPLGPVAVFGASNFP----LafsvaggDTA-SALAAGCPVVVKahPAhpGTSELVARAIRAALRATGLPAGVfSLLQG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 170 GREEIS-ALLELP-FDFIFFTGSAAVGKVVMRAAAEHLT--PVILELGGQNPTVVDATAnLDIAIDRIAWGHNAI----S 241
Cdd:cd07129 177 GGREVGvALVKHPaIKAVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFILPGA-LAERGEAIAQGFVGSltlgA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 242 GQWCIAPGYVYVHHSIA-DDFIARIKRSLTAmygedpsrSPDfARMISAHDAQRVANYIQ------PEKVVHGGRFDIPG 314
Cdd:cd07129 256 GQFCTNPGLVLVPAGPAgDAFIAALAEALAA--------APA-QTMLTPGIAEAYRQGVEalaaapGVRVLAGGAAAEGG 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502316442 315 RYVEPTVLYPSSWD---DPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDQ 372
Cdd:cd07129 327 NQAAPTLFKVDAAAflaDPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEED 387
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
107-385 |
7.84e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 79.75 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 107 GPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTptvAALLQTLI-----PKYFAPEAVTVVTGGREEISALLElP 181
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATAT---AWLTQRMVkdvvaAGILPAGALSVVCGSSAGLLDHLQ-P 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 182 FDFIFFTGSAAVGK-------VVMRAA-----AEHLTPVILelggqNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPG 249
Cdd:PRK11903 226 FDVVSFTGSAETAAvlrshpaVVQRSVrvnveADSLNSALL-----GPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 250 YVYVHHSIADDFIARIKRSLTAMYGEDPSRspDFARMIS-----AHDAQR--VANYIQPEKVVHGGR----FDIP---GR 315
Cdd:PRK11903 301 RIFVPEALYDAVAEALAARLAKTTVGNPRN--DGVRMGPlvsraQLAAVRagLAALRAQAEVLFDGGgfalVDADpavAA 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502316442 316 YVEPTVLYPSSWDDPAM--QQEIFGPVLPVLPYDDLDEVIETIKRKPKSLAAYIFSKDqraiDRFLGSVSFG 385
Cdd:PRK11903 379 CVGPTLLGASDPDAATAvhDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD----AAFLAAAALE 446
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
91-381 |
9.40e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 76.00 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 91 GLEAEGYRGmiykePYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVA-ALLQTLIPKYFAPEAVTVV-T 168
Cdd:cd07126 133 GQQSSGYRW-----PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMeQFLRLLHLCGMPATDVDLIhS 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 169 GGREEISALLELPFDFIFFTGSAavgKVVMRAAAEHLTPVILELGGQN-----PTVVDatanldiaIDRIAWGHN----A 239
Cdd:cd07126 208 DGPTMNKILLEANPRMTLFTGSS---KVAERLALELHGKVKLEDAGFDwkilgPDVSD--------VDYVAWQCDqdayA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 240 ISGQWCIAPGYVYVHHSIAD-DFIARIKRSLTAMYGEDPSRSPdfarmISAHDAQRVANY------IQPEKVVHGGR--- 309
Cdd:cd07126 277 CSGQKCSAQSILFAHENWVQaGILDKLKALAEQRKLEDLTIGP-----VLTWTTERILDHvdkllaIPGAKVLFGGKplt 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 310 -FDIPGRY--VEPTVLY------PSSWDDPAMQQEIFGPVLPVLPYDD--LDEVIETIKRKPKSLAAYIFSKDQRAIDRF 378
Cdd:cd07126 352 nHSIPSIYgaYEPTAVFvpleeiAIEENFELVTTEVFGPFQVVTEYKDeqLPLVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
...
gi 502316442 379 LGS 381
Cdd:cd07126 432 LAN 434
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
105-392 |
3.58e-14 |
|
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: 74.44 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 105 PYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKP--ANTTP---TVAALLQTLIPKYFAPEAVTVVTGGREE-ISALL 178
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPhpAAILPlaiTVQVAREVLAEAGFDPNLVTLAADTPEEpIAQTL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 179 ELPFD--FIFFTGSAAVGKVVMRAAAEHLtpVILELGGQNPTVVDATANLDIAIDRIAWGHNAISGQWCIAPGYVYV--- 253
Cdd:cd07127 273 ATRPEvrIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprd 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 254 ------HHSIADDFIARIKRSLTAMYGeDPSR---------SPDFARMISahDAQRVANYIQPEKVVHGGRFdiPGRYVE 318
Cdd:cd07127 351 giqtddGRKSFDEVAADLAAAIDGLLA-DPARaaallgaiqSPDTLARIA--EARQLGEVLLASEAVAHPEF--PDARVR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 319 -PTVLYPSSWDDPAMQQEIFGPVLPVLPYDDLDEVIET---IKRKPKSLAAYIFSKDQRAIDRFLG---------SVSFG 385
Cdd:cd07127 426 tPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELareSVREHGAMTVGVYSTDPEVVERVQEaaldagvalSINLT 505
|
....*...
gi 502316442 386 GGC-VNQT 392
Cdd:cd07127 506 GGVfVNQS 513
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
104-266 |
1.58e-07 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 53.38 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 104 EPYGPTLVIGPFNAPvLLLLDPAIAALAAGNPVTLKP----ANTTPTVAALLQTLIPKYFAPEAV-TVVTGGREEISALL 178
Cdd:cd07077 99 FPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPhpsaPFTNRALALLFQAADAAHGPKILVlYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 179 ELP-FDFIFFTGSAAVgkvvMRAAAEH--LTPVILELGGQNPTVVDATANLDIA---IDRIAWGHNAIsgqwCIAPGYVY 252
Cdd:cd07077 178 SHPkIDLIVATGGRDA----VDAAVKHspHIPVIGFGAGNSPVVVDETADEERAsgsVHDSKFFDQNA----CASEQNLY 249
|
170
....*....|....
gi 502316442 253 VHHSIADDFIARIK 266
Cdd:cd07077 250 VVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
87-354 |
2.32e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 53.04 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 87 EIPPGL--EAEGYRGMIYKEPYGPTLVIGPFNAPVLLLLDPAIAALAAGNPVTLKP----ANTTPTVAALLQTLIPKYFA 160
Cdd:cd07081 75 EKTCGVltGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 161 PE--AVTVVTGGREEISALLELP-FDFIFFTGsaavGKVVMRAAAEHLTPVILELGGQNPTVVDATANLDIAIDRIAWGH 237
Cdd:cd07081 155 PEnlIGWIDNPSIELAQRLMKFPgIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 238 NAISGQWCIAPGYVYVHHSIADDFIARIK-RSLTAMYGEDPS-------RSPDFARMISAHDAQRVANYIQpEKVVHGGR 309
Cdd:cd07081 231 TFDNGVICASEQSVIVVDSVYDEVMRLFEgQGAYKLTAEELQqvqpvilKNGDVNRDIVGQDAYKIAAAAG-LKVPQETR 309
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 502316442 310 FDIpgryVEPTVLYpsswDDPAMQQEIFGPVLPVLPYDDLDEVIE 354
Cdd:cd07081 310 ILI----GEVTSLA----EHEPFAHEKLSPVLAMYRAANFADADA 346
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
87-378 |
3.04e-07 |
|
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: 52.62 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 87 EIPPGLE------AEGYRGMIYKE--PYGptlVIG---PFNAPVLLLLDPAIAALAAGNPVTLKPANTTPTVAALLQTLI 155
Cdd:cd07121 71 EKTPGTEdltttaWSGDNGLTLVEyaPFG---VIGaitPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 156 PKYFAPE------AVTVVTGGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEhltpVILELGGQNPTVVDATANLDI 228
Cdd:cd07121 148 NKAIAEAggpdnlVVTVEEPTIETTNELMAHPdINLLVVTGGPAVVKAALSSGKK----AIGAGAGNPPVVVDETADIEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 229 AIDRIAWG----HNAIsgqwCIAPGYVYVHHSIADDFIARIKRsltamYGedpsrspdfARMISAHDAQRVAnyiqpEKV 304
Cdd:cd07121 224 AARDIVQGasfdNNLP----CIAEKEVIAVDSVADYLIAAMQR-----NG---------AYVLNDEQAEQLL-----EVV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 305 VHGGRFDIPGR-YV--EPTVL-------YPSSW---------DDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSL-- 363
Cdd:cd07121 281 LLTNKGATPNKkWVgkDASKIlkaagieVPADIrliivetdkDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrh 360
|
330
....*....|....*
gi 502316442 364 AAYIFSKDQRAIDRF 378
Cdd:cd07121 361 TAIIHSKNVENLTKM 375
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
90-378 |
1.98e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 46.82 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 90 PGLEA------EGYRGMIYKE--PYGptlVIG---PFNAPVLLLLDPAIAALAAGNPVTLKP----ANTTPTVAALLQTL 154
Cdd:PRK15398 106 PGVEDlttealTGDNGLTLIEyaPFG---VIGavtPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 155 IPKYFAPE--AVTVVTGGREEISALLELP-FDFIFFTGSAAVGKVVMRAAAEhltpVILELGGQNPTVVDATANLDIAID 231
Cdd:PRK15398 183 IVAAGGPEnlVVTVAEPTIETAQRLMKHPgIALLVVTGGPAVVKAAMKSGKK----AIGAGAGNPPVVVDETADIEKAAR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 232 RIAWG----HNAIsgqwCIAPGYVYVHHSIADDFIARIKRsltamYGedpsrspdfARMISAHDAQRVanyiqpEKVVHG 307
Cdd:PRK15398 259 DIVKGasfdNNLP----CIAEKEVIVVDSVADELMRLMEK-----NG---------AVLLTAEQAEKL------QKVVLK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 308 GRFDIPGRYV--EPTVL-------YPSS---------WDDPAMQQEIFGPVLPVLPYDDLDEVIETIKRKPKSL--AAYI 367
Cdd:PRK15398 315 NGGTVNKKWVgkDAAKIleaaginVPKDtrllivetdANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIM 394
|
330
....*....|.
gi 502316442 368 FSKDQRAIDRF 378
Cdd:PRK15398 395 HSRNVDNLNKM 405
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
126-378 |
7.15e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 44.79 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 126 AIAALAAGNPVTLKP----ANTTPTVAALLQTLIPKYFAPE-AVTVVTG-GREEISALLELP-FDFIFFTGSAAVgkvvM 198
Cdd:cd07122 116 ALIALKTRNAIIFSPhpraKKCSIEAAKIMREAAVAAGAPEgLIQWIEEpSIELTQELMKHPdVDLILATGGPGM----V 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 199 RAAAEHLTPVIlelG---GQNPTVVDATANLDIAIDRIAWGH---NAISgqwCIAPGYVYVHHSIADDFIARIKRsltam 272
Cdd:cd07122 192 KAAYSSGKPAI---GvgpGNVPAYIDETADIKRAVKDIILSKtfdNGTI---CASEQSVIVDDEIYDEVRAELKR----- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316442 273 YGedpsrspdfARMISAHDAQRVANYIQPEKVVHggRFDIPGRYV------------EPTVL-----------YPSSwdd 329
Cdd:cd07122 261 RG---------AYFLNEEEKEKLEKALFDDGGTL--NPDIVGKSAqkiaelagievpEDTKVlvaeetgvgpeEPLS--- 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 502316442 330 pamqQEIFGPVLPVLPYDDLDEVIETIKR------KPKSLAayIFSKDQRAIDRF 378
Cdd:cd07122 327 ----REKLSPVLAFYRAEDFEEALEKARElleyggAGHTAV--IHSNDEEVIEEF 375
|
|
| |
