|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
5-550 |
0e+00 |
|
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: 852.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 5 LFEAHKPTLDAALSALRARGYWTPYAESPSPRSYGEDAAEAGKRAFESHLGRDFVLDQPGQAGWAATERSPYGVALDVRY 84
Cdd:cd07127 2 LFDKHRATLDAAVEAIASRGYWSPFPESPSPKIYGETAAAAGKAAFEALLGQRFDLDQPGASGWVGGEVSPYGVELGVTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 85 PVCAPDALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAFQAGGAHAQDRGLEAVATAW 164
Cdd:cd07127 82 PQCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQAGGPHAQDRGLEAVAYAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 165 DEMSRVPAEAVWEKPQGKNPPLRLRKHFEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVA 244
Cdd:cd07127 162 REMSRIPPTAEWEKPQGKHDPLAMEKTFTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 245 IAREVLAEQGLDPNLVTLAvVDDPAA--TRHLATHRAVKSIDFTGSTAFGNWLLDHARQAQVYAELAGVNNVVIESTDNY 322
Cdd:cd07127 242 VAREVLAEAGFDPNLVTLA-ADTPEEpiAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQVYTEKAGVNTVVVDSTDDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 323 KGMLKNLAFTLSLYAGQMCTTTQAIIVPAGGIDTDQGRKRFDEVAADLGAAVARFLSDESVATAVLGAIQSPATLARIEE 402
Cdd:cd07127 321 KAMLRNLAFSLSLYSGQMCTTPQNIYVPRDGIQTDDGRKSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 403 AHGFGQVVLASKALTHAEFPQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQLSERIVRERGALTVGLYS 482
Cdd:cd07127 401 ARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVREHGAMTVGVYS 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2230046767 483 TRSAVIETMTEATLRAGVALSLNLAGGVFVNQSAAFSDYHGVGMNPAANASYADAAFVANRFRVVQRR 550
Cdd:cd07127 481 TDPEVVERVQEAALDAGVALSINLTGGVFVNQSAAFSDFHGTGANPAANAALTDGAFVANRFRVVQRR 548
|
|
| PaaN_2 |
TIGR02288 |
phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening ... |
2-553 |
0e+00 |
|
phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardized in. This enzyme is related to aldehyde dehydrogenases and has a domain which is a member of the pfam00171 family. This family includes sequences from Burkholderia, Bordetella, Streptomyces. Other PaaN enzymes are represented by a separate model, TIGR02278.
Pssm-ID: 131341 Cd Length: 551 Bit Score: 851.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 2 SHPLFEAHKPTLDAALSALRARGYWTPYAESPspRSYGEDAAEAGKRAFESHLGRDFVLDQPGQAGWAATERSPYGVALD 81
Cdd:TIGR02288 1 AAQLFDRHRPTLEAAVQAIAARGYWSPFPESP--KVYGETAQDDGQAAFEALFGQDFDLGQPGRSGWVGGERSPYGVELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 82 VRYPVCAPDALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAFQAGGAHAQDRGLEAVA 161
Cdd:TIGR02288 79 VTYPQCDGDALLDAAHAALPGWRDAGARARAGVCLEILQRLNARSFEIAHAVMHTTGQAFMMAFQAGGPHAQDRGLEAVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 162 TAWDEMSRVPAEAVWEKPQGKNPPLRLRKHFEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAI 241
Cdd:TIGR02288 159 YAYREMSRIPETAVWEKPQGKNDPLKLKKRFTIVPRGIALVIGCSTFPTWNTYPGLFASLATGNPVLVKPHPGAILPLAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 242 SVAIAREVLAEQGLDPNLVTLAVVD--DPAATRhLATHRAVKSIDFTGSTAFGNWLLDHARQAQVYAELAGVNNVVIEST 319
Cdd:TIGR02288 239 TVQVAREVLGEAGFDPNLVTLAAFDpgHEAAQR-LATDPAVRIIDFTGSNAFGQWLEQNARQAQVYTEKAGVNTVIIEST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 320 DNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGGIDTDQGRKRFDEVAADLGAAVARFLSDESVATAVLGAIQSPATLAR 399
Cdd:TIGR02288 318 DDYKAMLRNLAFSLSLYSGQMCTTTQAILVPRDGIRTDQGRKSYDEVAADLATAIDGLLGDPARATAVLGAIQSPDTLAR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 400 IEEAHGFGQVVLASKALTHAEFPQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQLSERIVRERGALTVG 479
Cdd:TIGR02288 398 IAEARALGEVLLASTKIEHPEFPGARVRTPLLLKCDAADEAAYMQERFGPIAFVVAVDDGAHAVELARRSVREKGAMTVG 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2230046767 480 LYSTRSAVIETMTEATLRAGVALSLNLAGGVFVNQSAAFSDYHGVGMNPAANASYADAAFVANRFRVVQRRYHV 553
Cdd:TIGR02288 478 AYTTDPEVVDAVQEAAWDAAVALSLNLTGGVFVNQSAAFSDFHGTGGNPAANASLSDGAFVANRFRVVQRRRPA 551
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
89-549 |
4.16e-132 |
|
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: 392.37 E-value: 4.16e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 89 PDALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAFQAGGAHAQDRGLEAVATAWdems 168
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSY---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 169 RVPAEAVWEKPQGKNPplrlRKHFEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVAIARE 248
Cdd:cd07084 77 RIPHEPGNHLGQGLKQ----QSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 249 VLAeqgLDPNLVTLAvVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQAQVYAELAGVNNVVIEST-DNYKGMLK 327
Cdd:cd07084 153 AGL---LPPEDVTLI-NGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDaQAVDYVAW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 328 NLAFTLSLYAGQMCTTTQAIIVPAggidTDQGRKRFDEVAADlgaavarfLSDESVATAVLGAIQSPATLARIEEAHG-F 406
Cdd:cd07084 229 QCVQDMTACSGQKCTAQSMLFVPE----NWSKTPLVEKLKAL--------LARRKLEDLLLGPVQTFTTLAMIAHMENlL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 407 GQVVLASKALTHA----EFPQAQVRTPVIVACDAAD--EAAYMEERFGPISFVVRAADTGAALqLSERIVRERGALTVGL 480
Cdd:cd07084 297 GSVLLFSGKELKNhsipSIYGACVASALFVPIDEILktYELVTEEIFGPFAIVVEYKKDQLAL-VLELLERMHGSLTAAI 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230046767 481 YSTRSAVIETMTEATLRAGVALSLNLA-GGVFVNQsaafsdYHGVGMNPAANASYAD---AAFVANRFRVVQR 549
Cdd:cd07084 376 YSNDPIFLQELIGNLWVAGRTYAILRGrTGVAPNQ------NHGGGPAADPRGAGIGgpeAIKLVWRCHAEQA 442
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
90-526 |
1.53e-62 |
|
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: 211.68 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQG-WMMAFQAGGAHAQDRGLEAVATAWdems 168
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPiEEALGEVARAADTFRYYAGLARRL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 169 rvpaeavwEKPQGKNPPLRLRKHFEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVAIARE 248
Cdd:cd07078 77 --------HGEVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 249 VlaeqGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNNVVIESTDNYKGML 326
Cdd:cd07078 149 A----GLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEnlKRVTLELGGKSPLIVFDDADLDAAV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 327 KNLAFTLSLYAGQMCTTTQAIIVPAGgidtdqgrkRFDEVAADLGAAVARF-----LSDESVATAVLGAIQSPATLARIE 401
Cdd:cd07078 225 KGAVFGAFGNAGQVCTAASRLLVHES---------IYDEFVERLVERVKALkvgnpLDPDTDMGPLISAAQLDRVLAYIE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 402 EAHGFGQVVLAS-KALThaEFPQAQVRTPVIVACDAADEAAyMEERFGPISFVVRAADTGAALQLSErivRERGALTVGL 480
Cdd:cd07078 296 DAKAEGAKLLCGgKRLE--GGKGYFVPPTVLTDVDPDMPIA-QEEIFGPVLPVIPFKDEEEAIELAN---DTEYGLAAGV 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2230046767 481 YSTRSAVIETMTEAtLRagvalslnlAGGVFVNQSAAFSDYH----GVGM 526
Cdd:cd07078 370 FTRDLERALRVAER-LE---------AGTVWINDYSVGAEPSapfgGVKQ 409
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
95-522 |
1.97e-48 |
|
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: 172.03 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 95 AAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQG-WMMAFQAGGAHAQDRGLEAVATAWdemsrvpae 173
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPiEEALGEVARAIDTFRYAAGLADKL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 174 avwEKPQGKNPPLRLRKHFEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVAIAREVlaeq 253
Cdd:cd06534 73 ---GGPELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 254 GLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHA--RQAQVYAELAGVNNVVIESTDNYKGMLKNLAF 331
Cdd:cd06534 146 GLPPGVVNVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAaeNLKPVTLELGGKSPVIVDEDADLDAAVEGAVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 332 TLSLYAGQMCTTTQAIIVPaggidtdqgrkrfdevaadlgaavarflsdESVATAVLGAIQspatlarieeahgfgqvvl 411
Cdd:cd06534 226 GAFFNAGQICTAASRLLVH------------------------------ESIYDEFVEKLV------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 412 askalthaefpqaqvrtPVIVACDAADEAAyMEERFGPISFVVRAADTGAALqlsERIVRERGALTVGLYSTRSAVIETM 491
Cdd:cd06534 257 -----------------TVLVDVDPDMPIA-QEEIFGPVLPVIRFKDEEEAI---ALANDTEYGLTAGVFTRDLNRALRV 315
|
410 420 430
....*....|....*....|....*....|.
gi 2230046767 492 TEAtLRagvalslnlAGGVFVNQSAAFSDYH 522
Cdd:cd06534 316 AER-LR---------AGTVYINDSSIGVGPE 336
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
90-522 |
1.39e-46 |
|
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: 169.92 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAfqagGAHAqDRGLEAVATAWDEMSR 169
Cdd:COG1012 46 DAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA----RGEV-DRAADFLRYYAGEARR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAVwekpqgknpPLRLRKHFEIVGR---GVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAisvAIA 246
Cdd:COG1012 121 LYGETI---------PSDAPGTRAYVRReplGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSAL---LLA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 247 rEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHA--RQAQVYAELAGVNNVVIESTDNYKG 324
Cdd:COG1012 189 -ELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAaeNLKRVTLELGGKNPAIVLDDADLDA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 325 MLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATLARIEE- 402
Cdd:COG1012 268 AVEAAVRGAFGNAGQRCTAASRLLVH---------ESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAy 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 403 -----AHGfGQVVLASKALTHAEfpqAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALqlseRIVRE-RGAL 476
Cdd:COG1012 339 iedavAEG-AELLTGGRRPDGEG---GYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI----ALANDtEYGL 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2230046767 477 TVGLYSTRSAVIETMTEAtLRagvalslnlAGGVFVNQSAAFSDYH 522
Cdd:COG1012 411 AASVFTRDLARARRVARR-LE---------AGMVWINDGTTGAVPQ 446
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
90-522 |
1.23e-25 |
|
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: 109.93 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWmmafqaggahaqdrgleavATAWDEMSR 169
Cdd:pfam00171 32 DAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL-------------------AEARGEVDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAVW-----EKPQGKNPPLRLRKHFEIVGR--GVALVIGcgtfpTWNtYPGLFA------ALATGNPVIVKPHENAi 236
Cdd:pfam00171 93 AIDVLRYyaglaRRLDGETLPSDPGRLAYTRREplGVVGAIT-----PWN-FPLLLPawkiapALAAGNTVVLKPSELT- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 237 lpAAISVAIArEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHA--RQAQVYAELAGVNNV 314
Cdd:pfam00171 166 --PLTALLLA-ELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAaqNLKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 315 VIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQS 393
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVH---------ESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 394 PATLARIEE------AHGfGQVVLASkaltHAEFPQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQL-- 465
Cdd:pfam00171 314 KAQLERVLKyvedakEEG-AKLLTGG----EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIan 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2230046767 466 -SErivrerGALTVGLYSTRSAVIETMTEAtLRagvalslnlAGGVFVNQSAAFSDYH 522
Cdd:pfam00171 389 dTE------YGLAAGVFTSDLERALRVARR-LE---------AGMVWINDYTTGDADG 430
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
219-483 |
7.14e-20 |
|
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: 92.22 E-value: 7.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 219 AALATGNPVIVKPHeNAILPAAISVA-IAREVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLD 297
Cdd:cd07129 130 SALAAGCPVVVKAH-PAHPGTSELVArAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 298 HARQAQ----VYAELAGVNNVVIES---TDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGgidtdQGRKRFDEVAAD- 369
Cdd:cd07129 209 AAAARPepipFYAELGSVNPVFILPgalAERGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAG-----PAGDAFIAALAEa 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 370 LGAAVARFLSDESVATAVLGAIqspatlARIEEAHGFGQVVLASKALTHAEfpqaqvRTPVIVACDAAD---EAAYMEER 446
Cdd:cd07129 284 LAAAPAQTMLTPGIAEAYRQGV------EALAAAPGVRVLAGGAAAEGGNQ------AAPTLFKVDAAAflaDPALQEEV 351
|
250 260 270
....*....|....*....|....*....|....*..
gi 2230046767 447 FGPISFVVRAADTGAALQLSERIvreRGALTVGLYST 483
Cdd:cd07129 352 FGPASLVVRYDDAAELLAVAEAL---EGQLTATIHGE 385
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
83-522 |
2.65e-18 |
|
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: 87.69 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 83 RYPVCAPDALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHavmmttgqgwMMAFQAGGAHAQDRGlEAVAT 162
Cdd:cd07097 33 RASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR----------LLTREEGKTLPEARG-EVTRA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 163 AwdEMSRVPAEAVWEKPQGKNPPLRLRKHFEIVGR--GVALVIGCGTFPT----WNTYPglfaALATGNPVIVKPHENAI 236
Cdd:cd07097 102 G--QIFRYYAGEALRLSGETLPSTRPGVEVETTREplGVVGLITPWNFPIaipaWKIAP----ALAYGNTVVFKPAELTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 237 LPAAISVaiarEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHA--RQAQVYAELAGVN-N 313
Cdd:cd07097 176 ASAWALV----EILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAaaRGARVQLEMGGKNpL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 314 VVIESTDnykgmlKNLAFTLSL-----YAGQMCTTTQAIIVPAGgiDTDQGRKRFDEVAADL--GAAVARF-----LSDE 381
Cdd:cd07097 252 VVLDDAD------LDLAVECAVqgaffSTGQRCTASSRLIVTEG--IHDRFVEALVERTKALkvGDALDEGvdigpVVSE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 382 SVATAVLGAIQspatLARIEEAhgfgQVVLASKALTHAEfpQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGA 461
Cdd:cd07097 324 RQLEKDLRYIE----IARSEGA----KLVYGGERLKRPD--EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2230046767 462 ALQLSERIvrERGaLTVGLYSTRSAVIETMTEATlRAGValslnlaggVFVNQSAAFSDYH 522
Cdd:cd07097 394 ALAIANDT--EFG-LSAGIVTTSLKHATHFKRRV-EAGV---------VMVNLPTAGVDYH 441
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
90-489 |
3.21e-18 |
|
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: 87.66 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAfqaggahaqdrgLEAVATAWDEMSR 169
Cdd:cd07124 72 EAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA------------DADVAEAIDFLEY 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAVWEKPQGKNPPLRLRKHFEIVGRGVALVIgcgtfPTWNtYP-----GL-FAALATGNPVIVKPHENAILPAAISV 243
Cdd:cd07124 140 YAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVI-----SPWN-FPlailaGMtTAALVTGNTVVLKPAEDTPVIAAKLV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 244 aiarEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQAQ--------VYAELAGVNNVV 315
Cdd:cd07124 214 ----EILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQpgqkwlkrVIAEMGGKNAII 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 316 IESTDNY----KGMLKNlAFTlslYAGQMCTTTQAIIVPAGgidtdqgrkRFDEVaadlgaaVARFLsdESVATAVLGAI 391
Cdd:cd07124 290 VDEDADLdeaaEGIVRS-AFG---FQGQKCSACSRVIVHES---------VYDEF-------LERLV--ERTKALKVGDP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 392 QSPAT--------------LARIEEAHGFGQVVLASKALTHAE---FPQaqvrtPVIVAcDAADEAAYM-EERFGPISFV 453
Cdd:cd07124 348 EDPEVymgpvidkgardriRRYIEIGKSEGRLLLGGEVLELAAegyFVQ-----PTIFA-DVPPDHRLAqEEIFGPVLAV 421
|
410 420 430
....*....|....*....|....*....|....*....
gi 2230046767 454 VRAADTGAALQL---SERivrergALTVGLYSTRSAVIE 489
Cdd:cd07124 422 IKAKDFDEALEIandTEY------GLTGGVFSRSPEHLE 454
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
90-450 |
5.06e-18 |
|
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: 87.02 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHavmmttgqgwMMAFQAGGAHAQDRGleAVATAWDEMSR 169
Cdd:cd07131 40 DAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR----------LVTREMGKPLAEGRG--DVQEAIDMAQY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAvwEKPQGKNPPLRLRKHFEIVGR---GVALVIGCGTFP----TWNtypgLFAALATGNPVIVKPHENAilpAAIS 242
Cdd:cd07131 108 AAGEG--RRLFGETVPSELPNKDAMTRRqpiGVVALITPWNFPvaipSWK----IFPALVCGNTVVFKPAEDT---PACA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 243 VAIArEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHA--RQAQVYAELAGVNNVVIESTD 320
Cdd:cd07131 179 LKLV-ELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCarPNKRVALEMGGKNPIIVMDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 321 NYkgmlkNLAFTLSLY-----AGQMCTTTQAIIVpaggidtdqGRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSP 394
Cdd:cd07131 258 DL-----DLALEGALWsafgtTGQRCTATSRLIV---------HESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINE 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2230046767 395 ATLARIEEAHGFGQ-----VVLASKALTHAEFPQAQVRTPVIVACDAADEAAYMEERFGPI 450
Cdd:cd07131 324 AQLEKVLNYNEIGKeegatLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPV 384
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
93-465 |
1.89e-17 |
|
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: 85.07 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 93 IGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAvmmttgqgwmMAFQAGGAHAQdRGLEAVATAwdEMSRVPA 172
Cdd:cd07150 27 IAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDL----------LIDEGGSTYGK-AWFETTFTP--ELLRAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 173 EAVwEKPQGKNPPLRLRKHFEIVGR---GVALVIGcgtfpTWNtYPGLFA------ALATGNPVIVKPHEnaiLPAAISV 243
Cdd:cd07150 94 GEC-RRVRGETLPSDSPGTVSMSVRrplGVVAGIT-----PFN-YPLILAtkkvafALAAGNTVVLKPSE---ETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 244 AIArEVLAEQGLDP---NLVTL--AVVDDpaatrHLATHRAVKSIDFTGSTAFGNWLLDHARQA--QVYAELAGVNN-VV 315
Cdd:cd07150 164 KIA-EIMEEAGLPKgvfNVVTGggAEVGD-----ELVDDPRVRMVTFTGSTAVGREIAEKAGRHlkKITLELGGKNPlIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 316 IESTDNYKGMlKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARFLS-DESVATAVLGAIQSP 394
Cdd:cd07150 238 LADADLDYAV-RAAAFGAFMHQGQICMSASRIIVE---------EPVYDEFVKKFVARASKLKVgDPRDPDTVIGPLISP 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230046767 395 ATLARIeeaHGFGQVVLASKA-LTHAEFPQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07150 308 RQVERI---KRQVEDAVAKGAkLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALEL 376
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
189-465 |
1.48e-16 |
|
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: 82.35 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 189 RKHFEIVGRGVALVigcgtfpTWNtYP------GLFAALATGNPVIVKPHENAILPAAISVAIAREVLAEQGLDPNLVTL 262
Cdd:cd07098 115 RVEYEPLGVVGAIV-------SWN-YPfhnllgPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 263 aVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQA--QVYAELAGVNNVVI-ESTDnykgmLKNLAFTLS----L 335
Cdd:cd07098 187 -VTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESltPVVLELGGKDPAIVlDDAD-----LDQIASIIMrgtfQ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 336 YAGQMCTTTQAIIVpaggidtdqGRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATLARIEE----AHGFGQVV 410
Cdd:cd07098 261 SSGQNCIGIERVIV---------HEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEElvadAVEKGARL 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2230046767 411 LA-SKALTHAEFPQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07098 332 LAgGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEI 387
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
90-465 |
5.73e-16 |
|
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: 80.31 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTG-QGWMMAFQAGGAHAQDRGLEAVATAWDEMS 168
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGaTAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 169 rVPAEA------VWEKPQGK-------NPPLRLrkhfeiVGRGVAlvigcgtfptwntypglfAALATGNPVIVKPHENA 235
Cdd:cd07105 83 -IPSDKpgtlamVVKEPVGVvlgiapwNAPVIL------GTRAIA------------------YPLAAGNTVVLKASELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 236 ilPAAiSVAIAReVLAEQGLDP---NLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLldhARQA-----QVYAE 307
Cdd:cd07105 138 --PRT-HWLIGR-VFHEAGLPKgvlNVVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRII---AETAakhlkPVLLE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 308 LAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVpaggidtdqgrkrFDEVAADLGAAVARFLSDESVATAV 387
Cdd:cd07105 211 LGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIV-------------HESIADEFVEKLKAAAEKLFAGPVV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 388 LGAIQSPATLARIEE----AHGFGQVVLASKALthAEFPQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAAL 463
Cdd:cd07105 278 LGSLVSAAAADRVKElvddALSKGAKLVVGGLA--DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAV 355
|
..
gi 2230046767 464 QL 465
Cdd:cd07105 356 RI 357
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
90-499 |
2.67e-15 |
|
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: 78.78 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVgiclEILQRLNRRsFEIAHAVMMttgqgWMMAFQAG----GAHAQDRglEAV----- 160
Cdd:cd07125 72 DAALAIAAAAFAGWSATPVEERA----EILEKAADL-LEANRGELI-----ALAAAEAGktlaDADAEVR--EAIdfcry 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 161 -AtawDEMSRVPAEAVWEKPQGKNPPLRLRkhfeivGRGVALVIgcgtfPTWNtYP------GLFAALATGNPVIVKPHE 233
Cdd:cd07125 140 yA---AQARELFSDPELPGPTGELNGLELH------GRGVFVCI-----SPWN-FPlaiftgQIAAALAAGNTVIAKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 234 NAILPAAISVAIAREVlaeqGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTA----FGNWL-LDHARQAQVYAEL 308
Cdd:cd07125 205 QTPLIAARAVELLHEA----GVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTEtaklINRALaERDGPILPLIAET 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 309 AGVNNVVIESTDNYKGMLKNL---AFTlslYAGQMCTTTQAIIVPAggidtdqgrkrfdEVAADL-----GAAVARFLSD 380
Cdd:cd07125 281 GGKNAMIVDSTALPEQAVKDVvqsAFG---SAGQRCSALRLLYLQE-------------EIAERFiemlkGAMASLKVGD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 381 ESVATAVLGAIQSPATLARIEEAHGFGQVvlASKALTHAEFPQAQVR--TPVIVACDAADEaaYMEERFGPISFVVRAad 458
Cdd:cd07125 345 PWDLSTDVGPLIDKPAGKLLRAHTELMRG--EAWLIAPAPLDDGNGYfvAPGIIEIVGIFD--LTTEVFGPILHVIRF-- 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2230046767 459 tgAALQLSE--RIVRERG-ALTVGLYSTRSAVIETMTEAtLRAG 499
Cdd:cd07125 419 --KAEDLDEaiEDINATGyGLTLGIHSRDEREIEYWRER-VEAG 459
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
90-518 |
6.78e-15 |
|
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: 77.09 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAFQAggahaQDRGLEAVATAWDEMSR 169
Cdd:cd07094 24 EEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE-----VDRAIDTLRLAAEEAER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAV-WEKPQGKNPPLRLRKHFEIvgrGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVaiarE 248
Cdd:cd07094 99 IRGEEIpLDATQGSDNRLAWTIREPV---GVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELA----K 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 249 VLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQAQVYAELAGVNNVVIESTDNYKGMLKN 328
Cdd:cd07094 172 ILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 329 LAFTLSLYAGQMCTTTQAIIVPAggidtdqgrKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPA----TLARIEEA 403
Cdd:cd07094 252 LAKGGFYHAGQVCISVQRIYVHE---------ELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEaaerVERWVEEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 404 HGFGQVVLASKALTHAEFPqaqvrtPVIVACDAADEAAYMEERFGPISFVVRAADTgaalqlsERIVRERGALTVGLYst 483
Cdd:cd07094 323 VEAGARLLCGGERDGALFK------PTVLEDVPRDTKLSTEETFGPVVPIIRYDDF-------EEAIRIANSTDYGLQ-- 387
|
410 420 430
....*....|....*....|....*....|....*
gi 2230046767 484 rSAVIETMTEATLRAGVALSlnlAGGVFVNQSAAF 518
Cdd:cd07094 388 -AGIFTRDLNVAFKAAEKLE---VGGVMVNDSSAF 418
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
90-465 |
1.31e-14 |
|
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: 76.03 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGqGWMM--AFQAGGAHAQDRGLEAVATawdem 167
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESG-STRPkaAFEVGAAIAILREAAGLPR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 168 srvpaeavweKPQGKNPPLRLRKHFEIVGR---GVALVIGcgtfPtWNtYPGLFA------ALATGNPVIVKPHENAilP 238
Cdd:cd07104 77 ----------RPEGEILPSDVPGKESMVRRvplGVVGVIS----P-FN-FPLILAmrsvapALALGNAVVLKPDSRT--P 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 239 AAISVAIAReVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLldhARQA-----QVYAELAGvNN 313
Cdd:cd07104 139 VTGGLLIAE-IFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHI---GELAgrhlkKVALELGG-NN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 314 --VVIESTDNYKGMlKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVATAVLGA 390
Cdd:cd07104 214 plIVLDDADLDLAV-SAAAFGAFLHQGQICMAAGRILVH---------ESVYDEFVEKLVAKAKALpVGDPRDPDTVIGP 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230046767 391 IQSPATLAR----IEEAHGFGQVVLASKalTHaefpQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07104 284 LINERQVDRvhaiVEDAVAAGARLLTGG--TY----EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVEL 356
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
73-518 |
1.60e-14 |
|
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: 75.74 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 73 RSPYGVALDVRYPVCAPDAL---IGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMttgqgwmmafQAGG 149
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIeeaIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVL----------EAGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 150 AHAQDRGleAVATAWDEMsRVPAEAVwEKPQGKNPPL----RLRKHFEIVGR---GVALVIGCGTFPTwntypGLFA--- 219
Cdd:cd07147 74 PIKDARG--EVARAIDTF-RIAAEEA-TRIYGEVLPLdisaRGEGRQGLVRRfpiGPVSAITPFNFPL-----NLVAhkv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 220 --ALATGNPVIVKPHENAILPAAIsvaIArEVLAEQGLDPNLVTLAVVDDPAATRhLATHRAVKSIDFTGSTAFGNWLLD 297
Cdd:cd07147 145 apAIAAGCPFVLKPASRTPLSALI---LG-EVLAETGLPKGAFSVLPCSRDDADL-LVTDERIKLLSFTGSPAVGWDLKA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 298 HARQAQVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF 377
Cdd:cd07147 220 RAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVH---------RSVYDEFKSRLVARVKAL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 378 LS-DESVATAVLGAIQSPATLARIE----EAhgfgqVVLASKALTHAEFPQAqVRTPVIVACDAADEAAYMEERFGPISF 452
Cdd:cd07147 291 KTgDPKDDATDVGPMISESEAERVEgwvnEA-----VDAGAKLLTGGKRDGA-LLEPTILEDVPPDMEVNCEEVFGPVVT 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2230046767 453 VVRAADTGAALQlseRIVRERGALTVGLYsTRSAvietmtEATLRAGVALSlnlAGGVFVNQSAAF 518
Cdd:cd07147 365 VEPYDDFDEALA---AVNDSKFGLQAGVF-TRDL------EKALRAWDELE---VGGVVINDVPTF 417
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
90-453 |
1.84e-14 |
|
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: 75.68 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAV------MMTTGQG-----WMMAFQAGGahaQDRGLE 158
Cdd:cd07086 38 EAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVslemgkILPEGLGevqemIDICDYAVG---LSRMLY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 159 AVATAwdemSRVPAEAVWEKPQgknpPLrlrkhfeivgrGVALVIGCGTFPT----WNtypgLFAALATGNPVIVKPHEN 234
Cdd:cd07086 115 GLTIP----SERPGHRLMEQWN----PL-----------GVVGVITAFNFPVavpgWN----AAIALVCGNTVVWKPSET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 235 AILPAAISVAIAREVLAEQGLDPNLVTLaVVDDPAATRHLATHRAVKSIDFTGSTAFGNWL--LDHARQAQVYAELAGvN 312
Cdd:cd07086 172 TPLTAIAVTKILAEVLEKNGLPPGVVNL-VTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVgeTVARRFGRVLLELGG-N 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 313 N--VVIESTDnykgmlKNLAFTLSLY-----AGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARFLSDESVAT 385
Cdd:cd07086 250 NaiIVMDDAD------LDLAVRAVLFaavgtAGQRCTTTRRLIVH---------ESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2230046767 386 AVL-GAIQSPATLARIEEA------HGfGQVVLASKALTHAEfpQAQVRTPVIVACDAADEAAYMEERFGPISFV 453
Cdd:cd07086 315 GTLvGPLINQAAVEKYLNAieiaksQG-GTVLTGGKRIDGGE--PGNYVEPTIVTGVTDDARIVQEETFAPILYV 386
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
90-500 |
1.93e-14 |
|
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: 75.39 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQG-WMMAFQAGGAHAQdrgLEAVATAWDEms 168
Cdd:cd07095 3 DAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPlWEAQTEVAAMAGK---IDISIKAYHE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 169 RVPAEAVwEKPQGKNPpLRLRKHfeivgrGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVaiarE 248
Cdd:cd07095 78 RTGERAT-PMAQGRAV-LRHRPH------GVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMV----E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 249 VLAEQGLDPNLVTLaVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLldharqAQVYA---------ELAGVNNVVIEST 319
Cdd:cd07095 146 LWEEAGLPPGVLNL-VQGGRETGEALAAHEGIDGLLFTGSAATGLLL------HRQFAgrpgkilalEMGGNNPLVVWDV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 320 DNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaGGIDTDQGRKRFDEVAADLgaAVARFLSDEsvatAVLGAIQSPATLAR 399
Cdd:cd07095 219 ADIDAAAYLIVQSAFLTAGQRCTCARRLIVP-DGAVGDAFLERLVEAAKRL--RIGAPDAEP----PFMGPLIIAAAAAR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 400 IEEAhGFGQVVLASKALTHAEFPQAQ--VRTPVIVACDAADEAAyMEERFGPISFVVRAADTGAALQLSErivRERGALT 477
Cdd:cd07095 292 YLLA-QQDLLALGGEPLLAMERLVAGtaFLSPGIIDVTDAADVP-DEEIFGPLLQVYRYDDFDEAIALAN---ATRFGLS 366
|
410 420
....*....|....*....|...
gi 2230046767 478 VGLYSTRSAVIETMTeATLRAGV 500
Cdd:cd07095 367 AGLLSDDEALFERFL-ARIRAGI 388
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
198-515 |
8.10e-14 |
|
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: 73.33 E-value: 8.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGcgtfpTWNtYP------GLFAALATGNPVIVKPHENAilpAAISVAIAREVlaEQGLDPNLVtlAVVD-DPAA 270
Cdd:cd07087 102 GVVLIIG-----PWN-YPlqlalaPLIGAIAAGNTVVLKPSELA---PATSALLAKLI--PKYFDPEAV--AVVEgGVEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 271 TRHLATHRaVKSIDFTGSTAFGNWLLDHArqAQ----VYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQA 346
Cdd:cd07087 169 ATALLAEP-FDHIFFTGSPAVGKIVMEAA--AKhltpVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 347 IIVPaggidtdqgRKRFDEVAADLGAAVARFLSDESVATAVLGAIQSPATLARIEE-------AHGfGQVVLASKALtha 419
Cdd:cd07087 246 VLVH---------ESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASllddgkvVIG-GQVDKEERYI--- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 420 efpqaqvrTPVIVAcDAADEAAYM-EERFGPISFVVRAADTGAALQlserIVRERG-ALTVGLYSTRSAVIETMTEATlr 497
Cdd:cd07087 313 --------APTILD-DVSPDSPLMqEEIFGPILPILTYDDLDEAIE----FINSRPkPLALYLFSEDKAVQERVLAET-- 377
|
330
....*....|....*...
gi 2230046767 498 agvalSlnlAGGVFVNQS 515
Cdd:cd07087 378 -----S---SGGVCVNDV 387
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
73-516 |
1.06e-13 |
|
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: 73.18 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 73 RSPYGVALDVrypvcapDALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGwmMAFQAGGAHA 152
Cdd:cd07107 12 RVPAASAADV-------DRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNP--VSAMLGDVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 153 QDRGLEAVATAWDEM--SRVPAEavwekpqGKNPPLRLRKHFEIVGRGVALvigcgtfptwnTYPGLFAA------LATG 224
Cdd:cd07107 83 AAALLDYFAGLVTELkgETIPVG-------GRNLHYTLREPYGVVARIVAF-----------NHPLMFAAakiaapLAAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 225 NPVIVKPHENAILPAAISVAIAREVLAeqgldPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQA-- 302
Cdd:cd07107 145 NTVVVKPPEQAPLSALRLAELAREVLP-----PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGik 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 303 QVYAELAGVNNVVI----ESTDNYKGMLKNLAFTlslYAGQMCTTTQAIIVpaggidtdqGRKRFDEVAADLGAAVARF- 377
Cdd:cd07107 220 HVTLELGGKNALIVfpdaDPEAAADAAVAGMNFT---WCGQSCGSTSRLFV---------HESIYDEVLARVVERVAAIk 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 378 LSDESVATAVLGAIQSPATLAR----IEEAHGFG-QVVLASKALTHAEFPQAQVRTPVIVACDAADEAAYMEERFGPISF 452
Cdd:cd07107 288 VGDPTDPATTMGPLVSRQQYDRvmhyIDSAKREGaRLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLS 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2230046767 453 VVRAADTGAAlqlseriVRERGALTVGLystrSAVIETMTEAT-LRAGVALSlnlAGGVFVNQSA 516
Cdd:cd07107 368 VLRWRDEAEM-------VAQANGVEYGL----TAAIWTNDISQaHRTARRVE---AGYVWINGSS 418
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
211-465 |
1.08e-13 |
|
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: 73.41 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 211 WNtYPGLFA------ALATGNPVIVKPHENAILpAAISVAiarEVLAEQGLdPNLVtLAVV--DDPAATRHLATHRAVKS 282
Cdd:cd07112 134 WN-FPLLMAawkiapALAAGNSVVLKPAEQSPL-TALRLA---ELALEAGL-PAGV-LNVVpgFGHTAGEALGLHMDVDA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 283 IDFTGSTAFGNWLLDHARQA---QVYAELAGVN-NVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdq 358
Cdd:cd07112 207 LAFTGSTEVGRRFLEYSGQSnlkRVWLECGGKSpNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVH-------- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 359 gRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATLAR----IEEAHGFGQVVLASKALTHAEFPQAQVRtPVIVA 433
Cdd:cd07112 279 -ESIKDEFLEKVVAAAREWkPGDPLDPATRMGALVSEAHFDKvlgyIESGKAEGARLVAGGKRVLTETGGFFVE-PTVFD 356
|
250 260 270
....*....|....*....|....*....|..
gi 2230046767 434 CDAADEAAYMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07112 357 GVTPDMRIAREEIFGPVLSVITFDSEEEAVAL 388
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
177-473 |
1.47e-13 |
|
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: 72.64 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 177 EKPQGKNPPLRLRK-HFEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAilPAAiSVAIARevLAEQGL 255
Cdd:cd07135 88 EKVKDGPLAFMFGKpRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELT--PHT-AALLAE--LVPKYL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 256 DPNLVtlAVVD-DPAATRHLATHRAVKsIDFTGSTAFGNWLldhARQAQ-----VYAELAGVNNVVIESTDNYKGMLKNL 329
Cdd:cd07135 163 DPDAF--QVVQgGVPETTALLEQKFDK-IFYTGSGRVGRII---AEAAAkhltpVTLELGGKSPVIVTKNADLELAAKRI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 330 AFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARFLSDESVATAVLGAIQSPATLARIEE--AHGFG 407
Cdd:cd07135 237 LWGKFGNAGQICVAPDYVLVD---------PSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSllDTTKG 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2230046767 408 QVVLASKALTHAEFPQaqvrtPVIVACDAADEAAYMEERFGPISFVVRAADTGAALqlseRIVRER 473
Cdd:cd07135 308 KVVIGGEMDEATRFIP-----PTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAI----KVINSR 364
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
90-465 |
2.71e-13 |
|
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: 71.97 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAFQaggahaqdrglEAVATAWDEMsR 169
Cdd:cd07092 22 DAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD-----------DELPGAVDNF-R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAVwEKPQGKNPPLRLRKHFEIVGR---GValvigCGTFPTWNtYPGLFA------ALATGNPVIVKPHENAILPAA 240
Cdd:cd07092 90 FFAGAA-RTLEGPAAGEYLPGHTSMIRRepiGV-----VAQIAPWN-YPLMMAawkiapALAAGNTVVLKPSETTPLTTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 241 ISVAIAREVLAeqgldPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNNVVIES 318
Cdd:cd07092 163 LLAELAAEVLP-----PGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADtlKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 319 TDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGgidtdqgrkRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATL 397
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHES---------VYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230046767 398 AR----IEEAHGFGQVVLASKAlthAEFPQAQVRTPVIVACDAADEAAyMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07092 309 ERvagfVERAPAHARVLTGGRR---AEGPGYFYEPTVVAGVAQDDEIV-QEEIFGPVVTVQPFDDEDEAIEL 376
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
198-515 |
7.96e-13 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 70.83 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHEnaiLPAAISVAIAREVLaeQGLDPNLVTLAVVDDPAATrHLATH 277
Cdd:PTZ00381 111 GVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSE---LSPHTSKLMAKLLT--KYLDPSYVRVIEGGVEVTT-ELLKE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 278 RaVKSIDFTGSTAFGNWLLDHARQAQVYA--ELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggid 355
Cdd:PTZ00381 185 P-FDHIFFTGSPRVGKLVMQAAAENLTPCtlELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH----- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 356 tdqgRKRFDEVAADLGAAVARFLSDESVATAVLGAIQSPATLARIEE---AHGfGQVVLASKALTHAEFPQaqvrtPVIV 432
Cdd:PTZ00381 259 ----RSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAElikDHG-GKVVYGGEVDIENKYVA-----PTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 433 ACDAADEAAYMEERFGPISFVVRAADTGAALQlserIVRER-GALTVGLYSTRSAVIETMTEATlragvalslnLAGGVF 511
Cdd:PTZ00381 329 VNPDLDSPLMQEEIFGPILPILTYENIDEVLE----FINSRpKPLALYYFGEDKRHKELVLENT----------SSGAVV 394
|
....
gi 2230046767 512 VNQS 515
Cdd:PTZ00381 395 INDC 398
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
73-518 |
1.35e-12 |
|
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: 69.93 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 73 RSPYGVALDVRYPVCAPDALIGAAEAAMPGWRKVG---AEGRVGICLEILQRLNRRSFEIAHAvmmttgqgwmMAFQAGG 149
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKslpAYERAEILERAAQLLEERREEFART----------IALEAGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 150 AHAQ-----DRGLEAVATAWDEMSR-----VPAEAVwekPQGKNpplrlRKHFEI-VGRGVALVIGCGTFPTwntypGLF 218
Cdd:cd07149 74 PIKDarkevDRAIETLRLSAEEAKRlagetIPFDAS---PGGEG-----RIGFTIrEPIGVVAAITPFNFPL-----NLV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 219 A-----ALATGNPVIVKPHENAILPAAISVaiarEVLAEQGLDPNLvtLAVVDDPAAT--RHLATHRAVKSIDFTGSTAF 291
Cdd:cd07149 141 AhkvgpAIAAGNAVVLKPASQTPLSALKLA----ELLLEAGLPKGA--LNVVTGSGETvgDALVTDPRVRMISFTGSPAV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 292 GNWLldhARQA---QVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVpaggidtdqGRKRFDEVAA 368
Cdd:cd07149 215 GEAI---ARKAglkKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFV---------HEDIYDEFLE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 369 DLGAAVARF-LSDESVATAVLGAIQSPATLARIE----EAHGFGQVVLASKAlthaefPQAQVRTPVIVACDAADEAAYM 443
Cdd:cd07149 283 RFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEewveEAVEGGARLLTGGK------RDGAILEPTVLTDVPPDMKVVC 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2230046767 444 EERFGPISFVVRAADTGAALQLSERIvreRGALTVGLYSTRSAVietmteaTLRAGVALSlnlAGGVFVNQSAAF 518
Cdd:cd07149 357 EEVFAPVVSLNPFDTLDEAIAMANDS---PYGLQAGVFTNDLQK-------ALKAARELE---VGGVMINDSSTF 418
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
83-450 |
1.57e-12 |
|
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: 69.48 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 83 RYPVCAP---DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHavMMTTGQG---WMMAFQAGGAHAQdrg 156
Cdd:cd07106 12 SAPVASEaqlDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELAR--LLTLEQGkplAEAQFEVGGAVAW--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 157 LEAVATAwdemsRVPAEAVWEkpqgkNPPLRLRKHFEIVGRGVALVigcgtfPtWNtYPGLFA------ALATGNPVIVK 230
Cdd:cd07106 87 LRYTASL-----DLPDEVIED-----DDTRRVELRRKPLGVVAAIV------P-WN-FPLLLAawkiapALLAGNTVVLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 231 PHENAILPAAISVAIAREVLAeqgldPNLVTlAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAEL 308
Cdd:cd07106 149 PSPFTPLCTLKLGELAQEVLP-----PGVLN-VVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKtlKRVTLEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 309 AGvNN--VVIESTDnYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVAT 385
Cdd:cd07106 223 GG-NDaaIVLPDVD-IDAVAPKLFWGAFINSGQVCAAIKRLYVH---------ESIYDEFCEALVALAKAAvVGDGLDPG 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230046767 386 AVLGAIQSPATLAR----IEEAHGFGQVVLASkalthAEFPQAQ---VRtPVIVAcDAADEAAYM-EERFGPI 450
Cdd:cd07106 292 TTLGPVQNKMQYDKvkelVEDAKAKGAKVLAG-----GEPLDGPgyfIP-PTIVD-DPPEGSRIVdEEQFGPV 357
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
212-518 |
2.14e-12 |
|
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: 69.30 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 212 NTYPGLFA-----ALATGNPVIVKPHENAILpAAISVAiarEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFT 286
Cdd:cd07145 134 NFPANLFAhkiapAIAVGNSVVVKPSSNTPL-TAIELA---KILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 287 GSTAFGNWLLDHA--RQAQVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFD 364
Cdd:cd07145 210 GSTAVGLLIASKAggTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVE---------EEVYD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 365 EVAADLGAAVARF-LSDESVATAVLGAIQSPATLARIEEahgfgqVVLAS-----KALTHAEFPQAQVRTPVIVACDAAD 438
Cdd:cd07145 281 KFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMEN------LVNDAvekggKILYGGKRDEGSFFPPTVLENDTPD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 439 EAAYMEERFGPISFVVRAADTGAALQLSERivrergaltvglystrsavietmTEATLRAGV-------ALSL--NL-AG 508
Cdd:cd07145 355 MIVMKEEVFGPVLPIAKVKDDEEAVEIANS-----------------------TEYGLQASVftndinrALKVarELeAG 411
|
330
....*....|
gi 2230046767 509 GVFVNQSAAF 518
Cdd:cd07145 412 GVVINDSTRF 421
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
176-524 |
3.47e-12 |
|
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: 68.41 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 176 WEKPQGKNPPLRL-----RKHFEivGRGVALVIGcgtfPtWNtYP------GLFAALATGNPVIVKPHENAILPAAISVA 244
Cdd:cd07134 77 WMKPKRVRTPLLLfgtksKIRYE--PKGVCLIIS----P-WN-YPfnlafgPLVSAIAAGNTAILKPSELTPHTSAVIAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 245 IAREVlaeqgLDPNLVTLAVVDDPAATRHLAthRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNNVVIESTDNY 322
Cdd:cd07134 149 IIREA-----FDEDEVAVFEGDAEVAQALLE--LPFDHIFFTGSPAVGKIVMAAAAKhlASVTLELGGKSPTIVDETADL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 323 KGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARFLSDEsvatavlGAIQSPATLARIEE 402
Cdd:cd07134 222 KKAAKKIAWGKFLNAGQTCIAPDYVFVH---------ESVKDAFVEHLKAEIEKFYGKD-------AARKASPDLARIVN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 403 AHGFGQVV-LASKALTH-AEF-----PQAQVRT--PVIVAcDAADEAAYM-EERFGPISFVVRAADTGAALQLseriVRE 472
Cdd:cd07134 286 DRHFDRLKgLLDDAVAKgAKVefggqFDAAQRYiaPTVLT-NVTPDMKIMqEEIFGPVLPIITYEDLDEVIEY----INA 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230046767 473 RGA-LTVGLYSTRSAVIETMTEATLRAGVALSLNLA---------GGvfVNQSAAFSdYHGV 524
Cdd:cd07134 361 KPKpLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhflnpnlpfGG--VNNSGIGS-YHGV 419
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
220-466 |
7.65e-12 |
|
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: 67.38 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 220 ALATGNPVIVKPHENAILpAAISVAiarEVLAEQGLDPNLVTLaVVDDPA-ATRHLATHRAVKSIDFTGSTAFGNWLLDH 298
Cdd:cd07146 144 AIAANNRIVLKPSEKTPL-SAIYLA---DLLYEAGLPPDMLSV-VTGEPGeIGDELITHPDVDLVTFTGGVAVGKAIAAT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 299 ARQAQVYAELAGvNN--VVIESTDnykgmlKNLAFTLSLY-----AGQMCTTTQAIIVPAGGIDtdqgrkRF-DEVAADL 370
Cdd:cd07146 219 AGYKRQLLELGG-NDplIVMDDAD------LERAATLAVAgsyanSGQRCTAVKRILVHESVAD------EFvDLLVEKS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 371 GAAVARFLSDEsvATAVLGAIQSPATL---ARIEEAHGFGqvvlaSKALTHAEFPQAQVRTPVIvacDAADEAAY--MEE 445
Cdd:cd07146 286 AALVVGDPMDP--ATDMGTVIDEEAAIqieNRVEEAIAQG-----ARVLLGNQRQGALYAPTVL---DHVPPDAElvTEE 355
|
250 260
....*....|....*....|.
gi 2230046767 446 RFGPISFVVRAADTGAALQLS 466
Cdd:cd07146 356 TFGPVAPVIRVKDLDEAIAIS 376
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
90-402 |
1.00e-11 |
|
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: 67.27 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGW-RKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAFqaggAHAQDRGLEAVATAWDEMS 168
Cdd:cd07089 22 DAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTAR----AMQVDGPIGHLRYFADLAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 169 RVPAE-AVWEKPQGKNPPLRLRKHfEIVGrgvalVIGCGT---FPTWNTYPGLFAALATGNPVIVKPHENAILPAAisvA 244
Cdd:cd07089 98 SFPWEfDLPVPALRGGPGRRVVRR-EPVG-----VVAAITpwnFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSAL---L 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 245 IArEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGVN-NVVIESTDN 321
Cdd:cd07089 169 LG-EIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAtlKRVLLELGGKSaNIVLDDADL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 322 YKGMLkNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATLARI 400
Cdd:cd07089 248 AAAAP-AAVGVCMHNAGQGCALTTRLLVP---------RSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRV 317
|
..
gi 2230046767 401 EE 402
Cdd:cd07089 318 EG 319
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
90-402 |
1.44e-11 |
|
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: 66.83 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPG--WRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQ--GWMMAFQAGGAHAQDRGLEAVAtawd 165
Cdd:cd07139 39 DAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENGMpiSWSRRAQGPGPAALLRYYAALA---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 166 emsrvpAEAVWEKPQGKNPPLRLRKHFEIVGRGVALVigcgtfpTWNTYPGLFA-----ALATGNPVIVKPHENAILPAA 240
Cdd:cd07139 115 ------RDFPFEERRPGSGGGHVLVRREPVGVVAAIV-------PWNAPLFLAAlkiapALAAGCTVVLKPSPETPLDAY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 241 IsvaIArEVLAEQGLDPNLVTLaVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHA--RQAQVYAELAGVN-NVVIE 317
Cdd:cd07139 182 L---LA-EAAEEAGLPPGVVNV-VPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCgeRLARVTLELGGKSaAIVLD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 318 STDNYKgMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPAT 396
Cdd:cd07139 257 DADLDA-AVPGLVPASLMNNGQVCVALTRILVP---------RSRYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQ 326
|
....*.
gi 2230046767 397 LARIEE 402
Cdd:cd07139 327 RERVEG 332
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
95-466 |
1.89e-11 |
|
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: 66.17 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 95 AAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMA-FQAGGAHAQDRglEAV-----ATAWDEMS 168
Cdd:cd07151 40 AAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKAnIEWGAAMAITR--EAAtfplrMEGRILPS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 169 RVPAEA--VWEKPQGknpplrlrkhfeIVGrgvalVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAilPAAISVAIA 246
Cdd:cd07151 118 DVPGKEnrVYREPLG------------VVG-----VISPWNFPLHLSMRSVAPALALGNAVVLKPASDT--PITGGLLLA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 247 ReVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLldhARQA-----QVYAELAGvNN--VVIEST 319
Cdd:cd07151 179 K-IFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHI---GELAgrhlkKVALELGG-NNpfVVLEDA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 320 DNYKGmLKNLAFTLSLYAGQMCTTTQAIIVPAGGIdtDQGRKRFDEVAADLGAAvarflsDESVATAVLGAI----QSPA 395
Cdd:cd07151 254 DIDAA-VNAAVFGKFLHQGQICMAINRIIVHEDVY--DEFVEKFVERVKALPYG------DPSDPDTVVGPLinesQVDG 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2230046767 396 TLARIEEAHGFGQVVLASKAlthaefPQAQVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQLS 466
Cdd:cd07151 325 LLDKIEQAVEEGATLLVGGE------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
90-449 |
2.53e-11 |
|
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: 65.66 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQgwmmAFQAGGAHAQDRGLEAVATAWDEMSR 169
Cdd:cd07093 22 DAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGK----PITLARTRDIPRAAANFRFFADYILQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAVWEKPQGKNPPLRLRKhfeivgrGVALVIGCGTFP----TWNTYPglfaALATGNPVIVKPHENAILPAAISVai 245
Cdd:cd07093 98 LDGESYPQDGGALNYVLRQPV-------GVAGLITPWNLPlmllTWKIAP----ALAFGNTVVLKPSEWTPLTAWLLA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 246 arEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLdhaRQA-----QVYAELAGVN-NVVIEST 319
Cdd:cd07093 165 --ELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIM---RAAapnlkPVSLELGGKNpNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 320 DnYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATLA 398
Cdd:cd07093 240 D-LDRAVDAAVRSSFSNNGEVCLAGSRILVQ---------RSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2230046767 399 RIE------EAHGfGQVVLASKALTHAEFPQAQVRTPVIVAcDAADEAAYM-EERFGP 449
Cdd:cd07093 310 KVLgyvelaRAEG-ATILTGGGRPELPDLEGGYFVEPTVIT-GLDNDSRVAqEEIFGP 365
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
219-455 |
3.49e-11 |
|
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: 65.26 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 219 AALATGNPVIVKPHENAilpAAISVAIARevLAEQ-GLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLD 297
Cdd:cd07114 142 PALAAGNTVVLKPSEHT---PASTLELAK--LAEEaGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIAR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 298 HA--RQAQVYAELAGVN-NVVIESTDnYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAgGIdtdqgrkrFDEVAADLGAAV 374
Cdd:cd07114 217 AAaeNLAPVTLELGGKSpNIVFDDAD-LDAAVNGVVAGIFAAAGQTCVAGSRLLVQR-SI--------YDEFVERLVARA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 375 ARF-LSDESVATAVLGAIQSPATLARIEE------AHGfGQVVLASKALTHAEFPQAQVRTPVIVACDAADEAAYMEERF 447
Cdd:cd07114 287 RAIrVGDPLDPETQMGPLATERQLEKVERyvararEEG-ARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVF 365
|
....*...
gi 2230046767 448 GPISFVVR 455
Cdd:cd07114 366 GPVLSVIP 373
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
219-465 |
3.59e-11 |
|
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: 65.54 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 219 AALATGNPVIVKPHENAILpAAISVAiarEVLAEQGLdPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLldh 298
Cdd:cd07113 165 AALATGCTIVIKPSEFTPL-TLLRVA---ELAKEAGI-PDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKI--- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 299 ARQA-----QVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAA 373
Cdd:cd07113 237 GRQAasdltRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVH---------RSKFDELVTKLKQA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 374 VARF--------------LSDESVATAVLGAIQspatLARIEEahgfGQVVLASKALTHAEFPQAqvrtPVIVACDAADE 439
Cdd:cd07113 308 LSSFqvgspmdesvmfgpLANQPHFDKVCSYLD----DARAEG----DEIVRGGEALAGEGYFVQ----PTLVLARSADS 375
|
250 260
....*....|....*....|....*.
gi 2230046767 440 AAYMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07113 376 RLMREETFGPVVSFVPYEDEEELIQL 401
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
90-466 |
4.32e-11 |
|
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: 65.15 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAhavmmttgqgWMMAFQAGGAHAQDRGLEAVATAwdemSR 169
Cdd:cd07115 22 DAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELA----------RLESLDTGKPIRAARRLDVPRAA----DT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAVW-EKPQGKNPPLRLRKHFEIVGRGVALVigcGTFPTWNtYPGLFA------ALATGNPVIVKPHENAILPAais 242
Cdd:cd07115 88 FRYYAGWaDKIEGEVIPVRGPFLNYTVREPVGVV---GAIVPWN-FPLMFAawkvapALAAGNTVVLKPAELTPLSA--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 243 VAIArEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNNVVIESTD 320
Cdd:cd07115 161 LRIA-ELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGnlKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 321 NYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATLAR 399
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVH---------ESIYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDR 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230046767 400 IEEAHGFGQVVLASkALTHAEFPQAQ--VRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQLS 466
Cdd:cd07115 311 VLDYVDVGREEGAR-LLTGGKRPGARgfFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIA 378
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
217-450 |
4.48e-11 |
|
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: 65.06 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 217 LFAALATGNPVIVKPhenAILPAAISVAIAREVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLL 296
Cdd:cd07120 138 LAPALAAGCTVVVKP---AGQTAQINAAIIRILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIM 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 297 DHA--RQAQVYAELAGVN-NVVIESTDnYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGgidtdqgrkRFDEVAADLGAA 373
Cdd:cd07120 215 AAAapTLKRLGLELGGKTpCIVFDDAD-LDAALPKLERALTIFAGQFCMAGSRVLVQRS---------IADEVRDRLAAR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 374 VARF-LSDESVATAVLGAIQSPATLAR----IEEAHGFG-QVVLASKALTHAEFPQAQVRtPVIVACDAADEAAYMEERF 447
Cdd:cd07120 285 LAAVkVGPGLDPASDMGPLIDRANVDRvdrmVERAIAAGaEVVLRGGPVTEGLAKGAFLR-PTLLEVDDPDADIVQEEIF 363
|
...
gi 2230046767 448 GPI 450
Cdd:cd07120 364 GPV 366
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
90-489 |
1.10e-10 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 64.19 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAhAVMM-TTGQGWMMAfQAGGAHAQDRgLEAVATawdEMS 168
Cdd:PRK03137 76 EKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS-AWLVkEAGKPWAEA-DADTAEAIDF-LEYYAR---QML 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 169 RV-PAEAVWEKPQGKNpplrlRKHFEIVGRGValVIgcgtfPTWNtYP------GLFAALATGNPVIVKPHENAILPAAI 241
Cdd:PRK03137 150 KLaDGKPVESRPGEHN-----RYFYIPLGVGV--VI-----SPWN-FPfaimagMTLAAIVAGNTVLLKPASDTPVIAAK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 242 SVaiarEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQAQ--------VYAELAGVNN 313
Cdd:PRK03137 217 FV----EVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQpgqiwlkrVIAEMGGKDA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 314 VVIESTDNYKGMLKNLAFTLSLYAGQMCTT-TQAIIVpaggidtdqgRKRFDEVaadLGAAVARFLS-------DESVAT 385
Cdd:PRK03137 293 IVVDEDADLDLAAESIVASAFGFSGQKCSAcSRAIVH----------EDVYDEV---LEKVVELTKEltvgnpeDNAYMG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 386 AVLGAIQSPATLARIEEAHGFGQVVLASKAL-THAEFPQaqvrtPVIVAcDAADEAAYM-EERFGPISFVVRAADTGAAL 463
Cdd:PRK03137 360 PVINQASFDKIMSYIEIGKEEGRLVLGGEGDdSKGYFIQ-----PTIFA-DVDPKARIMqEEIFGPVVAFIKAKDFDHAL 433
|
410 420
....*....|....*....|....*.
gi 2230046767 464 QLSERIvrERGaLTVGLYSTRSAVIE 489
Cdd:PRK03137 434 EIANNT--EYG-LTGAVISNNREHLE 456
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
90-465 |
1.16e-10 |
|
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: 63.69 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVmmTTGQGWMMAFQAGGAHaqdRGLEAVatawdEMsr 169
Cdd:cd07085 41 DAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLI--TLEHGKTLADARGDVL---RGLEVV-----EF-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 vpAEAVwekpqgknPPLRLRKHFEIVGRGVAL--------VIGCGT---FPT----WnTYPglfAALATGNPVIVKPHEN 234
Cdd:cd07085 109 --ACSI--------PHLLKGEYLENVARGIDTysyrqplgVVAGITpfnFPAmiplW-MFP---MAIACGNTFVLKPSER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 235 AILPAAIsvaIArEVLAEQGLDPNLVTLaVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQA--QVYAELAGVN 312
Cdd:cd07085 175 VPGAAMR---LA-ELLQEAGLPDGVLNV-VHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANgkRVQALGGAKN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 313 NVVI------ESTDNykgmlknlAFTLSLY--AGQMCTTTqAIIVPAGGIdTDQGRKRFDEVAADL--GAAvarflsdeS 382
Cdd:cd07085 250 HAVVmpdadlEQTAN--------ALVGAAFgaAGQRCMAL-SVAVAVGDE-ADEWIPKLVERAKKLkvGAG--------D 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 383 VATAVLGAIQSPATLARIE------EAHGfGQVVLASKALTHAEFPQAQVRTPVIVACDAADEAAYMEERFGPISFVVRA 456
Cdd:cd07085 312 DPGADMGPVISPAAKERIEgliesgVEEG-AKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRV 390
|
....*....
gi 2230046767 457 ADTGAALQL 465
Cdd:cd07085 391 DTLDEAIAI 399
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
90-465 |
1.37e-10 |
|
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: 63.52 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQ-----GWMM-------AFQAGGAHAQDRGL 157
Cdd:cd07110 22 DAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKpldeaAWDVddvagcfEYYADLAEQLDAKA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 158 EAVATAwdEMSRVPAEAVWEkpqgknpPLrlrkhfeivgrGVALVIGCGTFP----TWNTYPglfaALATGNPVIVKPHE 233
Cdd:cd07110 102 ERAVPL--PSEDFKARVRRE-------PV-----------GVVGLITPWNFPllmaAWKVAP----ALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 234 NAILPAAISVAIAREVlaeqGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGV 311
Cdd:cd07110 158 LTSLTELELAEIAAEA----GLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQdiKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 312 NNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARF-LSDESVATAVLGA 390
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVH---------ESIADAFLERLATAAEAIrVGDPLEEGVRLGP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 391 IQSPATLARIEEahgFGQVVLASKA--LTHAEFPQAQVR----TPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQ 464
Cdd:cd07110 305 LVSQAQYEKVLS---FIARGKEEGArlLCGGRRPAHLEKgyfiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIA 381
|
.
gi 2230046767 465 L 465
Cdd:cd07110 382 L 382
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
74-292 |
1.39e-10 |
|
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: 63.42 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 74 SPYGVALDVRYPVCAPDAL---IGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAvmMTtgqgWMMafqaGGA 150
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVraaLERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEE--LT----WQM----GRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 151 HAQDRG-LEAVATAWDEMSRVPAEAVWEKPQGKNPplRLRKHFEIVGRGVALVIgcgtfPTWNtYP------GLFAALAT 223
Cdd:cd07102 72 IAQAGGeIRGMLERARYMISIAEEALADIRVPEKD--GFERYIRREPLGVVLII-----APWN-YPyltavnAVIPALLA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230046767 224 GNPVIVKPHENAILPAAisvAIAReVLAEQGLDPNLVTLAVVDDPAATRHLATHRaVKSIDFTGSTAFG 292
Cdd:cd07102 144 GNAVILKHSPQTPLCGE---RFAA-AFAEAGLPEGVFQVLHLSHETSAALIADPR-IDHVSFTGSVAGG 207
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
220-450 |
1.65e-10 |
|
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: 63.21 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 220 ALATGNPVIVKPHENAILPAAISVAIarevLAEQGLDPNLVTLAVVDDPAATRHLATHRaVKSIDFTGSTAFGnWLLDH- 298
Cdd:cd07148 148 AIAAGCPVIVKPALATPLSCLAFVDL----LHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVG-WMLRSk 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 299 -ARQAQVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAggidtdqgrKRFDEVAADLGAAVARF 377
Cdd:cd07148 222 lAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPA---------EIADDFAQRLAAAAEKL 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2230046767 378 -LSDESVATAVLGAIQSPATLARIEE-----AHGFGQVVLASKALTHAEFpqaqvrTPVIVACDAADEAAYMEERFGPI 450
Cdd:cd07148 293 vVGDPTDPDTEVGPLIRPREVDRVEEwvneaVAAGARLLCGGKRLSDTTY------APTVLLDPPRDAKVSTQEIFGPV 365
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
198-465 |
1.91e-10 |
|
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: 62.99 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFPT----WNTypglFAALATGNPVIVKPHENAILPAAISVAIAREVLAEQGLDPNLVTLaVVDDPAATRH 273
Cdd:cd07130 134 GVVGVITAFNFPVavwgWNA----AIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASL-VCGGADVGEA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 274 LATHRAVKSIDFTGSTAFGNW--LLDHARQAQVYAELAGvNNVVIESTD-NYKGMLKNLAFTLSLYAGQMCTTTQAIIVP 350
Cdd:cd07130 209 LVKDPRVPLVSFTGSTAVGRQvgQAVAARFGRSLLELGG-NNAIIVMEDaDLDLAVRAVLFAAVGTAGQRCTTTRRLIVH 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 351 aggidtdqgRKRFDEVAADLGAAVARFLSDESVATAVL-GAIQSPAT----LARIEEAHGF-GQVVLASKALTHAEFpqa 424
Cdd:cd07130 288 ---------ESIYDEVLERLKKAYKQVRIGDPLDDGTLvGPLHTKAAvdnyLAAIEEAKSQgGTVLFGGKVIDGPGN--- 355
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2230046767 425 qVRTPVIVACdAADEAAYMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07130 356 -YVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAIAW 394
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
90-500 |
3.25e-10 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 62.28 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQG-WMMAFQAGgahaqdrgleAVATAWDEMS 168
Cdd:PRK09457 40 DAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPlWEAATEVT----------AMINKIAISI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 169 RVPAEAVWEKPQ---GKNPPLRLRKHfeivgrGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVai 245
Cdd:PRK09457 110 QAYHERTGEKRSemaDGAAVLRHRPH------GVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTV-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 246 arEVLAEQGLDPNLVTLaVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLldHarqaQVYA---------ELAGVNNVVI 316
Cdd:PRK09457 182 --KLWQQAGLPAGVLNL-VQGGRETGKALAAHPDIDGLLFTGSANTGYLL--H----RQFAgqpekilalEMGGNNPLVI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 317 ESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGgIDTDQGRKRFDEVAADLgaAVARFLSDEsvaTAVLGAIQSPAT 396
Cdd:PRK09457 253 DEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQG-AQGDAFLARLVAVAKRL--TVGRWDAEP---QPFMGAVISEQA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 397 LARIEEAhgfgQVVLAS---KALTHAEFPQAQ--VRTPVIVACDAADEAAYmEERFGPISFVVRAADTGAALQLSERIvr 471
Cdd:PRK09457 327 AQGLVAA----QAQLLAlggKSLLEMTQLQAGtgLLTPGIIDVTGVAELPD-EEYFGPLLQVVRYDDFDEAIRLANNT-- 399
|
410 420
....*....|....*....|....*....
gi 2230046767 472 eRGALTVGLYSTRSAVIETMTeATLRAGV 500
Cdd:PRK09457 400 -RFGLSAGLLSDDREDYDQFL-LEIRAGI 426
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
205-465 |
4.28e-10 |
|
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: 61.94 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 205 CGTFPTWNtYPGLFA------ALATGNPVIVKPHENAILpAAISVAiarEVLAEQGLDPNLVTLAVVDDPAATRHLATHR 278
Cdd:cd07119 138 CGLITPWN-YPLLQAawklapALAAGNTVVIKPSEVTPL-TTIALF---ELIEEAGLPAGVVNLVTGSGATVGAELAESP 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 279 AVKSIDFTGSTAFGNWLLdhaRQA-----QVYAELAGVN-NVVIESTDnYKGMLKNLAFTLSLYAGQMCTTTQAIIVpag 352
Cdd:cd07119 213 DVDLVSFTGGTATGRSIM---RAAagnvkKVALELGGKNpNIVFADAD-FETAVDQALNGVFFNAGQVCSAGSRLLV--- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 353 gidTDQGRKRFDEVAADLGAAVArfLSDESVATAVLGAIQSPATLARIEEAHGFGQ-----VVLASKALTHAEFPQAQVR 427
Cdd:cd07119 286 ---EESIHDKFVAALAERAKKIK--LGNGLDADTEMGPLVSAEHREKVLSYIQLGKeegarLVCGGKRPTGDELAKGYFV 360
|
250 260 270
....*....|....*....|....*....|....*...
gi 2230046767 428 TPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07119 361 EPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
90-499 |
4.42e-10 |
|
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: 62.06 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHavMMTTGQGwmmafqagGAHAQDRGlEAVATA----W- 164
Cdd:cd07103 22 DAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLAR--LLTLEQG--------KPLAEARG-EVDYAAsfleWf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 165 -DEMSRVPAEAVwekpQGKNPPLRLRKHFEIVGrgvalVigCGTFPTWNtYPG------LFAALATGNPVIVKPHENAIL 237
Cdd:cd07103 91 aEEARRIYGRTI----PSPAPGKRILVIKQPVG-----V--VAAITPWN-FPAamitrkIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 238 PAaisVAIArEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLldhARQA-----QVYAELAGvn 312
Cdd:cd07103 159 SA---LALA-ELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLL---MAQAadtvkRVSLELGG-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 313 N---VVIESTD---------NYKgmLKNlaftlslyAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARFL-- 378
Cdd:cd07103 230 NapfIVFDDADldkavdgaiASK--FRN--------AGQTCVCANRIYVH---------ESIYDEFVEKLVERVKKLKvg 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 379 --SDESVAtavLGAIQSPATLARIEE------AHGfGQVVLASKALTHAEFPQAqvrtPVIVAcDAADEAAYM-EERFGP 449
Cdd:cd07103 291 ngLDEGTD---MGPLINERAVEKVEAlvedavAKG-AKVLTGGKRLGLGGYFYE----PTVLT-DVTDDMLIMnEETFGP 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2230046767 450 ISFVVRAADTgaalqlsERIVRERGALTVGL----YSTRSAVIETMTEAtLRAG 499
Cdd:cd07103 362 VAPIIPFDTE-------DEVIARANDTPYGLaayvFTRDLARAWRVAEA-LEAG 407
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
73-406 |
1.01e-09 |
|
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: 60.74 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 73 RSPYGVALDVrypvcapDALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQgwmmafqaggAHA 152
Cdd:cd07088 28 TVPAATAEDA-------DRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGK----------TLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 153 QDRGlEAVATA--WDEMSRVPAEAVWEKPQGKNPPLRLRKHFEIVGRGVALVigcgtfpTWNtYP-GLFA-----ALATG 224
Cdd:cd07088 91 LARV-EVEFTAdyIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGIL-------PWN-FPfFLIArklapALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 225 NPVIVKPHENAILPAaisVAIArEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQ--A 302
Cdd:cd07088 162 NTIVIKPSEETPLNA---LEFA-ELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAEniT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 303 QVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGGIDT--DQGRKRFDEV--------AADLGA 372
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEfmEKLVEKMKAVkvgdpfdaATDMGP 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 2230046767 373 AVARfLSDESVATAVLGAIQSPATLA----RIEEAHGF 406
Cdd:cd07088 318 LVNE-AALDKVEEMVERAVEAGATLLtggkRPEGEKGY 354
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
181-486 |
1.12e-09 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 60.87 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 181 GKNPPLRLRkHFEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPhenAILPAAISVAIAREVLAEQGLDPNlv 260
Cdd:PRK11903 134 GKDPAFQGQ-HVLVPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKP---ATATAWLTQRMVKDVVAAGILPAG-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 261 TLAVVDDPAATRhLATHRAVKSIDFTGSTAFGNWLLDH----ARQAQVYAELAGVNNVVI-----ESTDNYKGMLKNLAF 331
Cdd:PRK11903 208 ALSVVCGSSAGL-LDHLQPFDVVSFTGSAETAAVLRSHpavvQRSVRVNVEADSLNSALLgpdaaPGSEAFDLFVKEVVR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 332 TLSLYAGQMCTTTQAIIVPAGgidtdqgrkRFDEVAADLGAAVARFL----SDESVATAVL-GAIQSPATLARIEEAHGF 406
Cdd:PRK11903 287 EMTVKSGQKCTAIRRIFVPEA---------LYDAVAEALAARLAKTTvgnpRNDGVRMGPLvSRAQLAAVRAGLAALRAQ 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 407 GQVVL--ASKALTHAEFPQAQVRTPVIVACDAADEAAYMEER--FGPISFVVRAADTGAALQLSErivRERGALTVGLYS 482
Cdd:PRK11903 358 AEVLFdgGGFALVDADPAVAACVGPTLLGASDPDAATAVHDVevFGPVATLLPYRDAAHALALAR---RGQGSLVASVYS 434
|
....
gi 2230046767 483 TRSA 486
Cdd:PRK11903 435 DDAA 438
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
205-513 |
1.82e-09 |
|
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: 60.23 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 205 CGTFPTWNtYPGLF------AALATGNPVIVKPHENAILPAAISVAIAREVlaeqGLDPNLVTLAVVDDPAATRHLATHR 278
Cdd:cd07143 148 CGQIIPWN-FPLLMcawkiaPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVVSGYGRTCGNAISSHM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 279 AVKSIDFTGSTAFGNWLLDHARQA---QVYAELAGVN-NVVIESTDnYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGgi 354
Cdd:cd07143 223 DIDKVAFTGSTLVGRKVMEAAAKSnlkKVTLELGGKSpNIVFDDAD-LESAVVWTAYGIFFNHGQVCCAGSRIYVQEG-- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 355 DTDQGRKRFDEVAADL------------GAAVARfLSDESVATAVLGAIQSPATLARIEEAHGfgqvvlaskalTHAEFP 422
Cdd:cd07143 300 IYDKFVKRFKEKAKKLkvgdpfaedtfqGPQVSQ-IQYERIMSYIESGKAEGATVETGGKRHG-----------NEGYFI 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 423 QAQVRTPVivacdAADEAAYMEERFGPISFVVRAADTGAALqlserivrERGALTVglYSTRSAVIETMTEATLRAGVAL 502
Cdd:cd07143 368 EPTIFTDV-----TEDMKIVKEEIFGPVVAVIKFKTEEEAI--------KRANDST--YGLAAAVFTNNINNAIRVANAL 432
|
330
....*....|.
gi 2230046767 503 SlnlAGGVFVN 513
Cdd:cd07143 433 K---AGTVWVN 440
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
205-483 |
3.14e-09 |
|
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: 59.34 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 205 CGTFPTWNtYP------GLFAALATGNPVIVKPHENAILpaaiSVAIAREVLAEQGLDPNLVTLAVVDDPAATRHLATHR 278
Cdd:cd07144 148 CGQIIPWN-YPlamaawKLAPALAAGNTVVIKPAENTPL----SLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHP 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 279 AVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGgiDT 356
Cdd:cd07144 223 DVDKIAFTGSTATGRLVMKAAAQnlKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQES--IY 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 357 DQGRKRFDEVAADlGAAVARFLSDESVATAVLGAIQSPATLARIEEAHGFGQVVLASKALTHAEFPQAQVRTPVIVACDA 436
Cdd:cd07144 301 DKFVEKFVEHVKQ-NYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIFTDVP 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2230046767 437 ADEAAYMEERFGPI----SF------VVRAADT----GAA-----LQLSERIVRERGALTVGLYST 483
Cdd:cd07144 380 QDMRIVKEEIFGPVvvisKFktyeeaIKKANDTtyglAAAvftkdIRRAHRVARELEAGMVWINSS 445
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
198-466 |
7.87e-09 |
|
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: 57.97 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVaiarEVLAEQGLDP---NLVTL--AVVDDPaatr 272
Cdd:cd07082 143 GVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLA----EAFHDAGFPKgvvNVVTGrgREIGDP---- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 273 hLATHRAVKSIDFTGSTAFGNWLLDHARQAQVYAELAGVNNVVIESTDNYKGMLKN-LAFTLSlYAGQMCTTTQAIIVPa 351
Cdd:cd07082 215 -LVTHGRIDVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEiVKGALS-YSGQRCTAIKRVLVH- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 352 ggidtdqgRKRFDEVAADLGAAVARF--------------LSDESVATAVLGAIQSPatlarieEAHGfGQVVLASKALT 417
Cdd:cd07082 292 --------ESVADELVELLKEEVAKLkvgmpwdngvditpLIDPKSADFVEGLIDDA-------VAKG-ATVLNGGGREG 355
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2230046767 418 HAEFpqaqvrTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQLS 466
Cdd:cd07082 356 GNLI------YPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELA 398
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
93-465 |
1.35e-08 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 57.39 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 93 IGAAEAAMPGWRKVGAEGRVGICleilqrlnRRSFEIAHAVMMTTGQgwMMAFQAGGAHAQDRGLEAVATAW-----DEM 167
Cdd:PLN02278 68 IASAHDAFPSWSKLTASERSKIL--------RRWYDLIIANKEDLAQ--LMTLEQGKPLKEAIGEVAYGASFleyfaEEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 168 SRVPAEAVwekPqgknPPLRLRKHFeIVGRGVALvigCGTFPTWNtYP------GLFAALATGNPVIVKPHENAILpaai 241
Cdd:PLN02278 138 KRVYGDII---P----SPFPDRRLL-VLKQPVGV---VGAITPWN-FPlamitrKVGPALAAGCTVVVKPSELTPL---- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 242 sVAIAREVLAEQ-GLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQA--QVYAELAGVNNVVIES 318
Cdd:PLN02278 202 -TALAAAELALQaGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATvkRVSLELGGNAPFIVFD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 319 TDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGgidtdqgrkRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATL 397
Cdd:PLN02278 281 DADLDVAVKGALASKFRNSGQTCVCANRILVQEG---------IYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAV 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230046767 398 ARIE----EAHGFGQVVLASKaltHAEFPQAQVRTPVIVaCDAADEAAYM-EERFGPISFVVRAADTGAALQL 465
Cdd:PLN02278 352 QKVEshvqDAVSKGAKVLLGG---KRHSLGGTFYEPTVL-GDVTEDMLIFrEEVFGPVAPLTRFKTEEEAIAI 420
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
90-454 |
2.12e-08 |
|
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: 56.53 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGqgwmmAFQAGGAHAqdrgLEAVATAWDEMSR 169
Cdd:cd07152 16 DRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-----SIRPKAGFE----VGAAIGELHEAAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEavwekPQGK---NPPLRLrKHFEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAilPAAISVAIA 246
Cdd:cd07152 87 LPTQ-----PQGEilpSAPGRL-SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT--PVSGGVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 247 ReVLAEQGLDPNLVTLaVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNNVVIESTDNYKG 324
Cdd:cd07152 159 R-LFEEAGLPAGVLHV-LPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRhlKKVSLELGGKNALIVLDDADLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 325 MLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLgAAVARFLS--DESVATAVLGAIQSPATLARIE- 401
Cdd:cd07152 237 AASNGAWGAFLHQGQICMAAGRHLVH---------ESVADAYTAKL-AAKAKHLPvgDPATGQVALGPLINARQLDRVHa 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2230046767 402 ---EAHGFGQVVLASKalTHAE-FPQAQVRTPVivacdAADEAAYMEERFGPISFVV 454
Cdd:cd07152 307 ivdDSVAAGARLEAGG--TYDGlFYRPTVLSGV-----KPGMPAFDEEIFGPVAPVT 356
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
83-292 |
3.89e-08 |
|
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: 55.69 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 83 RYPVCAPDALIGA---AEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGWMMAfqaggAHAQDRGLEA 159
Cdd:cd07099 11 EVPVTDPAEVAAAvarARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA-----GLEVLLALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 160 VATAWDEMSRV-PAEAVWEKPQGKNPPLRLrkhfEIVGRGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILP 238
Cdd:cd07099 86 IDWAARNAPRVlAPRKVPTGLLMPNKKATV----EYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2230046767 239 AAISVAIAREVLAEQGLdpnlvtLAVVDDPAAT-RHLATHRaVKSIDFTGSTAFG 292
Cdd:cd07099 162 GELLAEAWAAAGPPQGV------LQVVTGDGATgAALIDAG-VDKVAFTGSVATG 209
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
197-465 |
6.30e-08 |
|
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: 55.04 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 197 RGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHEnaiLPAAISVAIArEVLAEQGLDPNLVTLAVVDDPAATRHLAT 276
Cdd:cd07118 120 IGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSE---FTSGTTLMLA-ELLIEAGLPAGVVNIVTGYGATVGQAMTE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 277 HRAVKSIDFTGSTAFGNWLLDHARQA--QVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggi 354
Cdd:cd07118 196 HPDVDMVSFTGSTRVGKAIAAAAARNlkKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVH---- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 355 dtdqgrkrfDEVAADLGAAVARFLSDESV-----ATAVLGAIQSPATLARI----EEAHGFG-QVVLASKALTHAefpQA 424
Cdd:cd07118 272 ---------ESIADAFVAAVVARSRKVRVgdpldPETKVGAIINEAQLAKItdyvDAGRAEGaTLLLGGERLASA---AG 339
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2230046767 425 QVRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07118 340 LFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIAL 380
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
198-341 |
7.64e-08 |
|
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: 54.82 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGcgtfPtWNtYP------GLFAALATGNPVIVKPHENAILPAAISVAIAREVlaeqgLDPNLVtlAVVD-DPAA 270
Cdd:cd07136 102 GVVLIIA----P-WN-YPfqlalaPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-----FDEEYV--AVVEgGVEE 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2230046767 271 TRHLaTHRAVKSIDFTGSTAFGNWLLDHArqAQ----VYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMC 341
Cdd:cd07136 169 NQEL-LDQKFDYIFFTGSVRVGKIVMEAA--AKhltpVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
211-465 |
2.53e-07 |
|
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: 53.39 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 211 WNtYP------GLFAALATGNPVIVKPHENAILPAaisVAIArEVLAEQGLDP---NLVTLAVVDDPAAtrhLATHRAVK 281
Cdd:cd07109 127 WN-YPlqitgrSVAPALAAGNAVVVKPAEDAPLTA---LRLA-ELAEEAGLPAgalNVVTGLGAEAGAA---LVAHPGVD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 282 SIDFTGSTAFGNWLLDHA--RQAQVYAELAGVN-NVVIESTDN-------YKGMLKNlaftlslyAGQMCTTTQAIIVPa 351
Cdd:cd07109 199 HISFTGSVETGIAVMRAAaeNVVPVTLELGGKSpQIVFADADLeaalpvvVNAIIQN--------AGQTCSAGSRLLVH- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 352 ggidtdqgRKRFDEVAADLGAAVARFLSDESVATAVLGAIQSPATLARIE----EAHGFGQVVLASKALTHAEFPQAQVR 427
Cdd:cd07109 270 --------RSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEgfvaRARARGARIVAGGRIAEGAPAGGYFV 341
|
250 260 270
....*....|....*....|....*....|....*....
gi 2230046767 428 TPVIV-ACDAADEAAyMEERFGPISFVVRAADTGAALQL 465
Cdd:cd07109 342 APTLLdDVPPDSRLA-QEEIFGPVLAVMPFDDEAEAIAL 379
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
93-466 |
1.11e-06 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 51.06 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 93 IGAAEAAMPGWRKVGAEGRVGICleilqrlnRRSFEiahavMMTTGQ---GWMMAFQAGGAHAQDRGLEAVATAWDEMSR 169
Cdd:PRK11241 54 IDAANRALPAWRALTAKERANIL--------RRWFN-----LMMEHQddlARLMTLEQGKPLAEAKGEISYAASFIEWFA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 170 VPAEAVW-EKPQGKNPPLRLrkhfeIVGR---GVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAaisVAI 245
Cdd:PRK11241 121 EEGKRIYgDTIPGHQADKRL-----IVIKqpiGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSA---LAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 246 ARevLAEQGLDPNLVtLAVVDDPAAT--RHLATHRAVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAG-VNNVVIESTD 320
Cdd:PRK11241 193 AE--LAIRAGIPAGV-FNVVTGSAGAvgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKdiKKVSLELGGnAPFIVFDDAD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 321 NYKGMLKNLAftlSLY--AGQMCTTTQAIIVPAGgidtdqgrkRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATL 397
Cdd:PRK11241 270 LDKAVEGALA---SKFrnAGQTCVCANRLYVQDG---------VYDRFAEKLQQAVSKLhIGDGLEKGVTIGPLIDEKAV 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230046767 398 ARIEEaHGFGQVVLASKALTHAEfPQAQVRT---PVIVACDAADEAAYMEERFGPISFVVRAADTGAALQLS 466
Cdd:PRK11241 338 AKVEE-HIADALEKGARVVCGGK-AHELGGNffqPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
211-466 |
1.74e-06 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 50.66 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 211 WNtYPGLFA------ALATGNPVIVKPHENAILPAAISVAIAREVlaeqGLDPNLVTLAVVDDPAATRHLATHRAVKSID 284
Cdd:PRK09847 167 WN-FPLLLTcwklgpALAAGNSVILKPSEKSPLSAIRLAGLAKEA----GLPDGVLNVVTGFGHEAGQALSRHNDIDAIA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 285 FTGSTAFGNWLLDHARQA---QVYAELAGVN-NVVIESTDNYKgmlknlaftlslyagqmctttQAIIVPAGGIDTDQGR 360
Cdd:PRK09847 242 FTGSTRTGKQLLKDAGDSnmkRVWLEAGGKSaNIVFADCPDLQ---------------------QAASATAAGIFYNQGQ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 361 krfdevaadLGAAVARFLSDESVATAVLGAIQS------------PATL-------ARIEEAHGF-------GQVVLASK 414
Cdd:PRK09847 301 ---------VCIAGTRLLLEESIADEFLALLKQqaqnwqpghpldPATTmgtlidcAHADSVHSFiregeskGQLLLDGR 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2230046767 415 ALTHAefpqAQVRTPVIVACDAADEAAyMEERFGPISFVVRAADTGAALQLS 466
Cdd:PRK09847 372 NAGLA----AAIGPTIFVDVDPNASLS-REEIFGPVLVVTRFTSEEQALQLA 418
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
198-526 |
3.04e-06 |
|
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: 49.91 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGcgtfpTWNtYP------GLFAALATGNPVIVKPHEnailpaaISVAIAReVLAE---QGLDPNL--VTLAVVD 266
Cdd:cd07132 102 GVVLIIG-----AWN-YPlqltlvPLVGAIAAGNCVVIKPSE-------VSPATAK-LLAElipKYLDKECypVVLGGVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 267 DpaaTRHLATHRaVKSIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCttt 344
Cdd:cd07132 168 E---TTELLKQR-FDYIFYTGSTSVGKIVMQAAAKhlTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 345 qaiIVPAGGIDTDQGRKRFDEvaaDLGAAVARFLSDESVATAVLGAIQSPATLARIEE-------AHGfGQVVLASKALt 417
Cdd:cd07132 241 ---IAPDYVLCTPEVQEKFVE---ALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKllsggkvAIG-GQTDEKERYI- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 418 haefpqaqvrTPVIVAcDAADEAAYM-EERFGPISFVVRAADTGAALQLSERivRERgALTVGLYSTRSAVIETMTEATl 496
Cdd:cd07132 313 ----------APTVLT-DVKPSDPVMqEEIFGPILPIVTVNNLDEAIEFINS--REK-PLALYVFSNNKKVINKILSNT- 377
|
330 340 350
....*....|....*....|....*....|....*
gi 2230046767 497 ragvalslnLAGGVFVNQSAAFSDYH-----GVGM 526
Cdd:cd07132 378 ---------SSGGVCVNDTIMHYTLDslpfgGVGN 403
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
198-350 |
4.22e-06 |
|
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: 49.33 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAilPAAiSVAIARevLAEQGLDPNLVTLaVVDDPAATRHLATH 277
Cdd:cd07137 103 GVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELA--PAT-SALLAK--LIPEYLDTKAIKV-IEGGVPETTALLEQ 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2230046767 278 RAVKsIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNNVVIESTDNYKGMLKNLAF-TLSLYAGQMCTTTQAIIVP 350
Cdd:cd07137 177 KWDK-IFFTGSPRVGRIIMAAAAKhlTPVTLELGGKCPVIVDSTVDLKVAVRRIAGgKWGCNNGQACIAPDYVLVE 251
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
211-349 |
4.39e-06 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 49.35 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 211 WNtYPGLFA------ALATGNPVIVKPHENAILPAAISVAIAREVlaeqGLDP---NLVTLAVVDDPAAtrhLATHRAVK 281
Cdd:PLN02467 161 WN-YPLLMAtwkvapALAAGCTAVLKPSELASVTCLELADICREV----GLPPgvlNVVTGLGTEAGAP---LASHPGVD 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2230046767 282 SIDFTGSTAFGNWLLDHARQ--AQVYAELAGVNN-VVIESTDNYKGMLKNLaFTLSLYAGQMCTTTQAIIV 349
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQmvKPVSLELGGKSPiIVFDDVDLDKAVEWAM-FGCFWTNGQICSATSRLLV 302
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
198-292 |
4.65e-06 |
|
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: 49.22 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFP----TWNTYPglfaALATGNPVIVKPHENAILPAaisVAIArEVLAEQGLDPNLVTlaVVDDPAAT-R 272
Cdd:cd07090 118 GVCAGIGAWNYPiqiaSWKSAP----ALACGNAMVYKPSPFTPLTA---LLLA-EILTEAGLPDGVFN--VVQGGGETgQ 187
|
90 100
....*....|....*....|
gi 2230046767 273 HLATHRAVKSIDFTGSTAFG 292
Cdd:cd07090 188 LLCEHPDVAKVSFTGSVPTG 207
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
211-450 |
6.43e-06 |
|
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: 48.64 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 211 WNtYP------GLFAALATGNPVIVKPHENAilPAaiSVAIAREVLAEQgLDPNLVtlAVVDDPAATRHLATHRAVKSID 284
Cdd:cd07133 111 WN-YPlylalgPLIAALAAGNRVMIKPSEFT--PR--TSALLAELLAEY-FDEDEV--AVVTGGADVAAAFSSLPFDHLL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 285 FTGSTAFGNwlldHARQAQ------VYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAGgidtdq 358
Cdd:cd07133 183 FTGSTAVGR----HVMRAAaenltpVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPED------ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 359 grkRFDEVAADLGAAVARFLSDeSVATAVLGAIQSPATLAR----IEEAHGFGQVVLaskALTHAEFPQAQVRT--PVIV 432
Cdd:cd07133 253 ---KLEEFVAAAKAAVAKMYPT-LADNPDYTSIINERHYARlqglLEDARAKGARVI---ELNPAGEDFAATRKlpPTLV 325
|
250
....*....|....*....
gi 2230046767 433 AcDAADEAAYM-EERFGPI 450
Cdd:cd07133 326 L-NVTDDMRVMqEEIFGPI 343
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
197-491 |
7.63e-06 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 48.42 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 197 RGVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPhenAILPAAISVAIAREVLaEQGLDP----NLVTLAVVD--Dpaa 270
Cdd:cd07128 145 RGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKP---ATATAYLTEAVVKDIV-ESGLLPegalQLICGSVGDllD--- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 271 trHLaTHRAVksIDFTGSTAFGNWLLDH----ARQAQVYAELAGVNNVVI-----ESTDNYKGMLKNLAFTLSLYAGQMC 341
Cdd:cd07128 218 --HL-GEQDV--VAFTGSAATAAKLRAHpnivARSIRFNAEADSLNAAILgpdatPGTPEFDLFVKEVAREMTVKAGQKC 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 342 TTTQAIIVPAGgidtdqgrkRFDEVAADLGAAVARF-LSDESVATAVLGAIQSPATLARIEEA-------------HGFG 407
Cdd:cd07128 293 TAIRRAFVPEA---------RVDAVIEALKARLAKVvVGDPRLEGVRMGPLVSREQREDVRAAvatllaeaevvfgGPDR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 408 QVVLASKALTHAEFPqaqvrtPVIVACDAADEAAYME--ERFGPISFVVRAADTGAALQLserIVRERGALTVGLYSTRS 485
Cdd:cd07128 364 FEVVGADAEKGAFFP------PTLLLCDDPDAATAVHdvEAFGPVATLMPYDSLAEAIEL---AARGRGSLVASVVTNDP 434
|
....*.
gi 2230046767 486 AVIETM 491
Cdd:cd07128 435 AFAREL 440
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
178-352 |
1.36e-05 |
|
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: 47.59 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 178 KPQGKNPPLRlRKHFEIVGR---GValvigCGTFPTWNtYPGLFA------ALATGNPVIVKPHENAILpAAISVAiarE 248
Cdd:cd07091 121 KIQGKTIPID-GNFLAYTRRepiGV-----CGQIIPWN-FPLLMLawklapALAAGNTVVLKPAEQTPL-SALYLA---E 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 249 VLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHARQA---QVYAELAGVNNVVIESTDNYKGM 325
Cdd:cd07091 190 LIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnlkKVTLELGGKSPNIVFDDADLDKA 269
|
170 180
....*....|....*....|....*..
gi 2230046767 326 LKNLAFTLSLYAGQMCTTTQAIIVPAG 352
Cdd:cd07091 270 VEWAAFGIFFNQGQCCCAGSRIFVQES 296
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
198-355 |
1.79e-05 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 47.51 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVAIAREVlaeqGLDPNLVTLAVVDDPAATRHLATH 277
Cdd:PLN02766 160 GVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLA----GVPDGVINVVTGFGPTAGAAIASH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 278 RAVKSIDFTGSTAFGNWLLDHARQA---QVYAELAGVNNVVIeSTDNYKGMLKNLAFTLSLY-AGQMCTTTQAIIVPAGG 353
Cdd:PLN02766 236 MDVDKVSFTGSTEVGRKIMQAAATSnlkQVSLELGGKSPLLI-FDDADVDMAVDLALLGIFYnKGEICVASSRVYVQEGI 314
|
..
gi 2230046767 354 ID 355
Cdd:PLN02766 315 YD 316
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
220-518 |
3.90e-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: 46.33 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 220 ALATGNPVIVKPHENAILPAAISVAIAREVLAEQGLDPNLVtlAVVDDP--AATRHLATHRAVKSIDFTGSTAfgnwLLD 297
Cdd:cd07122 119 ALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLI--QWIEEPsiELTQELMKHPDVDLILATGGPG----MVK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 298 HARQAQVYAELAGVNNV--VIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPAggidtdqgrKRFDEVAADLGAAVA 375
Cdd:cd07122 193 AAYSSGKPAIGVGPGNVpaYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDD---------EIYDEVRAELKRRGA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 376 RFLSDE--------------SVATAVLGaiQSPATLArieEAHGFgqvvlaskalthaEFPQAqvrTPVIVA--CDAADE 439
Cdd:cd07122 264 YFLNEEekeklekalfddggTLNPDIVG--KSAQKIA---ELAGI-------------EVPED---TKVLVAeeTGVGPE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 440 AAYMEERFGPISFVVRAADTGAALQLSERIVRERGA-LTVGLYSTRSAVIEtmteatlragvALSLNL-AGGVFVNQSAA 517
Cdd:cd07122 323 EPLSREKLSPVLAFYRAEDFEEALEKARELLEYGGAgHTAVIHSNDEEVIE-----------EFALRMpVSRILVNTPSS 391
|
.
gi 2230046767 518 F 518
Cdd:cd07122 392 L 392
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
198-341 |
6.33e-05 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 45.57 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFP----TWNTYPglfaALATGNPVIVKPHENAILPAAIsvaiAREVLAEQGLDPNLVTLAVVDDPAATRH 273
Cdd:PLN02466 197 GVAGQIIPWNFPllmfAWKVGP----ALACGNTIVLKTAEQTPLSALY----AAKLLHEAGLPPGVLNVVSGFGPTAGAA 268
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230046767 274 LATHRAVKSIDFTGSTAFGNWLLDHARQAQ---VYAELAGVNN-VVIESTDNYKGMlkNLA-FTLSLYAGQMC 341
Cdd:PLN02466 269 LASHMDVDKLAFTGSTDTGKIVLELAAKSNlkpVTLELGGKSPfIVCEDADVDKAV--ELAhFALFFNQGQCC 339
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
192-349 |
9.90e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 44.91 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 192 FEIVGRGVALVIGCGTFPTWNTYPGLFAAL---ATGNPVIVKPHENAILPAAISVAIAREVLAEQGLDPNLVTLAVVDDP 268
Cdd:cd07077 92 GETYVRAFPIGVTMHILPSTNPLSGITSALrgiATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLYVPHPSDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 269 AATRhLATHRAVKSIDFTGSTAFGNWLLDHARQAQVYAELAGVNNVVIESTDNYKGMLKnLAFTLSLYAGQMCTTTQAII 348
Cdd:cd07077 172 LAEE-LLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASG-SVHDSKFFDQNACASEQNLY 249
|
.
gi 2230046767 349 V 349
Cdd:cd07077 250 V 250
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
73-465 |
4.92e-04 |
|
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: 42.68 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 73 RSPYGVALDVRYPVCAP---DALIGAAEAAMPGWRKVGAEGRVGICLEILQRLNRRSFEIAHAVMMTTGQGwmmafqagG 149
Cdd:cd07101 1 EAPFTGEPLGELPQSTPadvEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKA--------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 150 AHAQDRGLEAVATAWDEMSRVPAEAVWEKPQGKNPPL-RLRKHFEIVGrgvalVIGCGTfpTWNtYP------GLFAALA 222
Cdd:cd07101 73 RHAFEEVLDVAIVARYYARRAERLLKPRRRRGAIPVLtRTTVNRRPKG-----VVGVIS--PWN-YPltlavsDAIPALL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 223 TGNPVIVKPHENAilpaAISVAIAREVLAEQGLDPNLVtlAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWLLDHA--R 300
Cdd:cd07101 145 AGNAVVLKPDSQT----ALTALWAVELLIEAGLPRDLW--QVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAgrR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 301 QAQVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPaggidtdqgRKRFDEVAADLGAAVARFLSD 380
Cdd:cd07101 219 LIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVH---------ESVYDEFVRRFVARTRALRLG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 381 ESVATAV-LGAIQSPATLARI----EEAHGFGQVVLA---SKALTHAEFPQAQVRTPVivacdAADEAAYMEERFGPISF 452
Cdd:cd07101 290 AALDYGPdMGSLISQAQLDRVtahvDDAVAKGATVLAggrARPDLGPYFYEPTVLTGV-----TEDMELFAEETFGPVVS 364
|
410
....*....|...
gi 2230046767 453 VVRAADTGAALQL 465
Cdd:cd07101 365 IYRVADDDEAIEL 377
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
219-318 |
6.04e-04 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 43.04 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 219 AALATGNPVIVKPHENAILPAAISVAIarevLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTAFGNWL--- 295
Cdd:PRK11809 791 AALAAGNSVLAKPAEQTPLIAAQAVRI----LLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqrn 866
|
90 100
....*....|....*....|....*...
gi 2230046767 296 ----LDHA-RQAQVYAELAGVNNVVIES 318
Cdd:PRK11809 867 lagrLDPQgRPIPLIAETGGQNAMIVDS 894
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
224-290 |
8.73e-04 |
|
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: 42.19 E-value: 8.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230046767 224 GNPVIVKPHENAILpaaiSVAIAREVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTA 290
Cdd:cd07123 197 GNVVLWKPSDTAVL----SNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTP 259
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
90-290 |
1.01e-03 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 42.11 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 90 DALIGAAEAAMPGWRKVGAEGRVgiclEILQRLnrrsfeiahAVMMTTGQGWMMAF--QAGGAHAQD-----RglEAV-- 160
Cdd:PRK11904 588 EQALAAARAAFPAWSRTPVEERA----AILERA---------ADLLEANRAELIALcvREAGKTLQDaiaevR--EAVdf 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 161 -----ATAWDEMS---RVPAeavwekPQGKNPPLRLRkhfeivGRGVALVIGcgtfPtWNtYP-GLF-----AALATGNP 226
Cdd:PRK11904 653 cryyaAQARRLFGapeKLPG------PTGESNELRLH------GRGVFVCIS----P-WN-FPlAIFlgqvaAALAAGNT 714
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2230046767 227 VIVKPHENAILPAAISVaiarEVLAEQGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTA 290
Cdd:PRK11904 715 VIAKPAEQTPLIAAEAV----KLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTE 774
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
198-469 |
1.51e-03 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 41.36 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFPT----WNTypglFAALATGNPVIVKPHENAILPAAISVAIAREVLAEQGLDPNLVTlAVVDDPAATRH 273
Cdd:PLN02315 156 GIVGVITAFNFPCavlgWNA----CIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFT-SFCGGAEIGEA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 274 LATHRAVKSIDFTGSTAFGNWLLD--HARQAQVYAELAGVNNVVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVPA 351
Cdd:PLN02315 231 IAKDTRIPLVSFTGSSKVGLMVQQtvNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 352 GGIDT--DQGRKRFDEVAadlgaavarfLSDESVATAVLGAIQSPATLARIEE------AHGfGQVVLASKALThaefPQ 423
Cdd:PLN02315 311 SIYDDvlEQLLTVYKQVK----------IGDPLEKGTLLGPLHTPESKKNFEKgieiikSQG-GKILTGGSAIE----SE 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2230046767 424 AQVRTPVIVACdAADEAAYMEERFGPISFVVRAADTGAALQLSERI 469
Cdd:PLN02315 376 GNFVQPTIVEI-SPDADVVKEELFGPVLYVMKFKTLEEAIEINNSV 420
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
198-491 |
2.11e-03 |
|
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: 40.71 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 198 GVALVIGCGTFPTWNTYPGLFAALATGNPVIVKPHENAILPAAISVAIAREVLAEQGLDPNLvtLAVVDDPA--ATRHLA 275
Cdd:cd07081 97 GVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENL--IGWIDNPSieLAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 276 THRAVKSIDFTGstafGNWLLDHARQAQVYAELAGVNN--VVIESTDNYKGMLKNLAFTLSLYAGQMCTTTQAIIVpagg 353
Cdd:cd07081 175 KFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNtpVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV---- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230046767 354 IDT--DQGRKRFDEVAA------DLGAAVARFLSDESVATAVLGaiQSPATLArieEAHGFgqvvlaskalthaEFPQaQ 425
Cdd:cd07081 247 VDSvyDEVMRLFEGQGAykltaeELQQVQPVILKNGDVNRDIVG--QDAYKIA---AAAGL-------------KVPQ-E 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230046767 426 VRTPVIVACDAADEAAYMEERFGPISFVVRAADTGAALQLSERIVRERG-ALTVGLYSTRSAVIETM 491
Cdd:cd07081 308 TRILIGEVTSLAEHEPFAHEKLSPVLAMYRAANFADADAKALALKLEGGcGHTSAMYSDNIKAIENM 374
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
219-290 |
2.32e-03 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 41.08 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230046767 219 AALATGNPVIVKPHENAILPAAISVAIAREVlaeqGLDPNLVTLAVVDDPAATRHLATHRAVKSIDFTGSTA 290
Cdd:COG4230 703 AALAAGNTVLAKPAEQTPLIAARAVRLLHEA----GVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTE 770
|
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