|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
29-482 |
0e+00 |
|
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: 792.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 EVTRLIDTFRVASEEAVRIDGEVLNLEISARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPAS 188
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 189 RTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGKKKVVLELGGNAAAIVDA 268
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 269 DQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWM 348
Cdd:cd07147 241 DA--DLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 349 DAAVAAGAKIIAGGKVDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQ 428
Cdd:cd07147 319 NEAVDAGAKLLTGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKAL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
5KF0_A 429 RAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVV 482
Cdd:cd07147 399 RAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
29-482 |
0e+00 |
|
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: 570.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 EVTRLIDTFRVASEEAVRIDGEVLNLEISARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPAS 188
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 189 RTPVGALIIAEVLAETNLPKGAFSVLPAHRD-GADLFTTDERFRLLSFTGSPAVGWALKEKAGKKKVVLELGGNAAAIVD 267
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 268 ADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGW 347
Cdd:cd07149 241 ADA--DLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 348 MDAAVAAGAKIIAGGKVDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHA 427
Cdd:cd07149 319 VEEAVEGGARLLTGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
5KF0_A 428 QRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVV 482
Cdd:cd07149 399 LKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
9-484 |
0e+00 |
|
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: 516.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 9 MLKDTYPYYLANEAVYANTD--LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRE 86
Cdd:COG1012 1 MTTPEYPLFIGGEWVAAASGetFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 87 RFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlnleISARAQGYTGYTRRVPIGPCSFISPFNFPLN 166
Cdd:COG1012 81 RREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGET----IPSDAPGTRAYVRREPLGVVGAITPWNFPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 167 LAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAH-RDGADLFTTDERFRLLSFTGSPAVGWAL 245
Cdd:COG1012 157 LAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 246 KEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLK 321
Cdd:COG1012 237 AAAAAEnlKRVTLELGGKNPAIVldDAD----LDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 322 MGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV----DGAMFEATLLEDVGREQDLYRKEAFGPVAILEK 397
Cdd:COG1012 313 VGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRpdgeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 398 FDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEP 477
Cdd:COG1012 393 FDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTET 472
|
....*..
5KF0_A 478 RLMVVRR 484
Cdd:COG1012 473 KTVTIRL 479
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
29-482 |
1.25e-174 |
|
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: 498.11 E-value: 1.25e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 EVTRLIDTFRVASEEAVRIDGEVLNLEISARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPAS 188
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 189 RTPVGALIIAEVLAETNLPKGAFSVL-PAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGKKKVVLELGGNAAAIVD 267
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVtGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 268 ADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGW 347
Cdd:cd07094 241 RDA--DLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 348 MDAAVAAGAKIIAGGKVDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHA 427
Cdd:cd07094 319 VEEAVEAGARLLCGGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
5KF0_A 428 QRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVV 482
Cdd:cd07094 399 FKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
57-478 |
1.32e-161 |
|
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: 465.47 E-value: 1.32e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNLei 136
Cdd:pfam00171 37 AARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 sarAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPA 216
Cdd:pfam00171 115 ---DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 217 H-RDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:pfam00171 192 SgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQnlKRVTLELGGKNPLIVleDAD----LDAAVEAAVFGAFGNAGQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVD---GAM 368
Cdd:pfam00171 268 VCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEAGldnGYF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 369 FEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFR 448
Cdd:pfam00171 348 VEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGD 427
|
410 420 430
....*....|....*....|....*....|
5KF0_A 449 VDNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:pfam00171 428 ADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
57-478 |
1.19e-156 |
|
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: 451.66 E-value: 1.19e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlnleI 136
Cdd:cd07078 6 AARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV----I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP- 215
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQSC 293
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEnlKRVTLELGGKSPLIVFDDA--DLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 294 IGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVD----GAMF 369
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeggkGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 370 EATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRV 449
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAE 399
|
410 420
....*....|....*....|....*....
5KF0_A 450 DNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07078 400 PSAPFGGVKQSGIGREGGPYGLEEYTEPK 428
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
29-482 |
7.67e-141 |
|
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: 412.51 E-value: 7.67e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 EVTRLIDTFRVASEEAVRIDGEVLNLEISARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPAS 188
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 189 RTPVGALIIAEVLAETNLPKGAFSVLPAHRDG-ADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAI 265
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEvGDEIVTNPKVNMISFTGSTAVGLLIASKAGGtgKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 266 V--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRR 343
Cdd:cd07145 241 VlkDAD----LERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 344 LSGWMDAAVAAGAKIIAGGK-VDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTD 422
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKrDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 423 SLTHAQRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVV 482
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
29-475 |
2.93e-135 |
|
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: 397.89 E-value: 2.93e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPmreLPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALAASYRST---LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 EVTRLIDTFRVASEEAVRIDGEVLNLEISARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPAS 188
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 189 RTPVGALIIAEVLAETNLPKGAFS-VLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGKKKVVLELGGNAAAIV- 266
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSvVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVm 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 267 -DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLS 345
Cdd:cd07146 238 dDAD----LERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 346 GWMDAAVAAGAKIIAGGKVDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLT 425
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
5KF0_A 426 HAQRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLG-REGIRYAIEDMT 475
Cdd:cd07146 394 TIKRLVERLDVGTVNVNEVPGFRSELSPFGGVKDSGLGgKEGVREAMKEMT 444
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
57-476 |
7.85e-133 |
|
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: 391.80 E-value: 7.85e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlnleI 136
Cdd:cd07103 27 AAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARRIYGRT----I 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPA 216
Cdd:cd07103 103 PSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 217 HRDG-ADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07103 183 SPAEiGEALCASPRVRKISFTGSTAVGKLLMAQAADtvKRVSLELGGNAPFIVfdDAD----LDKAVDGAIASKFRNAGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---DGAM 368
Cdd:cd07103 259 TCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRlglGGYF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 369 FEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIND-VPSf 447
Cdd:cd07103 339 YEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTgLIS- 417
|
410 420
....*....|....*....|....*....
5KF0_A 448 rVDNMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:cd07103 418 -DAEAPFGGVKESGLGREGGKEGLEEYLE 445
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
57-476 |
1.57e-130 |
|
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: 384.96 E-value: 1.57e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNlei 136
Cdd:cd07104 8 AAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILP--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAqGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPV-GALIIAEVLAETNLPKGAFSVLP 215
Cdd:cd07104 85 SDVP-GKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVtGGLLIAEIFEEAGLPKGVLNVVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHRDGA-DLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSG 290
Cdd:cd07104 164 GGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRhlKKVALELGGNNPLIVldDAD----LDLAVSAAAFGAFLHQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 291 QSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVDGAMFE 370
Cdd:cd07104 240 QICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEGLFYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 371 ATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVD 450
Cdd:cd07104 320 PTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEP 399
|
410 420
....*....|....*....|....*.
5KF0_A 451 NMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:cd07104 400 HVPFGGVKASGGGRFGGPASLEEFTE 425
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
29-478 |
3.14e-122 |
|
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: 364.73 E-value: 3.14e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 EVTRLIDTFRVASEEAVRIDGEVLNLEisarAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPAS 188
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSD----SPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 189 RTPVGALIIAEVLAETNLPKGAFSVLPAHRDG-ADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAI 265
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEvGDELVDDPRVRMVTFTGSTAVGREIAEKAGRhlKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 266 V--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRR 343
Cdd:cd07150 237 VlaDAD----LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 344 LSGWMDAAVAAGAKIIAGGKVDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDS 423
Cdd:cd07150 313 IKRQVEDAVAKGAKLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
5KF0_A 424 LthaQRAWD---ELEVGGVVINDVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07150 393 L---QRAFKlaeRLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
57-478 |
9.90e-120 |
|
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: 355.38 E-value: 9.90e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEvlnlEI 136
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGP----EL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP- 215
Cdd:cd06534 78 PSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQSC 293
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAEnlKPVTLELGGKSPVIVDEDA--DLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 294 IGVQRILVHASLYDTLRDKLVaktrslkmgdpkdpstfvgpmisesesrrlsgwmdaavaagakiiaggkvdgamfeaTL 373
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV---------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 374 LEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDNMP 453
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAP 338
|
410 420
....*....|....*....|....*
5KF0_A 454 YGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTK 363
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
68-482 |
1.00e-117 |
|
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: 353.26 E-value: 1.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 68 LPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNLEISARAQGYTGYT 147
Cdd:cd07148 41 LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPMGLTPASAGRIAFT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 148 RRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTTD 227
Cdd:cd07148 121 TREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 228 ERFRLLSFTGSPAVGWALKEK-AGKKKVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLY 306
Cdd:cd07148 201 PRVAFFSFIGSARVGWMLRSKlAPGTRCALEHGGAAPVIVDRSA--DLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 307 DTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK-VDGAMFEATLLEDVGREQDLYR 385
Cdd:cd07148 279 DDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKrLSDTTYAPTVLLDPPRDAKVST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 386 KEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLGRE 465
Cdd:cd07148 359 QEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYGTG 438
|
410
....*....|....*..
5KF0_A 466 GIRYAIEDMTEPRLMVV 482
Cdd:cd07148 439 GIPYTMHDMTQEKMAVI 455
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
14-483 |
3.96e-116 |
|
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: 349.95 E-value: 3.96e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 14 YPYYLANEAVYANTDL-EVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKP-MRELPAYRRQAVLDHCVARFRERFDEL 91
Cdd:cd07082 2 FKYLINGEWKESSGKTiEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGwWPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 92 AEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNLEISARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHK 171
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 172 VAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAH-RDGADLFTTDERFRLLSFTGSPAVGWALKEKAG 250
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 251 KKKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDP 328
Cdd:cd07082 242 MKRLVLELGGKDPAIVlpDAD----LELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 329 STFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK-VDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALAR 407
Cdd:cd07082 318 GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGrEGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5KF0_A 408 VNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVVR 483
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-476 |
1.32e-106 |
|
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: 325.03 E-value: 1.32e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 25 ANTDLEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPIN 104
Cdd:cd07151 8 SERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 105 DSRGEVTRLIDTFRVASEEAVRIDGEVLNLEIsaraQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVL 184
Cdd:cd07151 88 KANIEWGAAMAITREAATFPLRMEGRILPSDV----PGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 185 KPASRTPV-GALIIAEVLAETNLPKGAFSVL-PAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGG 260
Cdd:cd07151 164 KPASDTPItGGLLLAKIFEEAGLPKGVLNVVvGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRhlKKVALELGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 261 NAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISE 338
Cdd:cd07151 244 NNPFVVleDAD----IDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 339 SESRRLSGWMDAAVAAGAKIIAGGKVDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAG 418
Cdd:cd07151 320 SQVDGLLDKIEQAVEEGATLLVGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
5KF0_A 419 VFTDSLTHAQRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:cd07151 400 VFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTT 457
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
57-482 |
8.64e-105 |
|
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: 320.27 E-value: 8.64e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAV------KPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGE 130
Cdd:cd07114 23 RAVAAAraafegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 131 VLNLeisaRAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGA 210
Cdd:cd07114 103 VIPV----DKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 211 FSVLPAHRD--GADLfTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFG 284
Cdd:cd07114 179 VNVVTGFGPetGEAL-VEHPLVAKIAFTGGTETGRHIARAAAEnlAPVTLELGGKSPNIVfdDAD----LDAAVNGVVAG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 285 AYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV 364
Cdd:cd07114 254 IFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 365 -------DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVG 437
Cdd:cd07114 334 psgadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAG 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
5KF0_A 438 GVVINDVPSFRVdNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVV 482
Cdd:cd07114 414 TVWVNTYRALSP-SSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
57-478 |
9.17e-105 |
|
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: 319.90 E-value: 9.17e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLdHCVAR-FRERFDELAEALCIEAGKPINDSR-GEVTRLIDTFRVASEEAVRIDGEVLNl 134
Cdd:cd07093 27 AAKEAFPGWSRMSPAERARIL-HKVADlIEARADELALLESLDTGKPITLARtRDIPRAAANFRFFADYILQLDGESYP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 135 eisaRAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVL 214
Cdd:cd07093 105 ----QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 215 paHRDGA---DLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYY 287
Cdd:cd07093 181 --HGFGPeagAALVAHPDVDLISFTGETATGRTIMRAAAPnlKPVSLELGGKNPNIVfaDAD----LDRAVDAAVRSSFS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 288 QSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVD-- 365
Cdd:cd07093 255 NNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRPel 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 366 -----GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVV 440
Cdd:cd07093 335 pdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVW 414
|
410 420 430
....*....|....*....|....*....|....*...
5KF0_A 441 INDvPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07093 415 VNC-WLVRDLRTPFGGVKASGIGREGGDYSLEFYTELK 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
57-471 |
3.31e-104 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 317.48 E-value: 3.31e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVR-IDGEVLNLE 135
Cdd:cd07100 7 RAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAfLADEPIETD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 136 isaraqGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP 215
Cdd:cd07100 87 ------AGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07100 161 IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKnlKKSVLELGGSDPFIVldDAD----LDKAVKTAVKGRLQNAGQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---DGAM 368
Cdd:cd07100 237 SCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRpdgPGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 369 FEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVpsFR 448
Cdd:cd07100 317 YPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM--VK 394
|
410 420
....*....|....*....|....
5KF0_A 449 VD-NMPYGGVKDSGLGREGIRYAI 471
Cdd:cd07100 395 SDpRLPFGGVKRSGYGRELGRFGI 418
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
57-482 |
5.04e-101 |
|
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: 309.99 E-value: 5.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLnlei 136
Cdd:cd07152 21 RAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEIL---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 sARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPV-GALIIAEVLAETNLPKGAFSVLP 215
Cdd:cd07152 97 -PSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVsGGVVIARLFEEAGLPAGVLHVLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07152 176 GGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRhlKKVSLELGGKNALIVldDAD----LDLAASNGAWGAFLHQGQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVDGAMFEA 371
Cdd:cd07152 252 ICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYDGLFYRP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 372 TLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDN 451
Cdd:cd07152 332 TVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPH 411
|
410 420 430
....*....|....*....|....*....|..
5KF0_A 452 MPYGGVKDSGLG-REGIRYAIEDMTEPRLMVV 482
Cdd:cd07152 412 NPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
17-482 |
9.87e-101 |
|
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: 309.97 E-value: 9.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 17 YLANEAVYANTD--LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEA 94
Cdd:cd07088 1 YINGEFVPSSSGetIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 95 LCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNLEISARaqgyTGYTRRVPIGPCSFISPFNFPLNLAAHKVAP 174
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNE----NIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 175 ALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP-AHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK-- 251
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTgRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAEni 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 252 KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPS 329
Cdd:cd07088 237 TKVSLELGGKAPAIVmkDAD----LDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 330 TFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVD----GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDAL 405
Cdd:cd07088 313 TDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPegekGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5KF0_A 406 ARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDvPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVV 482
Cdd:cd07088 393 ELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINR-ENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
31-476 |
8.06e-100 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 307.05 E-value: 8.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 31 VTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEV 110
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 111 TRLIDTFRVASEEAVRIDGEVlnleISARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRT 190
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDT----IPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 191 PVGALIIAEVLAETNLPKGAFSVLPAHRDGA--DLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV 266
Cdd:TIGR01780 157 PLSALALARLAEQAGIPKGVLNVITGSRAKEvgNVLTTSPLVRKISFTGSTNVGKILMKQSAStvKKVSMELGGNAPFIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 267 DADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSG 346
Cdd:TIGR01780 237 FDDA--DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 347 WMDAAVAAGAKIIAGGKVD---GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDS 423
Cdd:TIGR01780 315 HIADAVEKGAKVVTGGKRHelgGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
5KF0_A 424 LTHAQRAWDELEVGGVVIND-VPSFRVdnMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:TIGR01780 395 LSRIWRVAEALEYGMVGINTgLISNVV--APFGGVKQSGLGREGSKYGIEEYLE 446
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
36-478 |
2.91e-98 |
|
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: 303.21 E-value: 2.91e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 36 SGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG-EVTRLI 114
Cdd:cd07115 6 TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 115 DTFRVASEEAVRIDGEVLNLEisaraQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGA 194
Cdd:cd07115 86 DTFRYYAGWADKIEGEVIPVR-----GPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 195 LIIAEVLAETNLPKGAFSVLPAH-RDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DAD 269
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGnlKRVSLELGGKSANIVfaDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 270 qfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMD 349
Cdd:cd07115 241 ----LDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 350 AAVAAGAKIIAGGKVDGA---MFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTH 426
Cdd:cd07115 317 VGREEGARLLTGGKRPGArgfFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
5KF0_A 427 AQRAWDELEVGGVVINDVPSFRVdNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDP-GSPFGGYKQSGFGREMGREALDEYTEVK 447
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
57-478 |
4.55e-97 |
|
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: 301.05 E-value: 4.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVK------PMRELPAYRRQAVLdHCVARFRER-FDELAEALCIEAGKPINDS-RGEVTRLIDTFRVASEEAVRID 128
Cdd:cd07091 45 AAVKAARaafetgWWRKMDPRERGRLL-NKLADLIERdRDELAALESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 129 GEVLNLEisaraQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPK 208
Cdd:cd07091 124 GKTIPID-----GNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 209 GAFSVLPAH-RDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK---KKVVLELGGNAAAIV--DADqfeqLDYVVDRLA 282
Cdd:cd07091 199 GVVNIVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsnlKKVTLELGGKSPNIVfdDAD----LDKAVEWAA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 283 FGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGG 362
Cdd:cd07091 275 FGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 363 KV---DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGV 439
Cdd:cd07091 355 ERhgsKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTV 434
|
410 420 430
....*....|....*....|....*....|....*....
5KF0_A 440 VINDVPSFRVdNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07091 435 WVNTYNVFDA-AVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
57-472 |
8.25e-97 |
|
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: 299.93 E-value: 8.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNlei 136
Cdd:cd07097 45 AAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLP--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARaQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFS-VLP 215
Cdd:cd07097 122 STR-PGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNlVMG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07097 201 SGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAArgARVQLEMGGKNPLVVldDAD----LDLAVECAVQGAFFSTGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV-----DG 366
Cdd:cd07097 277 RCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkrpdEG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 367 AMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINdVPS 446
Cdd:cd07097 357 YYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN-LPT 435
|
410 420
....*....|....*....|....*...
5KF0_A 447 FRVD-NMPYGGVKDSGLG-REGIRYAIE 472
Cdd:cd07097 436 AGVDyHVPFGGRKGSSYGpREQGEAALE 463
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
56-481 |
2.67e-96 |
|
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: 298.09 E-value: 2.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 56 GAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSR-GEVTRLIDTFRVASEEAVRIDGEVLNl 134
Cdd:cd07092 26 AAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPGAVDNFRFFAGAARTLEGPAAG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 135 eisARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETnLPKGAFSVL 214
Cdd:cd07092 105 ---EYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEV-LPPGVVNVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 215 PAHRDGA-DLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQS 289
Cdd:cd07092 181 CGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADtlKRVHLELGGKAPVIVfdDAD----LDAAVAGIATAGYYNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 290 GQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAvAAGAKIIAGGKV---DG 366
Cdd:cd07092 257 GQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA-PAHARVLTGGRRaegPG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 367 AMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPS 446
Cdd:cd07092 336 YFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP 415
|
410 420 430
....*....|....*....|....*....|....*.
5KF0_A 447 FrVDNMPYGGVKDSGLGREGIRYAIEDMTEPR-LMV 481
Cdd:cd07092 416 L-AAEMPHGGFKQSGYGKDLSIYALEDYTRIKhVMV 450
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
29-466 |
9.16e-95 |
|
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: 294.87 E-value: 9.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAV--KPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDS 106
Cdd:cd07139 16 IDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 107 R-GEVTRLIDTFRVASEeavrIDGEVLNLEISARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLK 185
Cdd:cd07139 96 RrAQGPGPAALLRYYAA----LARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 186 PASRTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAA 263
Cdd:cd07139 172 PSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGErlARVTLELGGKSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 264 AIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESES 341
Cdd:cd07139 252 AIVldDAD----LDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 342 RRLSGWMDAAVAAGAKIIAGGKV-----DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQ 416
Cdd:cd07139 328 ERVEGYIAKGRAEGARLVTGGGRpagldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLS 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
5KF0_A 417 AGVFTDSLTHAQRAWDELEVGGVVINdvpSFRVD-NMPYGGVKDSGLGREG 466
Cdd:cd07139 408 GSVWTADVERGLAVARRIRTGTVGVN---GFRLDfGAPFGGFKQSGIGREG 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
73-476 |
1.30e-94 |
|
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: 294.12 E-value: 1.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 73 RQAVLDHCVARFRERFDELAEALCIEAGKPINDSR-GEVTRLIDTFRVASEEAVRIDGEVlnleiSARAQGYTGYTRRVP 151
Cdd:cd07112 50 RKAVLLRLADLIEAHRDELALLETLDMGKPISDALaVDVPSAANTFRWYAEAIDKVYGEV-----APTGPDALALITREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 152 IGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPA-----------HRDg 220
Cdd:cd07112 125 LGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGfghtagealglHMD- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 221 adlftTDerfrLLSFTGSPAVGWALKEKAGK---KKVVLELGGNAAAIVDADQfEQLDYVVDRLAFGAYYQSGQSCIGVQ 297
Cdd:cd07112 204 -----VD----ALAFTGSTEVGRRFLEYSGQsnlKRVWLECGGKSPNIVFADA-PDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 298 RILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVD-----GAMFEAT 372
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVltetgGFFVEPT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 373 LLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVpsFRVDN- 451
Cdd:cd07112 354 VFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCF--DEGDIt 431
|
410 420
....*....|....*....|....*
5KF0_A 452 MPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:cd07112 432 TPFGGFKQSGNGRDKSLHALDKYTE 456
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
57-465 |
1.18e-93 |
|
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: 292.16 E-value: 1.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNLEI 136
Cdd:cd07086 43 AAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSER 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQgytgYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGAL----IIAEVLAETNLPKGAFS 212
Cdd:cd07086 123 PGHRL----MEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIavtkILAEVLEKNGLPPGVVN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 213 VLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQ 288
Cdd:cd07086 199 LVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARrfGRVLLELGGNNAIIVmdDAD----LDLAVRAVLFAAVGT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 289 SGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---- 364
Cdd:cd07086 275 AGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidgg 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 365 -DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWD--ELEVGGVVI 441
Cdd:cd07086 355 ePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGpkGSDCGIVNV 434
|
410 420
....*....|....*....|....
5KF0_A 442 NDVPSFRVDNMPYGGVKDSGLGRE 465
Cdd:cd07086 435 NIPTSGAEIGGAFGGEKETGGGRE 458
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
68-478 |
1.36e-93 |
|
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: 291.45 E-value: 1.36e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 68 LPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG-EVTRLIDTFRVASEEAVRIDGEVLNLEISARAQGYTGY 146
Cdd:cd07089 39 TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 147 TRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP-AHRDGADLFT 225
Cdd:cd07089 119 VRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTgSDNAVGEALT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 226 TDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILV 301
Cdd:cd07089 199 TDPRVDMVSFTGSTAVGRRIMAQAAAtlKRVLLELGGKSANIVldDAD----LAAAAPAAVGVCMHNAGQGCALTTRLLV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 302 HASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV-----DGAMFEATLLED 376
Cdd:cd07089 275 PRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGRpagldKGFYVEPTLFAD 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 377 VGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDNmPYGG 456
Cdd:cd07089 355 VDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDA-PFGG 433
|
410 420
....*....|....*....|..
5KF0_A 457 VKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07089 434 YKQSGLGRENGIEGLEEFLETK 455
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
24-476 |
1.51e-93 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 292.36 E-value: 1.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 24 YANTDLEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPI 103
Cdd:PLN02278 37 YDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 104 NDSRGEV---TRLIDTFrvaSEEAVRIDGEVLNLEISaraqgytgyTRRV-----PIGPCSFISPFNFPLNLAAHKVAPA 175
Cdd:PLN02278 117 KEAIGEVaygASFLEYF---AEEAKRVYGDIIPSPFP---------DRRLlvlkqPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 176 LAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFS-VLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--K 252
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNvVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAtvK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 253 KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPST 330
Cdd:PLN02278 265 RVSLELGGNAPFIVfdDAD----LDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 331 FVGPMISESESRRLSGWMDAAVAAGAKIIAGGK---VDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALAR 407
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKrhsLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5KF0_A 408 VNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIND--VPSfrvDNMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEglIST---EVAPFGGVKQSGLGREGSKYGIDEYLE 488
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
57-478 |
2.59e-93 |
|
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: 290.20 E-value: 2.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEeaVRIDGEVLNLEI 136
Cdd:cd07106 27 AAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTAS--LDLPDEVIEDDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAqgytgYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETnLPKGAFSVLPa 216
Cdd:cd07106 105 TRRV-----ELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVS- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 217 hrDGADL---FTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQS 289
Cdd:cd07106 178 --GGDELgpaLTSHPDIRKISFTGSTATGKKVMASAAKtlKRVTLELGGNDAAIVlpDVD----IDAVAPKLFWGAFINS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 290 GQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVD---G 366
Cdd:cd07106 252 GQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLdgpG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 367 AMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPS 446
Cdd:cd07106 332 YFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGA 411
|
410 420 430
....*....|....*....|....*....|..
5KF0_A 447 FRVDnMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07106 412 LDPD-APFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
56-476 |
6.83e-93 |
|
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: 289.24 E-value: 6.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 56 GAAVDAVK------PMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDG 129
Cdd:cd07118 22 DAAVAAARkafdkgPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 130 EVLNleisARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKG 209
Cdd:cd07118 102 DSYN----NLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 210 AFSVLPAHRDGA-DLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFG 284
Cdd:cd07118 178 VVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARnlKKVSLELGGKNPQIVfaDAD----LDAAADAVVFG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 285 AYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV 364
Cdd:cd07118 254 VYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 365 ----DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVV 440
Cdd:cd07118 334 lasaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVW 413
|
410 420 430
....*....|....*....|....*....|....*.
5KF0_A 441 INDVPSFRVDnMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:cd07118 414 VNTFLDGSPE-LPFGGFKQSGIGRELGRYGVEEYTE 448
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
57-478 |
2.92e-91 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 285.65 E-value: 2.92e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKpmRELPAYR------RQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG-EVTRLIDTFRVASeeavridG 129
Cdd:PRK13473 43 AAVAAAD--AAFPEWSqttpkeRAEALLKLADAIEENADEFARLESLNCGKPLHLALNdEIPAIVDVFRFFA-------G 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 130 EVLNLEISARAQ---GYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETnL 206
Cdd:PRK13473 114 AARCLEGKAAGEyleGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-L 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 207 PKGAFSVLPAH-RDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRL 281
Cdd:PRK13473 193 PPGVLNVVTGRgATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADsvKRTHLELGGKAPVIVfdDAD----LDAVVEGI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 282 AFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAG-AKIIA 360
Cdd:PRK13473 269 RTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 361 GGKV---DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVG 437
Cdd:PRK13473 349 GGEApdgKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYG 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
5KF0_A 438 GVVINDvpSFR-VDNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:PRK13473 429 CTWVNT--HFMlVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
57-476 |
5.46e-91 |
|
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: 285.40 E-value: 5.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNLEI 136
Cdd:cd07131 45 AAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQgytgYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPA 216
Cdd:cd07131 125 PNKDA----MTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 217 HRDGA-DLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07131 201 RGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARpnKRVALEMGGKNPIIVmdDAD----LDLALEGALWSAFGTTGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV------- 364
Cdd:cd07131 277 RCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltgggye 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 365 DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINdV 444
Cdd:cd07131 357 KGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN-A 435
|
410 420 430
....*....|....*....|....*....|....
5KF0_A 445 PSFRVD-NMPYGGVKDSGLG-REGIRYAIEDMTE 476
Cdd:cd07131 436 PTIGAEvHLPFGGVKKSGNGhREAGTTALDAFTE 469
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
36-472 |
1.78e-89 |
|
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: 280.73 E-value: 1.78e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 36 SGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLID 115
Cdd:cd07090 6 TGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 116 TFRVASEEAVRIDGEVLNLeisarAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGAL 195
Cdd:cd07090 86 CLEYYAGLAPTLSGEHVPL-----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 196 IIAEVLAETNLPKGAFSVLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqf 271
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKgiKHVTLELGGKSPLIIfdDAD-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 272 eqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAA 351
Cdd:cd07090 239 --LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 352 VAAGAKIIAGGKV--------DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDS 423
Cdd:cd07090 317 KQEGAKVLCGGERvvpedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
5KF0_A 424 LTHAQRAWDELEVGGVVINDVPSFRVdNMPYGGVKDSGLGREGIRYAIE 472
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPV-EVPFGGYKQSGFGRENGTAALE 444
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
57-476 |
1.13e-88 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 278.48 E-value: 1.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPI-NDSRGEVTRLIDTFR----VASEeavrIDGEV 131
Cdd:cd07108 27 AAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRyfggLAGE----LKGET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 132 LNLeisarAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETnLPKGAF 211
Cdd:cd07108 103 LPF-----GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 212 SVLPAHRD--GADLfTTDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGA 285
Cdd:cd07108 177 NVITGYGEecGAAL-VDHPDVDKVTFTGSTEVGKIIYRAAADRliPVSLELGGKSPMIVfpDAD----LDDAVDGAIAGM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 286 -YYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAA-GAKIIAGGK 363
Cdd:cd07108 252 rFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 364 V-------DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEV 436
Cdd:cd07108 332 LpgegplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEA 411
|
410 420 430 440
....*....|....*....|....*....|....*....|
5KF0_A 437 GGVVINDVPSFRVdNMPYGGVKDSGLGREgirYAIEDMTE 476
Cdd:cd07108 412 GWVQVNQGGGQQP-GQSYGGFKQSGLGRE---ASLEGMLE 447
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
58-476 |
2.41e-87 |
|
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: 276.11 E-value: 2.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 58 AVDAVK------PMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEV 131
Cdd:cd07119 40 AIAAARrafdsgEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 132 lnleISARAQGYTgYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAF 211
Cdd:cd07119 120 ----YDVPPHVIS-RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 212 SVL--PAHRDGADLFTTDErFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGA 285
Cdd:cd07119 195 NLVtgSGATVGAELAESPD-VDLVSFTGGTATGRSIMRAAAGnvKKVALELGGKNPNIVfaDAD----FETAVDQALNGV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 286 YYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK-- 363
Cdd:cd07119 270 FFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKrp 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 364 -----VDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGG 438
Cdd:cd07119 350 tgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGT 429
|
410 420 430
....*....|....*....|....*....|....*....
5KF0_A 439 VVINDV-PSFrvDNMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:cd07119 430 VWINDYhPYF--AEAPWGGYKQSGIGRELGPTGLEEYQE 466
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
57-478 |
8.31e-87 |
|
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: 273.74 E-value: 8.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEvtrlIDTFRVASEEAVRIDGEVLNLEI 136
Cdd:cd07102 26 RARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE----IRGMLERARYMISIAEEALADIR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVL-P 215
Cdd:cd07102 102 VPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLhL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHRDGADLfTTDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07102 182 SHETSAAL-IADPRIDHVSFTGSVAGGRAIQRAAAGRfiKVGLELGGKDPAYVrpDAD----LDAAAESLVDGAFFNSGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV------D 365
Cdd:cd07102 257 SCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALfpedkaG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 366 GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN--D 443
Cdd:cd07102 337 GAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcD 416
|
410 420 430
....*....|....*....|....*....|....*
5KF0_A 444 VPSFRvdnMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07102 417 YLDPA---LAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
57-481 |
1.53e-86 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 273.22 E-value: 1.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG-EVTRLIDTFRVASEEAVRIDGEvlnle 135
Cdd:cd07138 44 AARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAaQVGLGIGHLRAAADALKDFEFE----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 136 isaRAQGyTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLp 215
Cdd:cd07138 119 ---ERRG-NSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLV- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 aHRDGA---DLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQ 288
Cdd:cd07138 194 -NGDGPvvgEALSAHPDVDMVSFTGSTRAGKRVAEAAADtvKRVALELGGKSANIIldDAD----LEKAVPRGVAACFAN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 289 SGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGG--KVD- 365
Cdd:cd07138 269 SGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgRPEg 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 366 ---GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN 442
Cdd:cd07138 349 lerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN 428
|
410 420 430
....*....|....*....|....*....|....*....
5KF0_A 443 DVPsFRVDnMPYGGVKDSGLGREGIRYAIEDMTEPRLMV 481
Cdd:cd07138 429 GAA-FNPG-APFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
57-468 |
2.45e-85 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 269.86 E-value: 2.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRI--DGEVLNl 134
Cdd:cd07099 26 RARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVlaPRKVPT- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 135 eiSARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVL 214
Cdd:cd07099 105 --GLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 215 PAHRD-GADLFttDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07099 183 TGDGAtGAALI--DAGVDKVAFTGSVATGRKVMAAAAERliPVVLELGGKDPMIVLADA--DLERAAAAAVWGAMVNAGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK---VDGAM 368
Cdd:cd07099 259 TCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGArsnGGGPF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 369 FEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFR 448
Cdd:cd07099 339 YEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTA 418
|
410 420
....*....|....*....|....*
5KF0_A 449 -VDNMPYGGVKDSGLGR----EGIR 468
Cdd:cd07099 419 gIPALPFGGVKDSGGGRrhgaEGLR 443
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-476 |
2.48e-85 |
|
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: 269.06 E-value: 2.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlnleI 136
Cdd:cd07105 8 AAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS----I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPA 216
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 217 HRDGADLFTtdERF------RLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAY 286
Cdd:cd07105 164 SPEDAPEVV--EALiahpavRKVNFTGSTRVGRIIAETAAKhlKPVLLELGGKAPAIVleDAD----LDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 287 YQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDpkdpsTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV-- 364
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAde 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 365 --DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN 442
Cdd:cd07105 313 spSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430
....*....|....*....|....*....|....*....
5KF0_A 443 -----DVPSfrvdnMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:cd07105 393 gmtvhDEPT-----LPHGGVKSSGYGRFNGKWGIDEFTE 426
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
66-465 |
2.64e-85 |
|
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: 269.87 E-value: 2.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 66 RELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNLEisaraQGYTG 145
Cdd:cd07109 37 LRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKLHGETIPLG-----PGYFV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 146 YTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP--AHRDGADL 223
Cdd:cd07109 112 YTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTglGAEAGAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 224 fTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRI 299
Cdd:cd07109 192 -VAHPGVDHISFTGSVETGIAVMRAAAEnvVPVTLELGGKSPQIVfaDAD----LEAALPVVVNAIIQNAGQTCSAGSRL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 300 LVHASLYDTLRDKLVAKTRSLKMGDP-KDPStfVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV------DGAMFEAT 372
Cdd:cd07109 267 LVHRSIYDEVLERLVERFRALRVGPGlEDPD--LGPLISAKQLDRVEGFVARARARGARIVAGGRIaegapaGGYFVAPT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 373 LLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDNM 452
Cdd:cd07109 345 LLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIEL 424
|
410
....*....|...
5KF0_A 453 PYGGVKDSGLGRE 465
Cdd:cd07109 425 PFGGVKKSGHGRE 437
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
10-463 |
7.91e-84 |
|
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: 267.55 E-value: 7.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 10 LKDTYPYYLANEAVYANTDLEVTDKF-SGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERF 88
Cdd:cd07124 29 LGREYPLVIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 89 DELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNleisaRAQGYTGYTRRVPIGPCSFISPFNFPLNLA 168
Cdd:cd07124 109 FELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVE-----MVPGEDNRYVYRPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 169 AHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAhrDGA---DLFTTDERFRLLSFTGSPAVGWAL 245
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPG--PGEevgDYLVEHPDVRFIAFTGSREVGLRI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 246 KEKAGK--------KKVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKT 317
Cdd:cd07124 262 YERAAKvqpgqkwlKRVIAEMGGKNAIIVDEDA--DLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 318 RSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGaKIIAGGKVDGAMFEA-----TLLEDVGREQDLYRKEAFGPV 392
Cdd:cd07124 340 KALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGyfvqpTIFADVPPDHRLAQEEIFGPV 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
5KF0_A 393 AILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN-DVPSFRVDNMPYGGVKDSGLG 463
Cdd:cd07124 419 LAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrKITGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
17-483 |
1.35e-83 |
|
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: 266.23 E-value: 1.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 17 YLANEAVYANTD--LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMR-ELPAYRRQAVLDHCVARFRERFDELAE 93
Cdd:cd07113 3 FIDGRPVAGQSEkrLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWaKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 94 ALCIEAGKPINDSRG-EVTRLIDTFRVASEEAVRIDGEVLNLEISARA-QGYTGYTRRVPIGPCSFISPFNFPLNLAAHK 171
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLAPSIPSMQgERYTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 172 VAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK 251
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 252 --KKVVLELGG-NAAAIV-DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKD 327
Cdd:cd07113 243 dlTRVTLELGGkNAAAFLkDAD----IDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 328 PSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDA 404
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEAlagEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5KF0_A 405 LARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINdVPSFRVDNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVVR 483
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN-MHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
57-465 |
5.63e-83 |
|
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: 263.83 E-value: 5.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlNLEI 136
Cdd:cd07110 27 AARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQLDAKA-ERAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP- 215
Cdd:cd07110 106 PLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTg 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 -AHRDGADLfTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSG 290
Cdd:cd07110 186 tGDEAGAPL-AAHPGIDKISFTGSTATGSQVMQAAAQdiKPVSLELGGKSPIIVfdDAD----LEKAVEWAMFGCFWNNG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 291 QSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV-----D 365
Cdd:cd07110 261 QICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRRpahleK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 366 GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDV- 444
Cdd:cd07110 341 GYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSq 420
|
410 420
....*....|....*....|.
5KF0_A 445 PSFrvDNMPYGGVKDSGLGRE 465
Cdd:cd07110 421 PCF--PQAPWGGYKRSGIGRE 439
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
57-478 |
5.94e-83 |
|
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: 264.65 E-value: 5.94e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVK-----PMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPIN-DSRGEVTRLIDTFRVASEEAVRIDGE 130
Cdd:cd07144 49 KAVKAARkafesWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHsNALGDLDEIIAVIRYYAGWADKIQGK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 131 VLNLEISARAqgytgYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGA 210
Cdd:cd07144 129 TIPTSPNKLA-----YTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 211 FSVLPAH--RDGADLFTTDERFRlLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFG 284
Cdd:cd07144 204 VNIIPGYgaVAGSALAEHPDVDK-IAFTGSTATGRLVMKAAAQnlKAVTLECGGKSPALVfeDAD----LDQAVKWAAAG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 285 AYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRS-LKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK 363
Cdd:cd07144 279 IMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 364 VD------GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVG 437
Cdd:cd07144 359 KApeglgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAG 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
5KF0_A 438 GVVIN-----DVpsfrvdNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:cd07144 439 MVWINssndsDV------GVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
57-476 |
1.88e-82 |
|
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: 262.28 E-value: 1.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYR-----RQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEV 131
Cdd:cd07120 23 AAIAAARRAFDETDWAhdprlRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 132 LNLEisaraQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAE-TNLPKGA 210
Cdd:cd07120 103 IEPE-----PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEiPSLPAGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 211 FSVLPAHR-DGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGA 285
Cdd:cd07120 178 VNLFTESGsEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPtlKRLGLELGGKTPCIVfdDAD----LDAALPKLERAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 286 YYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKII-AGGKV 364
Cdd:cd07120 254 TIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVlRGGPV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 365 D-----GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGV 439
Cdd:cd07120 334 TeglakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTV 413
|
410 420 430
....*....|....*....|....*....|....*...
5KF0_A 440 VINDVPSFRvDNMPYGGVKDSGLGR-EGIRyAIEDMTE 476
Cdd:cd07120 414 WINDWNKLF-AEAEEGGYRQSGLGRlHGVA-ALEDFIE 449
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
29-482 |
6.94e-81 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 259.07 E-value: 6.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:PRK11241 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 EVTRLIDTFRVASEEAVRIDGEVLnleisaraQGYTGYTR----RVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVL 184
Cdd:PRK11241 108 EISYAASFIEWFAEEGKRIYGDTI--------PGHQADKRliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 185 KPASRTPVGALIIAEVLAETNLPKGAFSVL--PAHRDGADLfTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGG 260
Cdd:PRK11241 180 KPASQTPFSALALAELAIRAGIPAGVFNVVtgSAGAVGGEL-TSNPLVRKLSFTGSTEIGRQLMEQCAKdiKKVSLELGG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 261 NAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISE 338
Cdd:PRK11241 259 NAPFIVfdDAD----LDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 339 SESRRLSGWMDAAVAAGAKIIAGGK---VDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGL 415
Cdd:PRK11241 335 KAVAKVEEHIADALEKGARVVCGGKaheLGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGL 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
5KF0_A 416 QAGVFTDSLTHAQRAWDELEVGGVVIND-VPSFRVdnMPYGGVKDSGLGREGIRYAIEDMTEPRLMVV 482
Cdd:PRK11241 415 AAYFYARDLSRVFRVGEALEYGIVGINTgIISNEV--APFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
26-476 |
1.79e-79 |
|
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: 255.53 E-value: 1.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 26 NTDLEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPM--RELPAYRRQAVLDHcVARFRER-FDELAEALCIEAGKP 102
Cdd:cd07143 21 GGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDwgLKVSGSKRGRCLSK-LADLMERnLDYLASIEALDNGKT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 103 IND-SRGEVTRLIDTFRVASEEAVRIDGEVLNLEISARAqgytgYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCP 181
Cdd:cd07143 100 FGTaKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLT-----YTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 182 FVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAH-RDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK---KKVVLE 257
Cdd:cd07143 175 IVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYgRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsnlKKVTLE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 258 LGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPM 335
Cdd:cd07143 255 LGGKSPNIVfdDAD----LESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 336 ISESESRRLSGWMDAAVAAGAKIIAGGKV---DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSD 412
Cdd:cd07143 331 VSQIQYERIMSYIESGKAEGATVETGGKRhgnEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDST 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
5KF0_A 413 FGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVdNMPYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:cd07143 411 YGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHH-QVPFGGYKQSGIGRELGEYALENYTQ 473
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
68-476 |
2.28e-78 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 252.88 E-value: 2.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 68 LPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSR-GEVTRLIDTFRVASEEAVRIDGEVLNLEISARAqgytgY 146
Cdd:PRK13252 63 MTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFV-----Y 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 147 TRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTT 226
Cdd:PRK13252 138 TRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 227 DERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVH 302
Cdd:PRK13252 218 HPDIAKVSFTGGVPTGKKVMAAAAAslKEVTMELGGKSPLIVfdDAD----LDRAADIAMLANFYSSGQVCTNGTRVFVQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 303 ASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV-------DGAMFEATLLE 375
Cdd:PRK13252 294 KSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERlteggfaNGAFVAPTVFT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 376 DVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN---DVPSfrvdNM 452
Cdd:PRK13252 374 DCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINtwgESPA----EM 449
|
410 420
....*....|....*....|....
5KF0_A 453 PYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:PRK13252 450 PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
31-465 |
8.86e-76 |
|
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: 244.98 E-value: 8.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 31 VTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEV 110
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 111 TRLIDTFRVASEEAVRIDGEVLNLeisarAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRT 190
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPV-----GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 191 PVGALIIAEVLAETnLPKGAFSVLPAHRDGA-DLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV- 266
Cdd:cd07107 156 PLSALRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEgiKHVTLELGGKNALIVf 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 267 -DADqfeqLDYVVDRLAFGA-YYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRL 344
Cdd:cd07107 235 pDAD----PEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 345 SGWMDAAVAAGAKIIAGGKV-------DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQA 417
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRpegpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
5KF0_A 418 GVFTDSLTHAQRAWDELEVGGVVINDVpSFRVDNMPYGGVKDSGLGRE 465
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINGS-SRHFLGAPFGGVKNSGIGRE 437
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
57-483 |
1.70e-75 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 244.95 E-value: 1.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVK---PMRELPAYRRQAVLDHcVARFRER-FDELAEALCIEAGKPINDSR-GEVTRLIDTFRVASEEAVRIDGEV 131
Cdd:cd07141 52 AARAAFKlgsPWRTMDASERGRLLNK-LADLIERdRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 132 lnleISARAQGYTgYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAF 211
Cdd:cd07141 131 ----IPMDGDFFT-YTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 212 SVLP--AHRDGADLfTTDERFRLLSFTGSPAVGWALKEKAGK---KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFG 284
Cdd:cd07141 206 NVVPgyGPTAGAAI-SSHPDIDKVAFTGSTEVGKLIQQAAGKsnlKRVTLELGGKSPNIVfaDAD----LDYAVEQAHEA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 285 AYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV 364
Cdd:cd07141 281 LFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 365 ---DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVI 441
Cdd:cd07141 361 hgdKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWV 440
|
410 420 430 440
....*....|....*....|....*....|....*....|..
5KF0_A 442 NDVPSFRVdNMPYGGVKDSGLGREGIRYAIEDMTEPRLMVVR 483
Cdd:cd07141 441 NCYNVVSP-QAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
68-467 |
1.76e-75 |
|
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: 244.14 E-value: 1.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 68 LPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIdgevlnLEISARAQGYTGYT 147
Cdd:cd07101 37 RPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERL------LKPRRRRGAIPVLT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 148 R----RVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVL--------P 215
Cdd:cd07101 111 RttvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVtgpgsevgG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHRDGADLfttderfrlLSFTGSPAVGWALKEKAGKKKV--VLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07101 191 AIVDNADY---------VMFTGSTATGRVVAERAGRRLIgcSLELGGKNPMIVleDAD----LDKAAAGAVRACFSNAGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK----VDGA 367
Cdd:cd07101 258 LCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRarpdLGPY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 368 MFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIND--VP 445
Cdd:cd07101 338 FYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEgyAA 417
|
410 420
....*....|....*....|....*.
5KF0_A 446 SFRVDNMPYGGVKDSGLGR----EGI 467
Cdd:cd07101 418 AWASIDAPMGGMKDSGLGRrhgaEGL 443
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
25-484 |
1.29e-73 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 241.32 E-value: 1.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 25 ANTDLEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDhcvaRFR----ERFDELAEALCIEAG 100
Cdd:PRK09407 30 AGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLL----RFHdlvlENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 101 KPINDSRGEVTRLIDTFRVASEEAVRIdgevlnLEISARAQGYTGYTR----RVPIGPCSFISPFNFPLNLAAHKVAPAL 176
Cdd:PRK09407 106 KARRHAFEEVLDVALTARYYARRAPKL------LAPRRRAGALPVLTKttelRQPKGVVGVISPWNYPLTLAVSDAIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 177 AAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAhrDGADLFTT-DERFRLLSFTGSPAVGWALKEKAGKKKV- 254
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTG--PGPVVGTAlVDNADYLMFTGSTATGRVLAEQAGRRLIg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 255 -VLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTF 331
Cdd:PRK09407 258 fSLELGGKNPMIVldDAD----LDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSAD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 332 VGPMISESESRRLSGWMDAAVAAGAKIIAGGK----VDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALAR 407
Cdd:PRK09407 334 MGSLISEAQLETVSAHVDDAVAKGATVLAGGKarpdLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVER 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 408 VNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIND--VPSFRVDNMPYGGVKDSGLGR----EGI-RYaiedmTEPRLM 480
Cdd:PRK09407 414 ANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgyAAAWGSVDAPMGGMKDSGLGRrhgaEGLlKY-----TESQTI 488
|
....
5KF0_A 481 VVRR 484
Cdd:PRK09407 489 ATQR 492
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
15-469 |
3.91e-72 |
|
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: 236.26 E-value: 3.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 15 PYYLANEAVYANTD--LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELA 92
Cdd:cd07085 2 KLFINGEWVESKTTewLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 93 EALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEvlNLEISARaqGYTGYTRRVPIGPCSFISPFNFPLNLAAHKV 172
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGE--YLENVAR--GIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 173 APALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGKK 252
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 253 -KVVLELGG--NAAAIV-DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDP 328
Cdd:cd07085 238 gKRVQALGGakNHAVVMpDAD----LEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 329 STFVGPMISESESRRLSGWMDAAVAAGAKIIAGG---KV----DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRF 401
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvKVpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5KF0_A 402 DDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN-----DVPSFrvdnmPYGGVKDSGLG------REGIRY 469
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpipvPLAFF-----SFGGWKGSFFGdlhfygKDGVRF 467
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
29-465 |
9.10e-72 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 235.32 E-value: 9.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:cd07559 18 FDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 -EVTRLIDTFR-----VASEE--AVRIDGEVLNleisaraqgytgYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGC 180
Cdd:cd07559 98 aDIPLAIDHFRyfagvIRAQEgsLSEIDEDTLS------------YHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 181 PFVLKPASRTPVGALIIAEVLAETnLPKGAFSVL--PAHRDGADLFTTDeRFRLLSFTGSPAVGWALKEKAGKK--KVVL 256
Cdd:cd07559 166 TVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVtgFGSEAGKPLASHP-RIAKLAFTGSTTVGRLIMQYAAENliPVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 257 ELGGNAAAIVDADQFEQLDYVVDRL---AFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVG 333
Cdd:cd07559 244 ELGGKSPNIFFDDAMDADDDFDDKAeegQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 334 PMISESESRRLSGWMDAAVAAGAKIIAGGK-------VDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALA 406
Cdd:cd07559 324 AQVSKDQLEKILSYVDIGKEEGAEVLTGGErltlgglDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
5KF0_A 407 RVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN---DVPSfrvdNMPYGGVKDSGLGRE 465
Cdd:cd07559 404 IANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcyhQYPA----HAPFGGYKKSGIGRE 461
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
29-481 |
9.16e-72 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 235.08 E-value: 9.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDA--VKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDS 106
Cdd:cd07142 21 FPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 107 R-GEVTRLIDTFRVASEEAVRIDGEVLNLEisaraQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLK 185
Cdd:cd07142 101 RyAEVPLAARLFRYYAGWADKIHGMTLPAD-----GPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 186 PASRTPVGALIIAEVLAETNLPKGAFSVLPAHRD--GADLFT---TDErfrlLSFTGSPAVGWALKEKAGK---KKVVLE 257
Cdd:cd07142 176 PAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPtaGAAIAShmdVDK----VAFTGSTEVGKIIMQLAAKsnlKPVTLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 258 LGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPM 335
Cdd:cd07142 252 LGGKSPFIVceDAD----VDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 336 ISESESRRLSGWMDAAVAAGAKIIAGGKV---DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSD 412
Cdd:cd07142 328 VDKEQFEKILSYIEHGKEEGATLITGGDRigsKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSK 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5KF0_A 413 FGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDnMPYGGVKDSGLGREGIRYAIEDMTEPRLMV 481
Cdd:cd07142 408 YGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDAS-IPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
56-468 |
3.05e-71 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 233.48 E-value: 3.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 56 GAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAvridGEVLNLE 135
Cdd:PRK09406 30 ARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHA----EALLADE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 136 IS-ARAQGYT-GYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSV 213
Cdd:PRK09406 106 PAdAAAVGASrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 214 LPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQS 289
Cdd:PRK09406 186 LLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDeiKKTVLELGGSDPFIVmpSAD----LDRAAETAVTARVQNN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 290 GQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---DG 366
Cdd:PRK09406 262 GQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRpdgPG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 367 AMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIND-VP 445
Cdd:PRK09406 342 WFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGmTV 421
|
410 420
....*....|....*....|....*..
5KF0_A 446 SFrvDNMPYGGVKDSGLGRE----GIR 468
Cdd:PRK09406 422 SY--PELPFGGVKRSGYGRElsahGIR 446
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
14-476 |
1.13e-70 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 232.34 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 14 YPYYLANEAVYANTD--LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDEL 91
Cdd:cd07117 1 YGLFINGEWVKGSSGetIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 92 AEALCIEAGKPINDSRG-EVTRLIDTFR-----VASEE--AVRIDGEVLNLeisaraqgytgyTRRVPIGPCSFISPFNF 163
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRyfagvIRAEEgsANMIDEDTLSI------------VLREPIGVVGQIIPWNF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 164 PLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETnLPKGAFSVLPAH--RDGADLFTTDErFRLLSFTGSPAV 241
Cdd:cd07117 149 PFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgsKSGEYLLNHPG-LDKLAFTGSTEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 242 GWALKEKAGKKKV--VLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKT 317
Cdd:cd07117 227 GRDVAIAAAKKLIpaTLELGGKSANIIfdDAN----WDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 318 RSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK-------VDGAMFEATLLEDVGREQDLYRKEAFG 390
Cdd:cd07117 303 ENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHrltenglDKGFFIEPTLIVNVTNDMRVAQEEIFG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 391 PVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN---DVPSfrvdNMPYGGVKDSGLGREGI 467
Cdd:cd07117 383 PVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNtynQIPA----GAPFGGYKKSGIGRETH 458
|
....*....
5KF0_A 468 RYAIEDMTE 476
Cdd:cd07117 459 KSMLDAYTQ 467
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
82-463 |
1.22e-70 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 230.39 E-value: 1.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 82 ARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNleiSARAqGYTGYTRRVPIGPCSFISPF 161
Cdd:PRK10090 6 AGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQ---SDRP-GENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 162 NFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVL--PAHRDGADLfTTDERFRLLSFTGSP 239
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVlgRGETVGQEL-AGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 240 AVGWALKEKAGKK--KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVA 315
Cdd:PRK10090 161 SAGEKIMAAAAKNitKVCLELGGKAPAIVmdDAD----LDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 316 KTRSLKMGDPKDPSTF-VGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---DGAMFEATLLEDVGREQDLYRKEAFGP 391
Cdd:PRK10090 237 AMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAvegKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
5KF0_A 392 VAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDvPSFRVDNMPYGGVKDSGLG 463
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR-ENFEAMQGFHAGWRKSGIG 387
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
69-482 |
7.50e-70 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 230.80 E-value: 7.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 69 PAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRI--DGEVLNLEiSARAQGYTGY 146
Cdd:PLN00412 73 PLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRIlgEGKFLVSD-SFPGNERNKY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 147 --TRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAH-RDGADL 223
Cdd:PLN00412 152 clTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 224 FTTDERFRLLSFTGSPAvGWALKEKAGKKKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILV 301
Cdd:PLN00412 232 LTMHPGVNCISFTGGDT-GIAISKKAGMVPLQMELGGKDACIVleDAD----LDLAAANIIKGGFSYSGQRCTAVKVVLV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 302 HASLYDTLRDKLVAKTRSLKMGDPKDPSTfVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVDGAMFEATLLEDVGREQ 381
Cdd:PLN00412 307 MESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNLIWPLLLDNVRPDM 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 382 DLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDNMPYGGVKDSG 461
Cdd:PLN00412 386 RIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSG 465
|
410 420
....*....|....*....|.
5KF0_A 462 LGREGIRYAIEDMTEPRLMVV 482
Cdd:PLN00412 466 IGSQGITNSINMMTKVKSTVI 486
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
73-465 |
1.36e-69 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 230.39 E-value: 1.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 73 RQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlNLEISARAQGYTGYTRRVPI 152
Cdd:PLN02467 74 RAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQ-KAPVSLPMETFKGYVLKEPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 153 GPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP--AHRDGADLfTTDERF 230
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTglGTEAGAPL-ASHPGV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 231 RLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLY 306
Cdd:PLN02467 232 DKIAFTGSTATGRKIMTAAAQmvKPVSLELGGKSPIIVfdDVD----LDKAVEWAMFGCFWTNGQICSATSRLLVHERIA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 307 DTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK-----VDGAMFEATLLEDVGREQ 381
Cdd:PLN02467 308 SEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpehlKKGFFIEPTIITDVTTSM 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 382 DLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN-DVPSFrvDNMPYGGVKDS 460
Cdd:PLN02467 388 QIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINcSQPCF--CQAPWGGIKRS 465
|
....*
5KF0_A 461 GLGRE 465
Cdd:PLN02467 466 GFGRE 470
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
70-465 |
7.89e-68 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 224.36 E-value: 7.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 70 AYRRQAVLDHCVArFRERFDELAEALCIEAGKPINDSRGEVTR---LIDTFrvASEEAVRIDGEVLNLEisaRAQGYTGY 146
Cdd:PRK13968 51 DYRAQKLRDIGKA-LRARSEEMAQMITREMGKPINQARAEVAKsanLCDWY--AEHGPAMLKAEPTLVE---NQQAVIEY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 147 TrrvPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTT 226
Cdd:PRK13968 125 R---PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 227 DERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVH 302
Cdd:PRK13968 202 DSRIAAVTVTGSVRAGAAIGAQAGAalKKCVLELGGSDPFIVlnDAD----LELAVKAAVAGRYQNTGQVCAAAKRFIIE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 303 ASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGG-KVDGA--MFEATLLEDVGR 379
Cdd:PRK13968 278 EGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGeKIAGAgnYYAPTVLANVTP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 380 EQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIN--DVPSFRVdnmPYGGV 457
Cdd:PRK13968 358 EMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINgyCASDARV---AFGGV 434
|
....*...
5KF0_A 458 KDSGLGRE 465
Cdd:PRK13968 435 KKSGFGRE 442
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
30-465 |
2.07e-66 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 222.00 E-value: 2.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 30 EVTDKFSGKVATRVALADAQAIDAAIGAAVDAVK--PMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSR 107
Cdd:PLN02766 39 ETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 108 G-EVTRLIDTFRVASEEAVRIDGEVLNLeisarAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKP 186
Cdd:PLN02766 119 AvDIPAAAGLLRYYAGAADKIHGETLKM-----SRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 187 ASRTPVGALIIAEVLAETNLPKGAFSVLPAH--RDGADLfTTDERFRLLSFTGSPAVGWALKEKAGK---KKVVLELGGN 261
Cdd:PLN02766 194 AEQTPLSALFYAHLAKLAGVPDGVINVVTGFgpTAGAAI-ASHMDVDKVSFTGSTEVGRKIMQAAATsnlKQVSLELGGK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 262 AAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISES 339
Cdd:PLN02766 273 SPLLIfdDAD----VDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 340 ESRRLSGWMDAAVAAGAKIIAGGKV---DGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQ 416
Cdd:PLN02766 349 QFEKILSYIEHGKREGATLLTGGKPcgdKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLA 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
5KF0_A 417 AGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVDnMPYGGVKDSGLGRE 465
Cdd:PLN02766 429 AGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPD-CPFGGYKMSGFGRD 476
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
57-465 |
8.17e-65 |
|
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: 216.69 E-value: 8.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNlei 136
Cdd:cd07130 42 AAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIP--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAqGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGAL----IIAEVLAETNLPKGAFS 212
Cdd:cd07130 119 SERP-GHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIAS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 213 VLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQ 288
Cdd:cd07130 198 LVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARfgRSLLELGGNNAIIVmeDAD----LDLAVRAVLFAAVGT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 289 SGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---D 365
Cdd:cd07130 274 AGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVidgP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 366 GAMFEATLLEdvGREQD-LYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDEL---------- 434
Cdd:cd07130 354 GNYVEPTIVE--GLSDApIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsdcgivnvn 431
|
410 420 430
....*....|....*....|....*....|....*..
5KF0_A 435 ------EVGGVvindvpsfrvdnmpYGGVKDSGLGRE 465
Cdd:cd07130 432 igtsgaEIGGA--------------FGGEKETGGGRE 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
114-465 |
9.97e-65 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 216.98 E-value: 9.97e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 114 IDTFRVASEEAVRIDGEVLNLEiSARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVG 193
Cdd:cd07140 111 IQTFRYFAGWCDKIQGKTIPIN-QARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 194 ALIIAEVLAETNLPKGAFSVLP-AHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK---KKVVLELGGNAAAIVDAD 269
Cdd:cd07140 190 ALKFAELTVKAGFPKGVINILPgSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVsnlKKVSLELGGKSPLIIFAD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 270 QfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMD 349
Cdd:cd07140 270 C--DMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 350 AAVAAGAKIIAGGK-VD--GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDR--FDDALARVNDSDFGLQAGVFTDSL 424
Cdd:cd07140 348 RGVKEGATLVYGGKqVDrpGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDI 427
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
5KF0_A 425 THAQRAWDELEVGGVVIN-----DVPSfrvdnmPYGGVKDSGLGRE 465
Cdd:cd07140 428 NKALYVSDKLEAGTVFVNtynktDVAA------PFGGFKQSGFGKD 467
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
57-461 |
4.95e-64 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 215.95 E-value: 4.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRI-DGE-VLNL 134
Cdd:PRK03137 81 AALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLaDGKpVESR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 135 EisaraqGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVL 214
Cdd:PRK03137 161 P------GEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFV 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 215 PAhrDGA---DLFTTDERFRLLSFTGSPAVGWALKEKAGK--------KKVVLELGGNAAAIVDADQfeQLDYVVDRLAF 283
Cdd:PRK03137 235 PG--SGSevgDYLVDHPKTRFITFTGSREVGLRIYERAAKvqpgqiwlKRVIAEMGGKDAIVVDEDA--DLDLAAESIVA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 284 GAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPsTFVGPMISESESRRLSGWMDAAVAAGaKIIAGGK 363
Cdd:PRK03137 311 SAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 364 VD---GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVV 440
Cdd:PRK03137 389 GDdskGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLY 468
|
410 420
....*....|....*....|....*..
5KF0_A 441 INdvpsfR------VDNMPYGGVKDSG 461
Cdd:PRK03137 469 FN-----RgctgaiVGYHPFGGFNMSG 490
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
72-468 |
3.44e-61 |
|
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: 207.15 E-value: 3.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 72 RRQAVLDHCVARFRERFDELAEALCIEAGKPIND-SRGEVTRLIDTFRVASEEavridGEVlNLEISARAQGY-TGYTR- 148
Cdd:cd07098 41 ERRKVLRSLLKYILENQEEICRVACRDTGKTMVDaSLGEILVTCEKIRWTLKH-----GEK-ALRPESRPGGLlMFYKRa 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 149 RV---PIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGAL----IIAEVLAETNLPKGAFSVLPAHRDGA 221
Cdd:cd07098 115 RVeyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPETA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 222 DLFTTDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQ 297
Cdd:cd07098 195 EALTSHPVIDHITFIGSPPVGKKVMAAAAESltPVVLELGGKDPAIVldDAD----LDQIASIIMRGTFQSSGQNCIGIE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 298 RILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK-------VDGAMFE 370
Cdd:cd07098 271 RVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKryphpeyPQGHYFP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 371 ATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDV-PSFRV 449
Cdd:cd07098 351 PTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgVNYYV 430
|
410 420
....*....|....*....|...
5KF0_A 450 DNMPYGGVKDSGLGR----EGIR 468
Cdd:cd07098 431 QQLPFGGVKGSGFGRfageEGLR 453
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
57-471 |
1.07e-59 |
|
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: 202.12 E-value: 1.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRlidtfrVASEEAVRIDG--EVLNL 134
Cdd:cd07095 8 AARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAA------MAGKIDISIKAyhERTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 135 EISARAQGyTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVL 214
Cdd:cd07095 82 RATPMAQG-RAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 215 PAHRDGADLFTTDERFRLLSFTGSPAVGWALKEK-AGK--KKVVLELGGNAAAIVDADqfEQLDYVVDRLAFGAYYQSGQ 291
Cdd:cd07095 161 QGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRpgKILALEMGGNNPLVVWDV--ADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLY-DTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK--VDGAM 368
Cdd:cd07095 239 RCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMErlVAGTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 369 FEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFR 448
Cdd:cd07095 319 FLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA 398
|
410 420
....*....|....*....|...
5KF0_A 449 VDNMPYGGVKDSGLGREGIRYAI 471
Cdd:cd07095 399 SSTAPFGGVGLSGNHRPSAYYAA 421
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
26-476 |
3.43e-59 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 202.43 E-value: 3.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 26 NTDLEVTDKFSGKVATRVALadaqaidaaiGAAVD---AVKPMREL----------PAyRRQAVLDHCVARFRERFDELA 92
Cdd:PRK09847 34 NETFETVDPVTQAPLAKIAR----------GKSVDidrAVSAARGVfergdwslssPA-KRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 93 EALCIEAGKPINDS-RGEVTRLIDTFRVASEEAVRIDGEVlnleiSARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHK 171
Cdd:PRK09847 103 LLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEV-----ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 172 VAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP--AHRDGADLFTTDErFRLLSFTGSPAVGWALKEKA 249
Cdd:PRK09847 178 LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTgfGHEAGQALSRHND-IDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 250 GK---KKVVLELGGNAAAIVDADqFEQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPK 326
Cdd:PRK09847 257 GDsnmKRVWLEAGGKSANIVFAD-CPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 327 DPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVD-GAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDAL 405
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGlAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5KF0_A 406 ARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDvpsFRVDNM--PYGGVKDSGLGREGIRYAIEDMTE 476
Cdd:PRK09847 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN---YNDGDMtvPFGGYKQSGNGRDKSLHALEKFTE 485
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
151-480 |
1.15e-56 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 195.31 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 151 PIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTTDERF 230
Cdd:cd07111 147 PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 231 RLLSFTGSPAVGWAL-KEKAG-KKKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLY 306
Cdd:cd07111 227 DKVAFTGSTEVGRALrRATAGtGKKLSLELGGKSPFIVfdDAD----LDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 307 DTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---DGAMFEATLLEDVGREQDL 383
Cdd:cd07111 303 EELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADlpsKGPFYPPTLFTNVPPASRI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 384 YRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVdNMPYGGVKDSGLG 463
Cdd:cd07111 383 AQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDA-AAGFGGYRESGFG 461
|
330
....*....|....*..
5KF0_A 464 REGIRYAIEDMTEPRLM 480
Cdd:cd07111 462 REGGKEGLYEYLRPSWE 478
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
84-464 |
1.71e-56 |
|
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: 193.51 E-value: 1.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 84 FRERFDELAEALCIEAGKPindsrGEVTRLIDTFRVASEeavrIDGEVLNL---------EISARAQGYTGYTRRVPIGP 154
Cdd:cd07087 33 LTENEEEIAAALYADLGKP-----PAEAYLTEIAVVLGE----IDHALKHLkkwmkprrvSVPLLLQPAKAYVIPEPLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 155 CSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETnLPKGAFSVLPAhrdGADLFT--TDERFRL 232
Cdd:cd07087 104 VLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG---GVEVATalLAEPFDH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 233 LSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTLR 310
Cdd:cd07087 180 IFFTGSPAVGKIVMEAAAKHltPVTLELGGKSPCIVDKDA--NLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 311 DKLVAKTRSLkMGDPKDPSTFVGPMISESESRRLSGWMDaavaaGAKIIAGGKVDGA--MFEATLLEDVGREQDLYRKEA 388
Cdd:cd07087 258 EELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLD-----DGKVVIGGQVDKEerYIAPTILDDVSPDSPLMQEEI 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5KF0_A 389 FGPV-AILEkFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPS-FRVDNMPYGGVKDSGLGR 464
Cdd:cd07087 332 FGPIlPILT-YDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhAAIPNLPFGGVGNSGMGA 408
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
64-481 |
3.88e-55 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 192.72 E-value: 3.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 64 PMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG-EVTRLIDTFRVASEEAVRIDGevlnleISARAQG 142
Cdd:PLN02466 112 PWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHG------LTVPADG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 143 -YTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAH--RD 219
Cdd:PLN02466 186 pHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFgpTA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 220 GADL---FTTDErfrlLSFTGSPAVGWALKEKAGK---KKVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQSGQ 291
Cdd:PLN02466 266 GAALashMDVDK----LAFTGSTDTGKIVLELAAKsnlKPVTLELGGKSPFIVceDAD----VDKAVELAHFALFFNQGQ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 292 SCIGVQRILVHASLYDTLRDKlvAKTRSLK--MGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK---VDG 366
Cdd:PLN02466 338 CCCAGSRTFVHERVYDEFVEK--AKARALKrvVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDrfgSKG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 367 AMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPS 446
Cdd:PLN02466 416 YYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDV 495
|
410 420 430
....*....|....*....|....*....|....*
5KF0_A 447 FRVdNMPYGGVKDSGLGREGIRYAIEDMTEPRLMV 481
Cdd:PLN02466 496 FDA-AIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
57-463 |
7.17e-52 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 183.16 E-value: 7.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlnlEI 136
Cdd:cd07083 63 AAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPA---VE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPA 216
Cdd:cd07083 140 VVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 217 hrDGA---DLFTTDERFRLLSFTGSPAVGWALKEKAGK--------KKVVLELGGNAAAIVDADQfeQLDYVVDRLAFGA 285
Cdd:cd07083 220 --VGEevgAYLTEHERIRGINFTGSLETGKKIYEAAARlapgqtwfKRLYVETGGKNAIIVDETA--DFELVVEGVVVSA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 286 YYQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGaKIIAGGKVD 365
Cdd:cd07083 296 FGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 366 ---GAMFEATLLEDVGREQDLYRKEAFGPV--AILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVV 440
Cdd:cd07083 375 egeGYFVAPTVVEEVPPKARIAQEEIFGPVlsVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLY 454
|
410 420
....*....|....*....|....
5KF0_A 441 IND-VPSFRVDNMPYGGVKDSGLG 463
Cdd:cd07083 455 INRkITGALVGVQPFGGFKLSGTN 478
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
84-478 |
3.33e-51 |
|
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: 179.72 E-value: 3.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 84 FRERFDELAEALCIEAGKPINDSR-GEVTRLIDTF--------RVASEEAVRiDGEVLNLEISARaqgytgyTRRVPIGP 154
Cdd:cd07135 40 VKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDIlhmlknlkKWAKDEKVK-DGPLAFMFGKPR-------IRKEPLGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 155 CSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEvLAETNLPKGAFSVLpahrDGADLFTT---DERFR 231
Cdd:cd07135 112 VLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE-LVPKYLDPDAFQVV----QGGVPETTallEQKFD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 232 LLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDTL 309
Cdd:cd07135 187 KIFYTGSGRVGRIIAEAAAKHltPVTLELGGKSPVIVTKNA--DLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 310 RDKLVAKTRSLKMGDPKDPSTFvGPMISESESRRLSGWMDaavAAGAKIIAGGKVDGA--MFEATLLEDVGREQDLYRKE 387
Cdd:cd07135 265 VEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKSLLD---TTKGKVVIGGEMDEAtrFIPPTIVSDVSWDDSLMSEE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 388 AFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDV-PSFRVDNMPYGGVKDSGLGREG 466
Cdd:cd07135 341 LFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTlIHVGVDNAPFGGVGDSGYGAYH 420
|
410
....*....|..
5KF0_A 467 IRYAIEDMTEPR 478
Cdd:cd07135 421 GKYGFDTFTHER 432
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
36-466 |
5.49e-49 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 174.95 E-value: 5.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 36 SGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG-EVTRLI 114
Cdd:cd07116 25 TGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAaDIPLAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 115 DTFRV------ASEEAV-RIDGEVLNLEISAraqgytgytrrvPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPA 187
Cdd:cd07116 105 DHFRYfagcirAQEGSIsEIDENTVAYHFHE------------PLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 188 SRTPVGALIIAEVLAETnLPKGAFSVL--PAHRDGADLFTTDeRFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAA 263
Cdd:cd07116 173 EQTPASILVLMELIGDL-LPPGVVNVVngFGLEAGKPLASSK-RIAKVAFTGETTTGRLIMQYASENiiPVTLELGGKSP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 264 AIVDADQFEQLDYVVDRLAFGAY---YQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESE 340
Cdd:cd07116 251 NIFFADVMDADDAFFDKALEGFVmfaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 341 SRRLSGWMDAAVAAGAKIIAGGK-------VDGAMFEATLLEDvGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDF 413
Cdd:cd07116 331 LEKILSYIDIGKEEGAEVLTGGErnelgglLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLY 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
5KF0_A 414 GLQAGVFTDSLTHAQRAWDELEVGGVVINDVPSFRVdNMPYGGVKDSGLGREG 466
Cdd:cd07116 410 GLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPA-HAAFGGYKQSGIGREN 461
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
29-445 |
2.46e-47 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 173.01 E-value: 2.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 29 LEVTDKFSGKVATRVALADAQAIDAAIGAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRG 108
Cdd:PLN02419 131 IDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 109 EVTRLIDTFRVASEEAVRIDGEVLnleiSARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPAS 188
Cdd:PLN02419 211 DIFRGLEVVEHACGMATLQMGEYL----PNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 189 RTPVGALIIAEVLAETNLPKGAFSVLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIV 266
Cdd:PLN02419 287 KDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAkgKRIQSNMGAKNHGLV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 267 DADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRIlVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSG 346
Cdd:PLN02419 367 LPDA--NIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 347 WMDAAVAAGAK-------IIAGGKVDGAMFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGV 419
Cdd:PLN02419 444 LIQSGVDDGAKllldgrdIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAI 523
|
410 420
....*....|....*....|....*.
5KF0_A 420 FTDSLTHAQRAWDELEVGGVVINdVP 445
Cdd:PLN02419 524 FTSSGAAARKFQMDIEAGQIGIN-VP 548
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
65-464 |
3.86e-47 |
|
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: 168.94 E-value: 3.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 65 MRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPindsRGEVtRLIDTFRVASEeavrIDGEVLNLEISARAQ--- 141
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP----AAEV-DLTEILPVLSE----INHAIKHLKKWMKPKrvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 142 ------GYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVlp 215
Cdd:cd07134 85 tplllfGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVF-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 ahRDGADLFT--TDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIVD--ADqfeqLDYVVDRLAFGAYYQS 289
Cdd:cd07134 163 --EGDAEVAQalLELPFDHIFFTGSPAVGKIVMAAAAKHlaSVTLELGGKSPTIVDetAD----LKKAAKKIAWGKFLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 290 GQSCIGVQRILVHASLYDTLRDKLVAKTRSL--KMGDPKDPSTFvGPMISESESRRLSGWMDAAVAAGAKIIAGGKVDGA 367
Cdd:cd07134 237 GQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASPDL-ARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 368 --MFEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVP 445
Cdd:cd07134 316 qrYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVV 395
|
410 420
....*....|....*....|
5KF0_A 446 SFRVD-NMPYGGVKDSGLGR 464
Cdd:cd07134 396 LHFLNpNLPFGGVNNSGIGS 415
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
145-464 |
1.81e-46 |
|
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: 167.30 E-value: 1.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 145 GYTRRVPIGPCSFISPFNFPLNLAahkVAP---ALAAGCPFVLKPASRTPVGALIIAEVLAETnLPKGAFSVLPAHRDGA 221
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 222 DlFTTDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRI 299
Cdd:cd07136 170 Q-ELLDQKFDYIFFTGSVRVGKIVMEAAAKHltPVTLELGGKSPCIVDEDA--NLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 300 LVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFvGPMISESESRRLSGWMDaavaaGAKIIAGGKVDGA--MFEATLLEDV 377
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLD-----NGKIVFGGNTDREtlYIEPTILDNV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 378 GREQDLYRKEAFGPV-AILEkFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIND-VPSFRVDNMPYG 455
Cdd:cd07136 321 TWDDPVMQEEIFGPIlPVLT-YDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDtIMHLANPYLPFG 399
|
....*....
5KF0_A 456 GVKDSGLGR 464
Cdd:cd07136 400 GVGNSGMGS 408
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
57-463 |
1.39e-45 |
|
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: 166.22 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLnlei 136
Cdd:cd07125 77 IAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPE---- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 sarAQGYTGYTRRV---PIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSV 213
Cdd:cd07125 153 ---LPGPTGELNGLelhGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 214 LPAhrDGADL---FTTDERFRLLSFTGSPAVGWA-LKEKAGKK----KVVLELGGNAAAIVD--ADQfEQLdyVVDRL-- 281
Cdd:cd07125 230 VPG--DGEEIgeaLVAHPRIDGVIFTGSTETAKLiNRALAERDgpilPLIAETGGKNAMIVDstALP-EQA--VKDVVqs 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 282 AFGAyyqSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSG---WMDAAvaagAKI 358
Cdd:cd07125 305 AFGS---AGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAhteLMRGE----AWL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 359 IAGGKVD---GAMFEATLLEDVGreQDLYRKEAFGPVAILEKFDRF--DDALARVNDSDFGLQAGVFT-DSLTHAQraW- 431
Cdd:cd07125 378 IAPAPLDdgnGYFVAPGIIEIVG--IFDLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSrDEREIEY--Wr 453
|
410 420 430 440
....*....|....*....|....*....|....*....|
5KF0_A 432 DELEVGGVVINdvpsfRvdNM--------PYGGVKDSGLG 463
Cdd:cd07125 454 ERVEAGNLYIN-----R--NItgaivgrqPFGGWGLSGTG 486
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
57-470 |
6.07e-41 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 153.19 E-value: 6.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIdtfrvaseeavridGEVlnlEI 136
Cdd:PRK09457 45 AARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMI--------------NKI---AI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARA-QGYTGYTRRV-----------PIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAET 204
Cdd:PRK09457 108 SIQAyHERTGEKRSEmadgaavlrhrPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 205 NLPKGAFSVLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEK-AGK--KKVVLELGGNAAAIVdaDQFEQLDYVVDRL 281
Cdd:PRK09457 188 GLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQfAGQpeKILALEMGGNNPLVI--DEVADIDAAVHLI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 282 AFGAYYQSGQSCIGVQRILVHASLY-DTLRDKLVAKTRSLKMGDP-KDPSTFVGPMISESESRRLsgwmdaaVAAGAKII 359
Cdd:PRK09457 266 IQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWdAEPQPFMGAVISEQAAQGL-------VAAQAQLL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 360 A-GGKvdgAMFEATLLE-----------DVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHA 427
Cdd:PRK09457 339 AlGGK---SLLEMTQLQagtglltpgiiDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDY 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
5KF0_A 428 QRAWDELEVGGV----VINDVPSfrvdNMPYGGVKDSGLGREGIRYA 470
Cdd:PRK09457 416 DQFLLEIRAGIVnwnkPLTGASS----AAPFGGVGASGNHRPSAYYA 458
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
57-421 |
8.60e-41 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 153.07 E-value: 8.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlnleI 136
Cdd:PLN02315 64 ACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSI----I 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 SARAQGYTGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGAL----IIAEVLAETNLPKGAFS 212
Cdd:PLN02315 140 PSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 213 VLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYYQ 288
Cdd:PLN02315 220 SFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARfgKCLLELSGNNAIIVmdDAD----IQLAVRSVLFAAVGT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 289 SGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKV---D 365
Cdd:PLN02315 296 AGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAiesE 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
5KF0_A 366 GAMFEATLLEdVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFT 421
Cdd:PLN02315 376 GNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT 430
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
65-478 |
1.35e-40 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 152.11 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 65 MRELPAyrRQAVLDHCVARFRERFDELAEALCIEAGKP--------INDSRGEVTRLIDTF-RVASEEAVriDGEVLNLE 135
Cdd:PTZ00381 25 TRPLEF--RKQQLRNLLRMLEENKQEFSEAVHKDLGRHpfetkmteVLLTVAEIEHLLKHLdEYLKPEKV--DTVGVFGP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 136 ISaraqgytGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLaeTN-LPKGAFSVL 214
Cdd:PTZ00381 101 GK-------SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL--TKyLDPSYVRVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 215 pahRDGADLFT--TDERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSG 290
Cdd:PTZ00381 172 ---EGGVEVTTelLKEPFDHIFFTGSPRVGKLVMQAAAENltPCTLELGGKSPVIVDKSC--NLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 291 QSCIGVQRILVHASLYDTLRDKLvAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDaavAAGAKIIAGGKVDGA--M 368
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGGEVDIEnkY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 369 FEATLLEDVGREQDLYRKEAFGPV-AILEkFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVpSF 447
Cdd:PTZ00381 323 VAPTIIVNPDLDSPLMQEEIFGPIlPILT-YENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDC-VF 400
|
410 420 430
....*....|....*....|....*....|...
5KF0_A 448 RV--DNMPYGGVKDSGLGREGIRYAIEDMTEPR 478
Cdd:PTZ00381 401 HLlnPNLPFGGVGNSGMGAYHGKYGFDTFSHPK 433
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
57-440 |
4.14e-37 |
|
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: 141.61 E-value: 4.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPiNDSRGEVTRLIDTFR-----VASEEAVRIDGEV 131
Cdd:cd07084 7 AADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRarafvIYSYRIPHEPGNH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 132 LNLEISARAQGYtgytrRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETN-LPKGA 210
Cdd:cd07084 86 LGQGLKQQSHGY-----RWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 211 FSVLPAHRDGADLFTTDERFRLLSFTGSPAVGWALKEKAGKKKVVLELGGNAAAIVDADQfEQLDYVVDRLAFGAYYQSG 290
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDA-QAVDYVAWQCVQDMTACSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 291 QSCIGVQRILVHAS-----LYDTLRDKLvaKTRSLKmgdpkdpSTFVGPMISES-----ESRRLSGWMDaaVAAGAKIIA 360
Cdd:cd07084 240 QKCTAQSMLFVPENwsktpLVEKLKALL--ARRKLE-------DLLLGPVQTFTtlamiAHMENLLGSV--LLFSGKELK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 361 GGKVD---GAMFEATLL---EDVGREQDLYRKEAFGPVAILEKF--DRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWD 432
Cdd:cd07084 309 NHSIPsiyGACVASALFvpiDEILKTYELVTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFLQELIG 388
|
....*...
5KF0_A 433 ELEVGGVV 440
Cdd:cd07084 389 NLWVAGRT 396
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
73-464 |
2.91e-36 |
|
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: 139.16 E-value: 2.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 73 RQAVLDHCVARFRERFDELAEALCIEAGkpiNDSRGEvTRLIDTFRVASEeavrIDGEVLNL---------EISARAQGY 143
Cdd:cd07133 22 RRDRLDRLKALLLDNQDALAEAISADFG---HRSRHE-TLLAEILPSIAG----IKHARKHLkkwmkpsrrHVGLLFLPA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 144 TGYTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPK------G------AF 211
Cdd:cd07133 94 KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDevavvtGgadvaaAF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 212 SVLPahrdgadlfttderFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAYY 287
Cdd:cd07133 174 SSLP--------------FDHLLFTGSTAVGRHVMRAAAENltPVTLELGGKSPAIIapDAD----LAKAAERIAFGKLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 288 QSGQSCIGVQRILVHASLYDTLRDKlvAKTRSLKM-GDPKDPSTFVGpMISESESRRLSGWMDAAVAAGAKII----AGG 362
Cdd:cd07133 236 NAGQTCVAPDYVLVPEDKLEEFVAA--AKAAVAKMyPTLADNPDYTS-IINERHYARLQGLLEDARAKGARVIelnpAGE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 363 KVDGAM-FEATLLEDVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVI 441
Cdd:cd07133 313 DFAATRkLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTI 392
|
410 420
....*....|....*....|....*
5KF0_A 442 NDVpSFRV--DNMPYGGVKDSGLGR 464
Cdd:cd07133 393 NDT-LLHVaqDDLPFGGVGASGMGA 416
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
151-464 |
2.07e-34 |
|
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: 134.08 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 151 PIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLaETNLPKGAFSVLPAhrdGADLFTT--DE 228
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEG---GVPETTAllEQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 229 RFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAY-YQSGQSCIGVQRILVHASL 305
Cdd:cd07137 177 KWDKIFFTGSPRVGRIIMAAAAKhlTPVTLELGGKCPVIVDSTV--DLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 306 YDTLRDKLVAKTRSLKMGDPKDpSTFVGPMISESESRRLSGWMDAAVAAgAKIIAGGKVD--GAMFEATLLEDVGREQDL 383
Cdd:cd07137 255 APTLIDALKNTLEKFFGENPKE-SKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERDekNLYIEPTILLDPPLDSSI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 384 YRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIND-VPSFRVDNMPYGGVKDSGL 462
Cdd:cd07137 333 MTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDtVVQYAIDTLPFGGVGESGF 412
|
..
5KF0_A 463 GR 464
Cdd:cd07137 413 GA 414
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
158-461 |
1.92e-33 |
|
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: 132.71 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 158 ISPFNFP---LNLAAhkvAPALAaGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAhrDGA---DLFTTDERFR 231
Cdd:cd07123 177 VSPFNFTaigGNLAG---APALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPG--DGPvvgDTVLASPHLA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 232 LLSFTGSPAVGWALKEKAGKK--------KVVLELGGNAAAIV--DADqfeqLDYVVDRLAFGAY-YQsGQSCIGVQRIL 300
Cdd:cd07123 251 GLHFTGSTPTFKSLWKQIGENldryrtypRIVGETGGKNFHLVhpSAD----VDSLVTATVRGAFeYQ-GQKCSAASRAY 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 301 VHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAA-GAKIIAGGKVD---GAMFEATLLED 376
Cdd:cd07123 326 VPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDdsvGYFVEPTVIET 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 377 VGREQDLYRKEAFGPVAILEKFD--RFDDALARVND-SDFGLQAGVFTDSLTHAQRAWDELE--VGGVVINDVPSFR-VD 450
Cdd:cd07123 406 TDPKHKLMTEEIFGPVLTVYVYPdsDFEETLELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAvVG 485
|
330
....*....|.
5KF0_A 451 NMPYGGVKDSG 461
Cdd:cd07123 486 QQPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
146-483 |
4.24e-33 |
|
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: 130.42 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 146 YTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETnLPKGAFSVLPAhrdGADLFT 225
Cdd:cd07132 95 YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKY-LDKECYPVVLG---GVEETT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 226 --TDERFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAYYQSGQSCIGVQRILV 301
Cdd:cd07132 171 elLKQRFDYIFYTGSTSVGKIVMQAAAKhlTPVTLELGGKSPCYVDKSC--DIDVAARRIAWGKFINAGQTCIAPDYVLC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 302 HASlydtLRDKLVAKTR-SLKM---GDPKDPSTFvGPMISESESRRLSGWMDaavaaGAKIIAGGKVDGA--MFEATLLE 375
Cdd:cd07132 249 TPE----VQEKFVEALKkTLKEfygEDPKESPDY-GRIINDRHFQRLKKLLS-----GGKVAIGGQTDEKerYIAPTVLT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 376 DVGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVPS-FRVDNMPY 454
Cdd:cd07132 319 DVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMhYTLDSLPF 398
|
330 340
....*....|....*....|....*....
5KF0_A 455 GGVKDSGLGREGIRYAIEDMTEPRLMVVR 483
Cdd:cd07132 399 GGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
56-463 |
1.20e-32 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 130.03 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 56 GAAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEvlnle 135
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 136 ISARaqgytgytrrvPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP 215
Cdd:TIGR01238 156 FSVE-----------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AHrdGADL---FTTDERFRLLSFTGSPAVGWALKEKAGKK-----KVVLELGGNAAAIVDADQF-EQLdyVVDRLAfGAY 286
Cdd:TIGR01238 225 GR--GADVgaaLTSDPRIAGVAFTGSTEVAQLINQTLAQRedapvPLIAETGGQNAMIVDSTALpEQV--VRDVLR-SAF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 287 YQSGQSCIGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVD- 365
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDs 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 366 -----GAMFEATLLEDvgREQDLYRKEAFGPVAILEKF--DRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGG 438
Cdd:TIGR01238 380 racqhGTFVAPTLFEL--DDIAELSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGN 457
|
410 420
....*....|....*....|....*.
5KF0_A 439 VVIN-DVPSFRVDNMPYGGVKDSGLG 463
Cdd:TIGR01238 458 CYVNrNQVGAVVGVQPFGGQGLSGTG 483
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
57-463 |
7.72e-31 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 126.85 E-value: 7.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAeALCI-EAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVLNLE 135
Cdd:PRK11904 593 AARAAFPAWSRTPVEERAAILERAADLLEANRAELI-ALCVrEAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLP 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 136 isaraqGYTG---YTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFS 212
Cdd:PRK11904 672 ------GPTGesnELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 213 VLPAhrDGADL---FTTDERFRLLSFTGSPAVGW----ALKEKAGkKKVVL--ELGGNAAAIVDAD-QFEQldyVVD--- 279
Cdd:PRK11904 746 LLPG--DGATVgaaLTADPRIAGVAFTGSTETARiinrTLAARDG-PIVPLiaETGGQNAMIVDSTaLPEQ---VVDdvv 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 280 RLAFGAyyqSGQSCiGVQRIL-VHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLS---GWMDAAvaag 355
Cdd:PRK11904 820 TSAFRS---AGQRC-SALRVLfVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDahiERMKRE---- 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 356 AKIIAGGKVD-----GAMFEATLLEdVGREQDLyRKEAFGPvaILE----KFDRFDDALARVNDSDFGLQAGVFTDSLTH 426
Cdd:PRK11904 892 ARLLAQLPLPagtenGHFVAPTAFE-IDSISQL-EREVFGP--ILHviryKASDLDKVIDAINATGYGLTLGIHSRIEET 967
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
5KF0_A 427 AQRAWDELEVGGVVINdvpsfRvdNM--------PYGGVKDSGLG 463
Cdd:PRK11904 968 ADRIADRVRVGNVYVN-----R--NQigavvgvqPFGGQGLSGTG 1005
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
151-485 |
6.97e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 119.06 E-value: 6.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 151 PIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAeTNLPKGAFSVLpahRDGADLFTT--DE 228
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVI---EGGPAVGEQllQH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 229 RFRLLSFTGSPAVGWALKEKAGK--KKVVLELGGNAAAIVDA-DQFEQLDYVVDRLAFGAYYQ-SGQSCIGVQRILVHAS 304
Cdd:PLN02203 184 KWDKIFFTGSPRVGRIIMTAAAKhlTPVALELGGKCPCIVDSlSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 305 LYDTLRDKLVAKTRSLKMGDPKDPSTfVGPMISESESRRLSGWM-DAAVAagAKIIAGGKVD-GAMF-EATLLEDVGREQ 381
Cdd:PLN02203 264 FAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLkDPRVA--ASIVHGGSIDeKKLFiEPTILLNPPLDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 382 DLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVIND-VPSFRVDNMPYGGVKDS 460
Cdd:PLN02203 341 DIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDaIIQYACDSLPFGGVGES 420
|
330 340
....*....|....*....|....*
5KF0_A 461 GLGREGIRYAIeDMTEPRLMVVRRR 485
Cdd:PLN02203 421 GFGRYHGKYSF-DTFSHEKAVLRRS 444
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
69-463 |
3.09e-27 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 116.12 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 69 PAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEvlnleisaraqgytgyTR 148
Cdd:PRK11905 610 PAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNG----------------PG 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 149 RVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAhrDGADL---FT 225
Cdd:PRK11905 674 HKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPG--DGRTVgaaLV 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 226 TDERFRLLSFTGSPAVGW----ALKEKAGkKKVVL--ELGGNAAAIVDADQF-EQldyVVDRLAFGAYYQSGQSCIGVqR 298
Cdd:PRK11905 752 ADPRIAGVMFTGSTEVARliqrTLAKRSG-PPVPLiaETGGQNAMIVDSSALpEQ---VVADVIASAFDSAGQRCSAL-R 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 299 IL-----VHASLYDTLRDKLvaktRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKI---IAGGKVDGAMFE 370
Cdd:PRK11905 827 VLclqedVADRVLTMLKGAM----DELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhqlPLPAETEKGTFV 902
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 371 A-TLLEdVGREQDLYRkEAFGPVAILEKFDR--FDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINdvpsf 447
Cdd:PRK11905 903 ApTLIE-IDSISDLER-EVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN----- 975
|
410 420
....*....|....*....|....
5KF0_A 448 RvdNM--------PYGGVKDSGLG 463
Cdd:PRK11905 976 R--NIigavvgvqPFGGEGLSGTG 997
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
157-429 |
6.06e-24 |
|
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: 104.66 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 157 FISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETN-LPKGAFSVLPAhrDGADLFTTDERFRLLSF 235
Cdd:cd07128 150 HINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG--SVGDLLDHLGEQDVVAF 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 236 TGSPAVGWALKEKAGKKK----VVLELGGNAAAIVDAD---QFEQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDT 308
Cdd:cd07128 228 TGSAATAAKLRAHPNIVArsirFNAEADSLNAAILGPDatpGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 309 LRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMdAAVAAGAKIIAGGKV----------DGAMFEATLL--ED 376
Cdd:cd07128 308 VIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDrfevvgadaeKGAFFPPTLLlcDD 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
5KF0_A 377 VGREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQR 429
Cdd:cd07128 387 PDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
157-434 |
2.92e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.48 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 157 FISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGAL-IIAEVLAETNLPKGAFSVLPAhrDGADLFTTDERFRLLSF 235
Cdd:PRK11903 154 FINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQrMVKDVVAAGILPAGALSVVCG--SSAGLLDHLQPFDVVSF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 236 TGSPAVGWALKEKAG----KKKVVLELGGNAAAIVDADQF---EQLDYVVDRLAFGAYYQSGQSCIGVQRILVHASLYDT 308
Cdd:PRK11903 232 TGSAETAAVLRSHPAvvqrSVRVNVEADSLNSALLGPDAApgsEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 309 LRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMdAAVAAGAKIIAGGK----VD-----GAMFEATLL--EDV 377
Cdd:PRK11903 312 VAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGgfalVDadpavAACVGPTLLgaSDP 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
5KF0_A 378 GREQDLYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDEL 434
Cdd:PRK11903 391 DAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
98-421 |
9.49e-23 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 102.36 E-value: 9.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 98 EAGKPINDSRGEVTRLIDTFRVASEEAvridgevlnleisarAQGYTGYTRRvPIGPCSFISPFNFPLNLAAHKVAPALA 177
Cdd:PRK11809 731 EAGKTFSNAIAEVREAVDFLRYYAGQV---------------RDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALA 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 178 AGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLPAHRD--GADLfTTDERFRLLSFTGSPAVGWALKEK-AGK--- 251
Cdd:PRK11809 795 AGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGEtvGAAL-VADARVRGVMFTGSTEVARLLQRNlAGRldp 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 252 --KKVVL--ELGGNAAAIVDADQF-EQLdyVVDRLAfGAYYQSGQSCIGVqRILVhasLYDTLRDKLVAKTR----SLKM 322
Cdd:PRK11809 874 qgRPIPLiaETGGQNAMIVDSSALtEQV--VADVLA-SAFDSAGQRCSAL-RVLC---LQDDVADRTLKMLRgamaECRM 946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 323 GDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGKVDGAMFEA------TL--LEDVGREQdlyrKEAFGPVAI 394
Cdd:PRK11809 947 GNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSgtfvppTLieLDSFDELK----REVFGPVLH 1022
|
330 340
....*....|....*....|....*....
5KF0_A 395 LEKFDR--FDDALARVNDSDFGLQAGVFT 421
Cdd:PRK11809 1023 VVRYNRnqLDELIEQINASGYGLTLGVHT 1051
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
57-442 |
1.69e-22 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 101.55 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAeALCI-EAGKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlnle 135
Cdd:COG4230 601 AAQAAFPAWSATPVEERAAILERAADLLEAHRAELM-ALLVrEAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAP---- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 136 isaraqgytgyTRRVPIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLP 215
Cdd:COG4230 676 -----------TVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLP 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 216 AhrDGADL---FTTDERFRLLSFTGSPAVGWA----LKEKAGkKKVVL--ELGGNAAAIVDAD-QFEQLdyVVDRL--AF 283
Cdd:COG4230 745 G--DGETVgaaLVADPRIAGVAFTGSTETARLinrtLAARDG-PIVPLiaETGGQNAMIVDSSaLPEQV--VDDVLasAF 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 284 gayyQS-GQSCIGVqRIL-VHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESESRRLSGWMDAAVAAGAKIIAG 361
Cdd:COG4230 820 ----DSaGQRCSAL-RVLcVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQL 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 362 ----GKVDGAMFEATLLEdVGREQDLyRKEAFGPVAILEKFDR--FDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELE 435
Cdd:COG4230 895 plpeECANGTFVAPTLIE-IDSISDL-EREVFGPVLHVVRYKAdeLDKVIDAINATGYGLTLGVHSRIDETIDRVAARAR 972
|
....*..
5KF0_A 436 VGGVVIN 442
Cdd:COG4230 973 VGNVYVN 979
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
151-483 |
2.08e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 96.65 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 151 PIGPCSFISPFNFPLNLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLaETNLPKGAFSVLpahrDGADLFTT---D 227
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVV----EGAVTETTallE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 228 ERFRLLSFTGSPAVGWALKEKAGKK--KVVLELGGNAAAIVDADQfeQLDYVVDRLAFGAY-YQSGQSCIGVQRILVHAS 304
Cdd:PLN02174 187 QKWDKIFYTGSSKIGRVIMAAAAKHltPVVLELGGKSPVVVDSDT--DLKVTVRRIIAGKWgCNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 305 LYDTLRDKLVAKTRSLKMGDPKDpSTFVGPMISESESRRLSGWMDAAVAAGaKIIAGGKVDGAMFE--ATLLEDVGREQD 382
Cdd:PLN02174 265 YAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSD-KIVYGGEKDRENLKiaPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 383 LYRKEAFGPVAILEKFDRFDDALARVNDSDFGLQAGVFTDSLTHAQRAWDELEVGGVVINDVP-SFRVDNMPYGGVKDSG 461
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAvHLALHTLPFGGVGESG 422
|
330 340
....*....|....*....|..
5KF0_A 462 LGREGIRYAIEDMTEPRLMVVR 483
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAVLYR 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
57-406 |
1.22e-18 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 87.98 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 57 AAVDAVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCIEAGKPINDSRGEVTRLIDTFRVASEEAVriDGEVLNLEI 136
Cdd:cd07129 7 AAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVR--EGSWLDARI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 137 ----SARAQGYTGYTRR--VPIGPCSFISPFNFPLnlaAHKV-----APALAAGCPFVLKPASRTP-----VGALIIAeV 200
Cdd:cd07129 85 dpadPDRQPLPRPDLRRmlVPLGPVAVFGASNFPL---AFSVaggdtASALAAGCPVVVKAHPAHPgtselVARAIRA-A 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 201 LAETNLPKGAFSVL--PAHRDGADLfTTDERFRLLSFTGSPAVGWALKEKAGK----KKVVLELGG-------------N 261
Cdd:cd07129 161 LRATGLPAGVFSLLqgGGREVGVAL-VKHPAIKAVGFTGSRRGGRALFDAAAArpepIPFYAELGSvnpvfilpgalaeR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 262 AAAIvdADQFeqldyvVDRLAFGAyyqsGQSCI--GVQrILVHASLYDTLRDKLVAKTRSlkmgdpKDPSTFVGPMISES 339
Cdd:cd07129 240 GEAI--AQGF------VGSLTLGA----GQFCTnpGLV-LVPAGPAGDAFIAALAEALAA------APAQTMLTPGIAEA 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5KF0_A 340 ESRRLSGWMDaavAAGAKIIAGGKVDGAMFE--ATLLE----DVGREQDLyRKEAFGPVAILEKFDRFDDALA 406
Cdd:cd07129 301 YRQGVEALAA---APGVRVLAGGAAAEGGNQaaPTLFKvdaaAFLADPAL-QEEVFGPASLVVRYDDAAELLA 369
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
112-429 |
1.29e-14 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 76.00 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 112 RLIDtfRVASEEAVRIDGEVL------------NLEISARA-------QGYTGYTRRVPIGPCSFISPFNFPLNLAAHKV 172
Cdd:cd07126 86 RLIQ--RVAPKSDAQALGEVVvtrkflenfagdQVRFLARSfnvpgdhQGQQSSGYRWPYGPVAIITPFNFPLEIPALQL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 173 APALAAGCPFVLKPASRTPVGALIIAEVLAETNLPKGAFSVLpaHRDGADL--FTTDERFRLLSFTGSPAVGWALKeKAG 250
Cdd:cd07126 164 MGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLI--HSDGPTMnkILLEANPRMTLFTGSSKVAERLA-LEL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 251 KKKVVLELGGNAAAIVDADqFEQLDYVVDRLAFGAYYQSGQSCiGVQRIL------VHASLYDTLrdKLVAKTRSLKmgd 324
Cdd:cd07126 241 HGKVKLEDAGFDWKILGPD-VSDVDYVAWQCDQDAYACSGQKC-SAQSILfahenwVQAGILDKL--KALAEQRKLE--- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 325 pkdpSTFVGPMISESESRRLSGWMDAAVAAGAKIIAGGK---------VDGAmFEATL----LEDVGREQ--DLYRKEAF 389
Cdd:cd07126 314 ----DLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKpltnhsipsIYGA-YEPTAvfvpLEEIAIEEnfELVTTEVF 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
5KF0_A 390 GPVAILEKFDRFD-----DALARVndsDFGLQAGVFTDSLTHAQR 429
Cdd:cd07126 389 GPFQVVTEYKDEQlplvlEALERM---HAHLTAAVVSNDIRFLQE 430
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
175-405 |
9.44e-13 |
|
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: 70.20 E-value: 9.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 175 ALAAGCPFVLKPASRTPVGALIIA----EVLAETNLPKgAFSVLPAHRDGADL---FTTDERFRLLSFTGSPAVGWALKE 247
Cdd:cd07127 217 SLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFDP-NLVTLAADTPEEPIaqtLATRPEVRIIDFTGSNAFGDWLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 248 KAGKKKVVLELGGNAAAIVDADqfEQLDYVVDRLAFGAYYQSGQSCIGVQRILV----------HASlYDTLRDKLVAKT 317
Cdd:cd07127 296 NARQAQVYTEKAGVNTVVVDST--DDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddgRKS-FDEVAADLAAAI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 318 RSLkMGDPKDPSTFVGPMISESESRRLSgwmdAAVAAGAKIIAGGKVDGAMFEAT------LLEDVGREQDLYRKEAFGP 391
Cdd:cd07127 373 DGL-LADPARAAALLGAIQSPDTLARIA----EARQLGEVLLASEAVAHPEFPDArvrtplLLKLDASDEAAYAEERFGP 447
|
250
....*....|....
5KF0_A 392 VAILEKFDRFDDAL 405
Cdd:cd07127 448 IAFVVATDSTDHSI 461
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
61-340 |
5.92e-07 |
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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: 51.45 E-value: 5.92e-07
10 20 30 40 50 60 70 80
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5KF0_A 61 AVKPMRELPAYRRQAVLDHCVARFRERFDELAEALCieagKPINDSRGEVTRLIDTFRVASEEAVRIDGEVlnleisaRA 140
Cdd:cd07077 21 IINAIANALYDTRQRLASEAVSERGAYIRSLIANWI----AMMGCSESKLYKNIDTERGITASVGHIQDVL-------LP 89
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5KF0_A 141 QGYTGYTRRVPIGPCSFISPFNFPLnLAAHKVAPALAAGCPFVLKPASRTPVGALIIAEVLAETnLPKGAFSVLPAHRDG 220
Cdd:cd07077 90 DNGETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAA-DAAHGPKILVLYVPH 167
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170 180 190 200 210 220 230 240
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5KF0_A 221 ADLFTTDERFR-----LLSFTGSP-AVGWAlkEKAGKKKVVLELG-GNAAAIVDAdqfEQLDYVVDRLAFGAYYQSGQSC 293
Cdd:cd07077 168 PSDELAEELLShpkidLIVATGGRdAVDAA--VKHSPHIPVIGFGaGNSPVVVDE---TADEERASGSVHDSKFFDQNAC 242
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250 260 270 280
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5KF0_A 294 IGVQRILVHASLYDTLRDKLVAKTRSLKMGDPKDPSTFVGPMISESE 340
Cdd:cd07077 243 ASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFD 289
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