|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
31-492 |
0e+00 |
|
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: 768.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDI 110
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 111 ASSADTFDFFGGIATAvLQGDSLELPGGpsqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAP 190
Cdd:cd07090 81 DSSADCLEYYAGLAPT-LSGEHVPLPGG---SFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 191 ASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFD 270
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 271 DSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRILGYVE 350
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTK-KIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 351 SAKQEGGVVLRGGVRVHPT-GVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFS 429
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995606 430 GNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVNVQ 492
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
15-493 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 579.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARC-DIASSADTFDFFGGIATAvLQGDSLELPGGPsqrIAYTRREPYGVVGCIGAWNYPFQTCVWKVAP 173
Cdd:PRK13252 90 ETLDTGKPIQETSVvDIVTGADVLEYYAGLAPA-LEGEQIPLRGGS---FVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKnV 253
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS-L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 254 KPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRV 333
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLL-ERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 334 GANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVI 413
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 414 ARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVNVQD 493
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
15-490 |
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: 572.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:COG1012 9 FIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARCDIASSADTFDFFGGIATAvLQGDSLelPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPA 174
Cdd:COG1012 89 LTLETGKPLAEARGEVDRAADFLRYYAGEARR-LYGETI--PSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 175 LAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNV 253
Cdd:COG1012 166 LAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA-ENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 254 KPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRV 333
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAA-KALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 334 GANINEGHLQRILGYVESAKQEGGVVLRGGVRVhptGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVI 413
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRP---DGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71995606 414 ARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYN-DTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVN 490
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTtGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
25-487 |
0e+00 |
|
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: 542.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 25 STETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIY 104
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 105 EARCDIASSADTFDFFGGIATAvLQGDSLELPGGpsqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYK 184
Cdd:pfam00171 85 EARGEVDRAIDVLRYYAGLARR-LDGETLPSDPG---RLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 185 PSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGK 263
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 264 SEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINEGHLQ 343
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAA-KKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 344 RILGYVESAKQEGGVVLRGGvrvhPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGL 423
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGG----EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995606 424 AAGVFSGNLARGHRVAARLQAGTVFINTYND-TEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTgDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
31-489 |
0e+00 |
|
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: 519.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC-D 109
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 110 IASSADTFDFFggiATAVLQGDSLELPGGPSQrIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFA 189
Cdd:cd07093 81 IPRAAANFRFF---ADYILQLDGESYPQDGGA-LNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 190 PASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIII 268
Cdd:cd07093 157 PLTAWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 269 FDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINEGHLQRILGY 348
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERA-KALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 349 VESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVF 428
Cdd:cd07093 315 VELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71995606 429 SGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
31-489 |
0e+00 |
|
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: 517.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC 108
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 109 DIASSADTFDFFGGIATAvLQGDSLELPGGPSQriAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPF 188
Cdd:cd07114 81 QVRYLAEWYRYYAGLADK-IEGAVIPVDKGDYL--NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 189 APASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEII 267
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-ENLAPVTLELGGKSPNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 268 IFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINEGHLQRILG 347
Cdd:cd07114 237 VFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARA-RAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 348 YVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGV 427
Cdd:cd07114 316 YVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71995606 428 FSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07114 396 WTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
52-489 |
8.30e-173 |
|
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: 493.26 E-value: 8.30e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 52 DQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSADTFDFFGGIATAvLQGD 131
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARR-LHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 132 SLELPGGPSQriAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYN 211
Cdd:cd07078 80 VIPSPDPGEL--AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 212 VIQGEQ-EAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQG 290
Cdd:cd07078 158 VVTGDGdEVGAALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 291 QVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPtg 370
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVK-ALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEG-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 371 vEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFIN 450
Cdd:cd07078 314 -GKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 71995606 451 TYND-TEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07078 393 DYSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
15-489 |
7.22e-171 |
|
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: 490.18 E-value: 7.22e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIA 92
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 93 IWEVKTNGKPIYE-ARCDIASSADTFDFFGGIATAVlQGDSLELPGgpsQRIAYTRREPYGVVGCIGAWNYPFQTCVWKV 171
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKI-QGKTIPIDG---NFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 172 APALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAT 250
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 KNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLED 330
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAE-KRVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 331 TRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVhptGVEGGaYFEPAIITGLSDEARAVREEIFGAVMLILPFETEE 410
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERH---GSKGY-FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 411 EVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
15-485 |
5.70e-166 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 477.38 E-value: 5.70e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEA-RCDIASSADTFDFFGGIATAvLQGDSLELPGgPSQriAYTRREPYGVVGCIGAWNYPFQTCVWKVAP 173
Cdd:TIGR01804 81 ETLDTGKTLQETiVADMDSGADVFEFFAGLAPA-LNGEIIPLGG-PSF--AYTIREPLGVCVGIGAWNYPLQIASWKIAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATkN 252
Cdd:TIGR01804 157 ALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDgAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-H 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 253 VKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTR 332
Cdd:TIGR01804 236 LKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERT-ERIKLGDPFDEATE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 333 VGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEV 412
Cdd:TIGR01804 315 MGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEV 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995606 413 IARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTK 485
Cdd:TIGR01804 395 IARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
31-487 |
3.04e-154 |
|
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: 446.88 E-value: 3.04e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDI 110
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 111 ASSADTFDFFGGIATAVlQGDSLELPGgPSQRIaYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAP 190
Cdd:cd07103 81 DYAASFLEWFAEEARRI-YGRTIPSPA-PGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 191 ASPVLLGEILTAAGVPKGVYNVIQGEQEA-GVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIF 269
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEiGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 270 DDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRILGYV 349
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVK-KLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 350 ESAKQEGGVVLRGGVRVHPtgveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFS 429
Cdd:cd07103 316 EDAVAKGAKVLTGGKRLGL----GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71995606 430 GNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07103 392 RDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
15-492 |
4.05e-153 |
|
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: 445.22 E-value: 4.05e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIA 92
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 93 IWEVKTNGKPIYEARCDIASSADTFDFFGGIATavlqGDSLELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVA 172
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLAT----KETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 173 PALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRqAATK 251
Cdd:cd07119 157 PALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSgATVGAELAESPDVDLVSFTGGTATGRSIMR-AAAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 252 NVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDT 331
Cdd:cd07119 236 NVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAK-KIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 332 RVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEE 411
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 412 VIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVNV 491
Cdd:cd07119 395 AIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
.
gi 71995606 492 Q 492
Cdd:cd07119 475 S 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
15-490 |
1.05e-152 |
|
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: 444.09 E-value: 1.05e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEAR-CDIASSADTFDFFGGiataVLQGDSLELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAP 173
Cdd:cd07559 84 ETLDNGKPIRETLaADIPLAIDHFRYFAG----VIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPSPFAPASPVLLGEILTAAgVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQrQAATKN 252
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIM-QYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 253 VKPVTLELGGKSEIIIFDD-----SDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPL 327
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAV-ERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 328 LEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFE 407
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 408 TEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
...
gi 71995606 488 YVN 490
Cdd:cd07559 477 LVS 479
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
27-489 |
3.76e-151 |
|
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: 439.34 E-value: 3.76e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 27 ETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIY 104
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 105 EARC-DIASSADTFDFFGGIATAVLQgdslELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVY 183
Cdd:cd07112 82 DALAvDVPSAANTFRWYAEAIDKVYG----EVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 184 KPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNVKPVTLELGG 262
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFgHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 263 KSEIIIFDD-SDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGH 341
Cdd:cd07112 238 KSPNIVFADaPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAR-EWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 342 LQRILGYVESAKQEGGVVLRGGVRVHPTGveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTY 421
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71995606 422 GLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07112 395 GLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
31-489 |
3.01e-150 |
|
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: 436.67 E-value: 3.01e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADA-QSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCD 109
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 110 IASSADTFDFFGGIATAvLQGDSLELPGGpsqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFA 189
Cdd:cd07109 81 VEAAARYFEYYGGAADK-LHGETIPLGPG---YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 190 PASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIII 268
Cdd:cd07109 157 PLTALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 269 FDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGdPLLEDTRVGANINEGHLQRILGY 348
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFR-ALRVG-PGLEDPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 349 VESAKQEGGVVLRGGVRVhPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVF 428
Cdd:cd07109 314 VARARARGARIVAGGRIA-EGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVW 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71995606 429 SGNLARGHRVAARLQAGTVFINTYNDTE-VNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07109 393 TRDGDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
15-490 |
1.05e-148 |
|
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: 434.14 E-value: 1.05e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA-QSAWGETTALDRGKVLHKVADLIREHAEEIAI 93
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 94 WEVKTNGKPIYE-ARCDIASSADTFDFFGGIATAVlQGDSLELPggpSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVA 172
Cdd:cd07144 91 IEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKI-QGKTIPTS---PNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 173 PALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQG-EQEAGVALCEHNLVAKVSFTGSVASGEAVQrQAATK 251
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVM-KAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 252 NVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANDKLKVGDPLLEDT 331
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 332 RVGANINEGHLQRILGYVESAKQEGGVVLRGGVrVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEE 411
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGE-KAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 412 VIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVN 490
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHIN 483
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
31-472 |
1.24e-147 |
|
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: 430.23 E-value: 1.24e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDI 110
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 111 ASSADTFDFFGGIATAVLQGDSLELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAP 190
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 191 ASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIIIF 269
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTgDEAGAPLAAHPGIDKISFTGSTATGSQVM-QAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 270 DDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINEGHLQRILGYV 349
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAA-EAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 350 ESAKQEGGVVLRGGVRvhPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFS 429
Cdd:cd07110 319 ARGKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 71995606 430 GNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRE 472
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRE 439
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
31-491 |
3.47e-145 |
|
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: 423.77 E-value: 3.47e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEAR-CD 109
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 110 IASSADTFDFFGGIATAvLQGDSLELPGGpsqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFA 189
Cdd:cd07115 81 VPRAADTFRYYAGWADK-IEGEVIPVRGP---FLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 190 PASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIII 268
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIM-QGAAGNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 269 FDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANDkLKVGDPLLEDTRVGANINEGHLQRILGY 348
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARS-LRPGDPLDPKTQMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 349 VESAKQEGGVVLRGGVRVHptgvEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVF 428
Cdd:cd07115 315 VDVGREEGARLLTGGKRPG----ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVW 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995606 429 SGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVNV 491
Cdd:cd07115 391 TRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
14-488 |
1.65e-142 |
|
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: 417.29 E-value: 1.65e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 14 YFLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAI 93
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 94 WEVKTNGKPIYEARcdiASSADTFDFFGGIATAVLQGDSLELPGGPSqRIaytRREPYGVVGCIGAWNYPFQTCVWKVAP 173
Cdd:cd07138 81 AITLEMGAPITLAR---AAQVGLGIGHLRAAADALKDFEFEERRGNS-LV---VREPIGVCGLITPWNWPLNQIVLKVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATkN 252
Cdd:cd07138 154 ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDgPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAD-T 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 253 VKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTR 332
Cdd:cd07138 233 VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAA-EAYVVGDPRDPATT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 333 VGANINEGHLQRILGYVESAKQEGGVVLRGGVRvHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEV 412
Cdd:cd07138 312 LGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995606 413 IARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINtYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIY 488
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
15-490 |
1.66e-142 |
|
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: 418.01 E-value: 1.66e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEAR-CDIASSADTFDFFGGiataVLQGDSLELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAP 173
Cdd:cd07117 84 ETLDNGKPIRETRaVDIPLAADHFRYFAG----VIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPSPFAPASPVLLGEILTAAgVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQrQAATKN 252
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVA-IAAAKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 253 VKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTR 332
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLK-EKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 333 VGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEV 412
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71995606 413 IARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVN 490
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYID 474
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
31-489 |
1.46e-141 |
|
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: 414.42 E-value: 1.46e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCD- 109
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 110 IASSADTFDFFGGiATAVLQGDSLE--LPGGPSqriaYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSP 187
Cdd:cd07092 81 LPGAVDNFRFFAG-AARTLEGPAAGeyLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 188 FAPASPVLLGEILtAAGVPKGVYNVIQGEQE-AGVALCEHNLVAKVSFTGSVASGEAVQRqAATKNVKPVTLELGGKSEI 266
Cdd:cd07092 156 TTPLTTLLLAELA-AEVLPPGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVAR-AAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 267 IIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQRIL 346
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALV-EAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 347 GYVESAKQeGGVVLRGGVRVHPTGveggAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAG 426
Cdd:cd07092 313 GFVERAPA-HARVLTGGRRAEGPG----YFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995606 427 VFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
31-489 |
4.41e-141 |
|
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: 413.08 E-value: 4.41e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDI 110
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 111 ASSADtfdFFGGIATAVLQGDSLELpgGPSQRIAyTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAP 190
Cdd:cd07106 81 GGAVA---WLRYTASLDLPDEVIED--DDTRRVE-LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 191 ASPVLLGEILTAAgVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFD 270
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 271 DSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRILGYVE 350
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAK-AAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 351 SAKQEGGVVLRGGVRVhptgvEGGAYF-EPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFS 429
Cdd:cd07106 312 DAKAKGAKVLAGGEPL-----DGPGYFiPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 430 GNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
15-490 |
6.39e-139 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 408.53 E-value: 6.39e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIEStETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:PRK13473 6 LINGELVAGEG-EKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARCD-IASSADTFDFFGGiATAVLQGDSLE--LPGGPSqriaYTRREPYGVVGCIGAWNYPFQTCVWKV 171
Cdd:PRK13473 85 ESLNCGKPLHLALNDeIPAIVDVFRFFAG-AARCLEGKAAGeyLEGHTS----MIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 172 APALAAGNAVVYKPSPFAPASPVLLGEILTAAgVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQrQAAT 250
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRgATVGDALVGHPKVRMVSLTGSIATGKHVL-SAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 KNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLED 330
Cdd:PRK13473 238 DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLA-AAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 331 TRVGANINEGHLQRILGYVESAKQEGGV-VLRGGVRvhPTGveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGHIrVVTGGEA--PDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 410 EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMV 472
|
.
gi 71995606 490 N 490
Cdd:PRK13473 473 K 473
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
31-489 |
4.16e-138 |
|
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: 405.98 E-value: 4.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPI-YEARCD 109
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 110 IASSADTFDFFGGIATAvLQGDSLelPGGPSQrIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFA 189
Cdd:cd07108 81 AAVLADLFRYFGGLAGE-LKGETL--PFGPDV-LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 190 PASPVLLGEILtAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNVkPVTLELGGKSEIII 268
Cdd:cd07108 157 PLAVLLLAEIL-AQVLPAGVLNVITGYgEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLI-PVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 269 FDDSDVKSAVASAMLA-NFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQRILG 347
Cdd:cd07108 235 FPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLV-AKLSKLKIGDPLDEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 348 YVESAKQE-GGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAG 426
Cdd:cd07108 314 YIDLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71995606 427 VFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAH-TQTKAIYV 489
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEHfTQKKTVNI 457
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-491 |
6.73e-137 |
|
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: 403.83 E-value: 6.73e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA-QSAWG-ETTALDRGKVLHKVADLIREHAEEIA 92
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 93 IWEVKTNGKPI-YEARCDIASSADTFDFFGGIATAVlQGDSLELPggpSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKV 171
Cdd:cd07143 90 SIEALDNGKTFgTAKRVDVQASADTFRYYGGWADKI-HGQVIETD---IKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 172 APALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAT 250
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYgRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 KNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLED 330
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAK-KLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 331 TRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRvhpTGVEGgaYF-EPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKR---HGNEG--YFiEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 410 EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07143 400 EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
..
gi 71995606 490 NV 491
Cdd:cd07143 480 NL 481
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
15-488 |
7.77e-137 |
|
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: 403.41 E-value: 7.77e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIA 92
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 93 IWEVKTNGKPIYEAR-CDIASSADTFDFFGGIATAVlQGdsLELPG-GPSQriAYTRREPYGVVGCIGAWNYPFQTCVWK 170
Cdd:cd07142 87 ALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKI-HG--MTLPAdGPHH--VYTLHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 171 VAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQG-EQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAA 249
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 250 TKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANDKLkVGDPLLE 329
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRV-VGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 330 DTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHptgvEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIG----SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 410 EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIY 488
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
31-490 |
6.55e-136 |
|
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: 400.21 E-value: 6.55e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDI 110
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 111 ASSADTFDFFGGIATAvLQGDSLELPGGpsqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAP 190
Cdd:cd07107 81 MVAAALLDYFAGLVTE-LKGETIPVGGR---NLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 191 ASPVLLGEIltAAGV-PKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIII 268
Cdd:cd07107 157 LSALRLAEL--AREVlPPGVFNILPGDgATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA-EGIKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 269 FDDSDVKsAVASAMLA--NFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQRIL 346
Cdd:cd07107 234 FPDADPE-AAADAAVAgmNFTWCGQSCGSTSRLFVHESIYDEVLARVV-ERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 347 GYVESAKQEGGVVLRGGVRvhPTGV--EGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLA 424
Cdd:cd07107 312 HYIDSAKREGARLVTGGGR--PEGPalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995606 425 AGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVN 490
Cdd:cd07107 390 AAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-489 |
8.87e-136 |
|
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: 400.41 E-value: 8.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIA 92
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 93 -IWeVKTNGKPIYEAR-CDIASSADTFDFFGGIATAVLQGDSLELPGGPSQRIaytRREPYGVVGCIGAWNYPFQTCVWK 170
Cdd:cd07139 82 rLW-TAENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLV---RREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 171 VAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAt 250
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 KNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLED 330
Cdd:cd07139 237 ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAV-AALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 331 TRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRvhPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEE 410
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 411 EVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYnDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
15-489 |
5.50e-135 |
|
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: 398.56 E-value: 5.50e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARCDIASSADTFDFFGGIATaVLQGDSleLPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPA 174
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWAR-RIEGEI--IPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 175 LAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNV 253
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRgSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA-ENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 254 KPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRV 333
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLV-EKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 334 GANINEGHLQRILGYVESAKQEGGVVLRGGVRVHptgVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVI 413
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPE---GEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995606 414 ARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07088 393 ELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
15-472 |
5.92e-135 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 399.49 E-value: 5.92e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSA-----WGETTALDRGKVLHKVADLIREHAE 89
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 90 EIAIWEVKTNGKPIYEARCDIASSADTFDFFGGIATAV--LQGDSLELPggPSQRIAYTRREPYGVVGCIGAWNYPFQTC 167
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALdaKQKAPVSLP--METFKGYVLKEPLGVVGLITPWNYPLLMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 168 VWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQR 246
Cdd:PLN02467 169 TWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTATGRKIMT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 247 qAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDP 326
Cdd:PLN02467 249 -AAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWA-KNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 327 LLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRvhPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPF 406
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995606 407 ETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRE 472
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRE 470
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
34-489 |
4.07e-134 |
|
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: 395.55 E-value: 4.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 34 PRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIA 111
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 112 SSADTFDFFGGIATAvLQGDSLELPGgpSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPA 191
Cdd:cd07118 84 GAADLWRYAASLART-LHGDSYNNLG--DDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 192 SPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFD 270
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYgATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 271 DSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQRILGYVE 350
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVV-ARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 351 SAKQEGGVVLRGGVRVhptGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSG 430
Cdd:cd07118 319 AGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSK 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 431 NLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07118 396 DIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
15-489 |
2.16e-133 |
|
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: 394.79 E-value: 2.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA---QSAWGETTALDRGKVLHKVADLIREHAEEI 91
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 92 AIWEVKTNGKPIYEAR-CDIASSADTFDFFGGIATAVlQGDSLELPGgpsQRIAYTRREPYGVVGCIGAWNYPFQTCVWK 170
Cdd:cd07141 90 ASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKI-HGKTIPMDG---DFFTYTRHEPVGVCGQIIPWNFPLLMAAWK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 171 VAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQE-AGVALCEHNLVAKVSFTGSVASGEAVQRQAA 249
Cdd:cd07141 166 LAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPtAGAAISSHPDIDKVAFTGSTEVGKLIQQAAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 250 TKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLE 329
Cdd:cd07141 246 KSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAK-KRVVGNPFDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 330 DTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHptgvEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:cd07141 325 KTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHG----DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 410 EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
31-487 |
3.82e-131 |
|
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: 388.14 E-value: 3.82e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALD-RGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC- 108
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTDAEeRARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 109 DIASSADTFDFFGGIATAVLQGDSLE---LPGGPSQRIAytRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKP 185
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPvpaLRGGPGRRVV--RREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 186 SPFAPASPVLLGEILTAAGVPKGVYNVIQG-EQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKS 264
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGsDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 265 EIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAiVQEANDKLKVGDPLLEDTRVGANINEGHLQR 344
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEA-LAAAFEALPVGDPADPGTVMGPLISAAQRDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 345 ILGYVESAKQEGGVVLRGGVRvhPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLA 424
Cdd:cd07089 317 VEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995606 425 AGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07089 395 GGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
15-489 |
3.35e-130 |
|
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: 386.22 E-value: 3.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRttIESTETFDVIEP-RIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAI 93
Cdd:cd07097 4 YIDGEW--VAGGDGEENRNPsDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 94 WEVKTNGKPIYEARCDIASSADTFDFFGGIATAvLQGDSLelpggPSQR---IAYTRREPYGVVGCIGAWNYPFQTCVWK 170
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALR-LSGETL-----PSTRpgvEVETTREPLGVVGLITPWNFPIAIPAWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 171 VAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRqAA 249
Cdd:cd07097 156 IAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSgSEVGQALVEHPDVDAVSFTGSTAVGRRIAA-AA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 250 TKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLE 329
Cdd:cd07097 235 AARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTK-ALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 330 DTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVhpTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERL--KRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 410 EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFIN-TYNDTEVNVPFGGFKNSGHG-RENCIDTLRAHTQTKAI 487
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
..
gi 71995606 488 YV 489
Cdd:cd07097 472 YV 473
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
51-489 |
6.56e-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: 384.19 E-value: 6.56e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSADTFDFFGGIATAVlQG 130
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRP-EG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 131 DslELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSP-FAPASPVLLGEILTAAGVPKGV 209
Cdd:cd07104 81 E--ILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrTPVTGGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 210 YNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLN 288
Cdd:cd07104 159 LNVVPGGgSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG-RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 289 QGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVhp 368
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVAKA-KALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 369 tgvegGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVF 448
Cdd:cd07104 315 -----GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVH 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 71995606 449 IN--TYNDtEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07104 390 INdqTVND-EPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
15-489 |
1.31e-129 |
|
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: 385.31 E-value: 1.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIA 92
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 93 IWEVKTNGKPIYEA-RCDIASSADTFDFFGGIATAVlQGDSLEL-PGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWK 170
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKI-QGKTIPInQARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 171 VAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAA 249
Cdd:cd07140 168 MAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSgSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 250 TKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLE 329
Cdd:cd07140 248 VSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVK-KMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 330 DTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVeggaYFEPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 410 --EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07140 403 dvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
..
gi 71995606 488 YV 489
Cdd:cd07140 483 TI 484
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
15-490 |
8.99e-129 |
|
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: 382.85 E-value: 8.99e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEP-RIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAI 93
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 94 WEVKTNGKPIYEARCDIASSADTFDFFGGiATAVLQGDSL--ELPggpsQRIAYTRREPYGVVGCIGAWNYPFQTCVWKV 171
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAG-EGRRLFGETVpsELP----NKDAMTRRQPIGVVALITPWNFPVAIPSWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 172 APALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAT 250
Cdd:cd07131 157 FPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRgEEVGEALVEHPDVDVVSFTGSTEVGERIGETCAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 KNvKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLED 330
Cdd:cd07131 237 PN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAK-RLRVGDGLDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 331 TRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEE 410
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 411 EVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINtyNDT---EVNVPFGGFKNSGHG-RENCIDTLRAHTQTKA 486
Cdd:cd07131 395 EAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTigaEVHLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
....
gi 71995606 487 IYVN 490
Cdd:cd07131 473 VYVD 476
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-494 |
2.95e-128 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 382.25 E-value: 2.95e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIA 92
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 93 IWEVKTNGK-PIYEARCDIASSADTFDFFGGIATAVlQGDSLELPGgpsQRIAYTRREPYGVVGCIGAWNYPFQTCVWKV 171
Cdd:PLN02766 104 ALDTIDAGKlFALGKAVDIPAAAGLLRYYAGAADKI-HGETLKMSR---QLQGYTLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 172 APALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQG-EQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAT 250
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 KNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANDkLKVGDPLLED 330
Cdd:PLN02766 260 SNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKD-WVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 331 TRVGANINEGHLQRILGYVESAKQEGGVVLRGGvrvHPTGvEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEE 410
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGG---KPCG-DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 411 EVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVN 490
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
....
gi 71995606 491 VQDT 494
Cdd:PLN02766 495 LYNS 498
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
29-472 |
3.71e-128 |
|
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: 380.40 E-value: 3.71e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 29 FDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC 108
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 109 DIASSADTFDFFGGIATAvLQGDSLEL---PGGpSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKP 185
Cdd:cd07149 81 EVDRAIETLRLSAEEAKR-LAGETIPFdasPGG-EGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 186 SPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtknVKPVTLELGGKS 264
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSgETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 265 EIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINEGHLQR 344
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAAT-KKLVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 345 ILGYVESAKQEGGVVLRGGVRVhptgvegGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLA 424
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRD-------GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 71995606 425 AGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNV-PFGGFKNSGHGRE 472
Cdd:cd07149 388 AGVFTNDLQKALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGRE 436
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
15-489 |
4.72e-128 |
|
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: 381.02 E-value: 4.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA-QSAWGETTALDRGKVLHKVADLIREHAEEIAI 93
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 94 WEVKTNGKPIYEARC-DIASSADTFDFFGGIATAVlQGDSLE--LPGGPSQR-IAYTRREPYGVVGCIGAWNYPFQTCVW 169
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKI-NGETLApsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 170 KVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAA 249
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 250 TkNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQeANDKLKVGDPLLE 329
Cdd:cd07113 242 S-DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQ-ALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 330 DTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVeggaYFEPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 410 EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
56-489 |
6.09e-128 |
|
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: 376.57 E-value: 6.09e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 56 KAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSADTFDFFGGIATAvLQGDslEL 135
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADK-LGGP--EL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 136 PGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQG 215
Cdd:cd06534 78 PSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 216 EQ-EAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCT 294
Cdd:cd06534 158 GGdEVGAALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 295 NATRVFVQKGILASFTEAIVqeandklkvgdplledtrvganineghlqrilgyvesakqeggvvlrggvrvhptgvegg 374
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 375 ayfepAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYND 454
Cdd:cd06534 257 -----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSI 331
|
410 420 430
....*....|....*....|....*....|....*.
gi 71995606 455 -TEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd06534 332 gVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
29-487 |
1.29e-127 |
|
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: 379.00 E-value: 1.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 29 FDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC 108
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 109 DIASSADTFDFFGGIAtAVLQGDSLELPGGP--SQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPS 186
Cdd:cd07145 81 EVERTIRLFKLAAEEA-KVLRGETIPVDAYEynERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 187 PFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKnVKPVTLELGGKSE 265
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYgSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 266 IIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRI 345
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVK-KLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 346 LGYVESAKQEGGVVLRGGVRvhptgvEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAA 425
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995606 426 GVFSGNLARGHRVAARLQAGTVFINtyNDTEV---NVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN--DSTRFrwdNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
15-472 |
8.94e-124 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 370.95 E-value: 8.94e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARCDIASSADTFDFFGGIATAVlQGDSLELPGGPSQRIAYtrREPYGVVGCIGAWNYPFQTCVWKVAPA 174
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRV-YGDIIPSPFPDRRLLVL--KQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 175 LAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEA-GVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNV 253
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEiGDALLASPKVRKITFTGSTAVGKKLMAGAA-ATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 254 KPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRV 333
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQ-KLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 334 GANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPtgveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVI 413
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSL----GGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAI 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 414 ARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINT-YNDTEVnVPFGGFKNSGHGRE 472
Cdd:PLN02278 419 AIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEgLISTEV-APFGGVKQSGLGRE 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
15-472 |
1.19e-122 |
|
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: 367.11 E-value: 1.19e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEAR-CDIASSADTFDFFGGIAtavlQGDSLELPGgpsqriaytrREPYGVVGCIGAWNYPFQTCVWKVAP 173
Cdd:cd07111 105 ESLDNGKPIRESRdCDIPLVARHFYHHAGWA----QLLDTELAG----------WKPVGVVGQIVPWNFPLLMLAWKICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNV 253
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATA-GTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 254 KPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIvQEANDKLKVGDPLLEDTRV 333
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKL-KERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 334 GANINEGHLQRILGYVESAKQEGGVVLRGGVRVhPTgveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVI 413
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADL-PS---KGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAV 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 414 ARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRE 472
Cdd:cd07111 405 ALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGRE 463
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
4-487 |
1.93e-119 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 361.05 E-value: 1.93e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 4 TVPSDLSGGLYFLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVA 81
Cdd:PLN02466 50 TPPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 82 DLIREHAEEIAIWEVKTNGKPiYE--ARCDIASSADTFDFFGGIATAVlqgDSLELPG-GPSQriAYTRREPYGVVGCIG 158
Cdd:PLN02466 130 DLLEKHNDELAALETWDNGKP-YEqsAKAELPMFARLFRYYAGWADKI---HGLTVPAdGPHH--VQTLHEPIGVAGQII 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 159 AWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQG-EQEAGVALCEHNLVAKVSFTGS 237
Cdd:PLN02466 204 PWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 238 VASGEAVQRQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEA 317
Cdd:PLN02466 284 TDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 318 NDKLkVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVeggaYFEPAIITGLSDEARAVREEIF 397
Cdd:PLN02466 364 LKRV-VGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIF 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 398 GAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDT 477
Cdd:PLN02466 439 GPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYS 518
|
490
....*....|
gi 71995606 478 LRAHTQTKAI 487
Cdd:PLN02466 519 LNNYLQVKAV 528
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
34-487 |
2.95e-119 |
|
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: 357.69 E-value: 2.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 34 PRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASS 113
Cdd:cd07099 3 PATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 114 ADTFDFFGGIATAVLQGDSLELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASP 193
Cdd:cd07099 83 LEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 194 VLLGEILTAAGVPKGVYNVIQGEQEAGVALCEhNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSD 273
Cdd:cd07099 163 ELLAEAWAAAGPPQGVLQVVTGDGATGAALID-AGVDKVAFTGSVATGRKVMAAAA-ERLIPVVLELGGKDPMIVLADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 274 VKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRILGYVESAK 353
Cdd:cd07099 241 LERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKAR-ALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 354 QEGGVVLRGGVRVHptgvEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLA 433
Cdd:cd07099 320 AKGAKALTGGARSN----GGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 71995606 434 RGHRVAARLQAGTVFIN--TYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07099 396 RAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
51-472 |
8.97e-115 |
|
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: 345.21 E-value: 8.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAiwEVKTN--GKPIYEARCDIASSADTFDFFGGIATAVL 128
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELA--RLITLemGKPIAEARAEVEKCAWICRYYAENAEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 129 QGDSLELPGGpsqrIAYTRREPYGVVGCIGAWNYPFqtcvWKV----APALAAGNAVVYKPSPFAPASPVLLGEILTAAG 204
Cdd:cd07100 79 ADEPIETDAG----KAYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 205 VPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLA 284
Cdd:cd07100 151 FPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAG-KNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 285 NFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGV 364
Cdd:cd07100 230 RLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMA-ALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 365 RV-HPtgvegGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQ 443
Cdd:cd07100 309 RPdGP-----GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
410 420
....*....|....*....|....*....
gi 71995606 444 AGTVFINTYNDTEVNVPFGGFKNSGHGRE 472
Cdd:cd07100 384 AGMVFINGMVKSDPRLPFGGVKRSGYGRE 412
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-490 |
1.09e-113 |
|
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: 344.16 E-value: 1.09e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 24 ESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIA---IWEVktnG 100
Cdd:cd07086 10 SGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGrlvSLEM---G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 101 KPIYEARCDIASSADTFDFFGGIaTAVLQGDSL--ELPGgpsqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAG 178
Cdd:cd07086 87 KILPEGLGEVQEMIDICDYAVGL-SRMLYGLTIpsERPG----HRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 179 NAVVYKPSPFAPASPV----LLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNvK 254
Cdd:cd07086 162 NTVVWKPSETTPLTAIavtkILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF-G 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 255 PVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVG 334
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYK-QVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 335 ANINEGHLQRILGYVESAKQEGGVVLRGGVRVhpTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIA 414
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRI--DGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 415 RANNTTYGLAAGVFSGNLARGHRV--AARLQAGTVFINT-YNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVN 490
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTIN 476
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
15-489 |
1.23e-113 |
|
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: 344.05 E-value: 1.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEA-RCDIASSADTFDFFGGIATAVlQGDSLELPggpSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAP 173
Cdd:cd07116 84 ETWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQ-EGSISEID---ENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPSPFAPASPVLLGEILTAAgVPKGVYNVIQG-EQEAGVALCEHNLVAKVSFTGSVASGEAVQrQAATKN 252
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIM-QYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 253 VKPVTLELGGKSEIIIF------DDSDVKSAVAS-AMLAnfLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGD 325
Cdd:cd07116 238 IIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGfVMFA--LNQGEVCTCPSRALIQESIYDRFMERALERV-KAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 326 PLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGlSDEARAVREEIFGAVMLILP 405
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 406 FETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTK 485
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
....
gi 71995606 486 AIYV 489
Cdd:cd07116 474 NLLV 477
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
37-470 |
2.02e-113 |
|
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: 342.35 E-value: 2.02e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 37 GQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSADT 116
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 117 FDFFGGIATavlQGDSLELPGGPSqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASP-VL 195
Cdd:cd07152 81 LHEAAGLPT---QPQGEILPSAPG-RLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 196 LGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSDVK 275
Cdd:cd07152 157 IARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 276 SAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQE 355
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKA-KHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 356 GGVVLRGGVRvhptgveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARG 435
Cdd:cd07152 315 GARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430
....*....|....*....|....*....|....*..
gi 71995606 436 HRVAARLQAGTVFIN--TYNDtEVNVPFGGFKNSGHG 470
Cdd:cd07152 388 MALADRLRTGMLHINdqTVND-EPHNPFGGMGASGNG 423
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
29-489 |
1.19e-112 |
|
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: 340.46 E-value: 1.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 29 FDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC 108
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 109 DIASSADTFDFFGGIATAVlQGDSLelPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPF 188
Cdd:cd07150 81 ETTFTPELLRAAAGECRRV-RGETL--PSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 189 APASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEII 267
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGgAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 268 IFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRILG 347
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARAS-KLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 348 YVESAKQEGGVVLRGGVRvhptgveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGV 427
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71995606 428 FSGNLARGHRVAARLQAGTVFIN--TYNDtEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07150 389 LTNDLQRAFKLAERLESGMVHINdpTILD-EAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
18-492 |
8.42e-111 |
|
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: 336.20 E-value: 8.42e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 18 GKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVK 97
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 98 TNGKPIYEARCDIASSADTFDffggiatavlqgDSLELPGGPSQRIA---------YTRREPYGVVGCIGAWNYPFQTCV 168
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITR------------EAATFPLRMEGRILpsdvpgkenRVYREPLGVVGVISPWNFPLHLSM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 169 WKVAPALAAGNAVVYKPSPFAPASP-VLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQR 246
Cdd:cd07151 149 RSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAgSEIGDAFVEHPVPRLISFTGSTPVGRHIGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 247 QAAtKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDP 326
Cdd:cd07151 229 LAG-RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVK-ALPYGDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 327 LLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVhptgvegGAYFEPAIITGLSDEARAVREEIFGAVMLILPF 406
Cdd:cd07151 307 SDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAE-------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 407 ETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFIN--TYNDtEVNVPFGGFKNSGHGRENCIDTLRAHTQT 484
Cdd:cd07151 380 DDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVND-EPHVPFGGEKNSGLGRFNGEWALEEFTTD 458
|
....*...
gi 71995606 485 KaiYVNVQ 492
Cdd:cd07151 459 K--WISVQ 464
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-492 |
1.47e-109 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 334.17 E-value: 1.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALDRGKVLHKVADLIREHAEEIA 92
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 93 IWEVKTNGKPI-YEARCDIASSADTFDFFGGIATAVLQgdslELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKV 171
Cdd:PRK09847 103 LLETLDTGKPIrHSLRDDIPGAARAIRWYAEAIDKVYG----EVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 172 APALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQG-EQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAT 250
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 KNVKPVTLELGGKSEIIIFDD-SDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANDkLKVGDPLLE 329
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADcPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQN-WQPGHPLDP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 330 DTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPtgveggAYFEPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:PRK09847 338 ATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLA------AAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 410 EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:PRK09847 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
...
gi 71995606 490 NVQ 492
Cdd:PRK09847 492 SLE 494
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
30-487 |
3.71e-107 |
|
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: 326.70 E-value: 3.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 30 DVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCD 109
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 110 IASSADTFDffggIATAVLQ---GDSLELP--GGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYK 184
Cdd:cd07094 82 VDRAIDTLR----LAAEEAErirGEEIPLDatQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 185 PSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNvkpVTLELGGK 263
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKR---IALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 264 SEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQ 343
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFV-AAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 344 RILGYVESAKQEGGVVLRGGVRvhptgveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGL 423
Cdd:cd07094 314 RVERWVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995606 424 AAGVFSGNLARGHRVAARLQAGTVFINTYNDTEV-NVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
32-489 |
2.32e-105 |
|
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: 321.99 E-value: 2.32e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 32 IEPRIGQVVAKCPKATADIVDQYVKAAADA--QSAWGETTALdRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCD 109
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAfdETDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 110 IASSADTFDFFGGIATAVlQGDSLEL-PGgpsqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPF 188
Cdd:cd07120 81 ISGAISELRYYAGLARTE-AGRMIEPePG----SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 189 APASPVLLGEILTAA-GVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEI 266
Cdd:cd07120 156 TAQINAAIIRILAEIpSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 267 IIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINEGHLQRIL 346
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARL-AAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 347 GYVESAKQEGG-VVLRGGvRVhPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAA 425
Cdd:cd07120 314 RMVERAIAAGAeVVLRGG-PV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71995606 426 GVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYV 489
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
15-491 |
4.98e-103 |
|
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: 318.01 E-value: 4.98e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRttIESTETFDVIEP-RIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAI 93
Cdd:cd07124 36 VIGGKE--VRTEEKIESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 94 WEVKTNGKPIYEARCDIASSADTFDFFGGIATAvLQGDSLELPGGPSQRIAYtrrEPYGVVGCIGAWNYPFQTCVWKVAP 173
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLR-LRGFPVEMVPGEDNRYVY---RPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAT-- 250
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPgEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKvq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 ---KNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPL 327
Cdd:cd07124 270 pgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLV-ERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 328 LEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVrvhPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFE 407
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEV---LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 408 TEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTyNDTEVNV---PFGGFKNSGHGRENC-IDTLRAHTQ 483
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANR-KITGALVgrqPFGGFKMSGTGSKAGgPDYLLQFMQ 504
|
....*...
gi 71995606 484 TKAIYVNV 491
Cdd:cd07124 505 PKTVTENF 512
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
14-490 |
2.44e-100 |
|
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: 309.50 E-value: 2.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 14 YFLNGKrtTIEST-ETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTAL-DRGKVLHKVADLIREHAEEI 91
Cdd:cd07082 4 YLINGE--WKESSgKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLeERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 92 A---IWEVktnGKPIYEARCDIASSAD----TFDFFGGIATAVLQGDSLElpgGPSQRIAYTRREPYGVVGCIGAWNYPF 164
Cdd:cd07082 82 AnllMWEI---GKTLKDALKEVDRTIDyirdTIEELKRLDGDSLPGDWFP---GTKGKIAQVRREPLGVVLAIGPFNYPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 165 QTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEA 243
Cdd:cd07082 156 NLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 244 VQRQAAtknVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKV 323
Cdd:cd07082 236 LKKQHP---MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEV-AKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 324 GDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTgveggaYFEPAIITGLSDEARAVREEIFGAVMLI 403
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGN------LIYPTLLDPVTPDMRLAWEEPFGPVLPI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 404 LPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNV-PFGGFKNSGHGRENCIDTLRAHT 482
Cdd:cd07082 386 IRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDALRSMT 465
|
....*...
gi 71995606 483 QTKAIYVN 490
Cdd:cd07082 466 RRKGIVIN 473
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
32-488 |
2.04e-99 |
|
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: 306.48 E-value: 2.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 32 IEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAI---WEVktnGKPIYEARC 108
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEeltWQM---GRPIAQAGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 109 DIASSADTFDFFGGIATAVLQGDSLELPGGPSQRIaytRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPF 188
Cdd:cd07102 78 EIRGMLERARYMISIAEEALADIRVPEKDGFERYI---RREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 189 APASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIII 268
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAA-GRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 269 FDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQRILGY 348
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVK-GYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 349 VESAKQEGGVVLRGGvRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVF 428
Cdd:cd07102 313 IADAIAKGARALIDG-ALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 429 SGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIY 488
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYH 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
29-472 |
3.64e-99 |
|
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: 306.09 E-value: 3.64e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 29 FDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC 108
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 109 DIASSADTFDFFGGIAT----AVLQGDSLELPGGpsqRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYK 184
Cdd:cd07147 81 EVARAIDTFRIAAEEATriygEVLPLDISARGEG---RQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 185 PSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATknvKPVTLELGGKS 264
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 265 EIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTRVGANINEGHLQR 344
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVK-ALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 345 ILGYVESAKQEGGVVLRGGVRvhptgveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLA 424
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQ 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 71995606 425 AGVFSGNLARGHRVAARLQAGTVFINTYNDTEV-NVPFGGFKNSGHGRE 472
Cdd:cd07147 387 AGVFTRDLEKALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGRE 435
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
51-487 |
2.03e-98 |
|
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: 303.34 E-value: 2.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSADTFDFFGGIATAVLQG 130
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 131 dslELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVY 210
Cdd:cd07105 82 ---SIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 211 NVIQGEQE--AGV--ALCEHNLVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANF 286
Cdd:cd07105 159 NVVTHSPEdaPEVveALIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 287 LNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDplledTRVGANINEGHLQRILGYVESAKQEGGVVLRGGvrv 366
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAE-KLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGG--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 367 HPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGT 446
Cdd:cd07105 309 LADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 71995606 447 VFIN--TYNDtEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07105 389 VHINgmTVHD-EPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
14-487 |
2.59e-97 |
|
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: 302.13 E-value: 2.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 14 YFLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAI 93
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 94 WEVKTNGKPIYEARCDIASSADTFDFFGGIATaVLQGDSLElpgGPSQRI-AYTRREPYGVVGCIGAWNYPFQTCVWKVA 172
Cdd:cd07085 83 LITLEHGKTLADARGDVLRGLEVVEFACSIPH-LLKGEYLE---NVARGIdTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 173 PALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQrQAATKN 252
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIY-ERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 253 VKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPLLEDTR 332
Cdd:cd07085 238 GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAK-KLKVGAGDDPGAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 333 VGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEV 412
Cdd:cd07085 317 MGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 413 IARANNTTYGLAAGVF--SGNLARghRVAARLQAGTVFINtyndteVNVP-------FGGFKNS--GHGRENCIDTLRAH 481
Cdd:cd07085 397 IAIINANPYGNGAAIFtrSGAAAR--KFQREVDAGMVGIN------VPIPvplaffsFGGWKGSffGDLHFYGKDGVRFY 468
|
....*.
gi 71995606 482 TQTKAI 487
Cdd:cd07085 469 TQTKTV 474
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
31-487 |
4.18e-97 |
|
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: 300.81 E-value: 4.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 31 VIEPRIGQVVAKCPKATADIVDqyvKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDI 110
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALR---EALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 111 ASSADTFDFfggIATAVLQGD----SLELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPS 186
Cdd:cd07146 80 GRAADVLRF---AAAEALRDDgesfSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 187 PFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVqrqAATKNVKPVTLELGGKSE 265
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 266 IIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQRI 345
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLV-EKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 346 LGYVESAKQEGGVVLRGGVRVhptgvegGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAA 425
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQRQ-------GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSS 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995606 426 GVFSGNLARGHRVAARLQAGTVFINT---YnDTEvNVPFGGFKNSGHG-RENCIDTLRAHTQTKAI 487
Cdd:cd07146 386 GVCTNDLDTIKRLVERLDVGTVNVNEvpgF-RSE-LSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
20-487 |
1.97e-95 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 298.72 E-value: 1.97e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 20 RTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIA---IWEV 96
Cdd:PRK09407 25 RVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLdlvQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 97 KTNGKPIYEARCDIASSAdtfDFFGGIATAVL-----QGdslELPGGPSQRiayTRREPYGVVGCIGAWNYPFQTCVWKV 171
Cdd:PRK09407 105 GKARRHAFEEVLDVALTA---RYYARRAPKLLaprrrAG---ALPVLTKTT---ELRQPKGVVGVISPWNYPLTLAVSDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 172 APALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHnlVAKVSFTGSVASGEAVQRQAAt 250
Cdd:PRK09407 176 IPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPgPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 251 KNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLED 330
Cdd:PRK09407 253 RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFV-AAVRAMRLGAGYDYS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 331 TRVGANINEGHLQRILGYVESAKQEGGVVLRGGvRVHPtgvEGGAYF-EPAIITGLSDEARAVREEIFGAVMLILPFETE 409
Cdd:PRK09407 332 ADMGSLISEAQLETVSAHVDDAVAKGATVLAGG-KARP---DLGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 410 EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFIN-----TYNDTEvnVPFGGFKNSGHGRENCIDTLRAHTQT 484
Cdd:PRK09407 408 DEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTES 485
|
...
gi 71995606 485 KAI 487
Cdd:PRK09407 486 QTI 488
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
32-487 |
4.33e-92 |
|
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: 287.67 E-value: 4.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 32 IEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIA---IWEVKTNGKPIYEARC 108
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLdliQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 109 DIASSADtfdFFGGIATAVLQGdslELPGGPSQRIAYTR--REPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPS 186
Cdd:cd07101 81 DVAIVAR---YYARRAERLLKP---RRRRGAIPVLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 187 PFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHnlVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSE 265
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPgSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG-RRLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 266 IIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQRI 345
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFV-ARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 346 LGYVESAKQEGGVVLRGGvRVHPTgvEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAA 425
Cdd:cd07101 311 TAHVDDAVAKGATVLAGG-RARPD--LGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995606 426 GVFSGNLARGHRVAARLQAGTVFIN-TYNDT--EVNVPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
15-472 |
1.86e-91 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 287.19 E-value: 1.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARCDIASSADTFDFFGGIATAVLqGDSLelPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPA 174
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIY-GDTI--PGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 175 LAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQ-EAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtKNV 253
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA-KDI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 254 KPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIvQEANDKLKVGDPLLEDTRV 333
Cdd:PRK11241 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKL-QQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 334 GANINEGHLQRILGYVESAKQEGGVVLRGGvRVHPTGvegGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVI 413
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGG-KAHELG---GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 414 ARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRE 472
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGRE 463
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
33-487 |
1.37e-89 |
|
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: 281.50 E-value: 1.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 33 EPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC-DIA 111
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLgEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 112 SSADTFDFFGGIATAVLQGDSLELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPA 191
Cdd:cd07098 82 VTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 192 SPVLLGEI----LTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRqAATKNVKPVTLELGGKSEII 267
Cdd:cd07098 162 SSGFFLSIirecLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMA-AAAESLTPVVLELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 268 IFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEaIVQEANDKLKVGDPLLEDTRVGANINEGHLQRILG 347
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLE-ILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 348 YVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGV 427
Cdd:cd07098 320 LVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71995606 428 FSGNLARGHRVAARLQAGTVFINTYNDTEVNV--PFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07098 400 FGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
77-489 |
3.12e-85 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 268.53 E-value: 3.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 77 LHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSADTFDFFGGIAT----AVLQGDSlelpggPSQRIaYTRREPYG 152
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegEIIQSDR------PGENI-LLFKRALG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 153 VVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAK 231
Cdd:PRK10090 74 VTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRgETVGQELAGNPKVAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 232 VSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTE 311
Cdd:PRK10090 154 VSMTGSVSAGEKIM-AAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 312 AIVqEANDKLKVGDPLLEDT-RVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHptgvEGGAYFEPAIITGLSDEAR 390
Cdd:PRK10090 233 RLG-EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 391 AVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHG 470
Cdd:PRK10090 308 IMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIG 387
|
410
....*....|....*....
gi 71995606 471 RENCIDTLRAHTQTKAIYV 489
Cdd:PRK10090 388 GADGKHGLHEYLQTQVVYL 406
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
16-487 |
1.01e-81 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 262.56 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 16 LNGKRttIESTETFDVIEP-RIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:PRK03137 41 IGGER--ITTEDKIVSINPaNKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARCDIASSADTFDFFGGIATAVLQGDSLELPGGPSQRIAYtrrEPYGVVGCIGAWNYPFQTCVWKVAPA 174
Cdd:PRK03137 119 LVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYFY---IPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 175 LAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASG-----EAVQRQA 248
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSgSEVGDYLVDHPKTRFITFTGSREVGlriyeRAAKVQP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 249 ATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPlL 328
Cdd:PRK03137 276 GQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTK-ELTVGNP-E 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 329 EDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGvrvhpTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFET 408
Cdd:PRK03137 354 DNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGE-----GDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 409 EEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTyNDTEVNV---PFGGFKNSG-HGRENCIDTLRAHTQT 484
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNR-GCTGAIVgyhPFGGFNMSGtDSKAGGPDYLLLFLQA 507
|
...
gi 71995606 485 KAI 487
Cdd:PRK03137 508 KTV 510
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
51-471 |
2.65e-80 |
|
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: 256.43 E-value: 2.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSAdtfdffGGIATAVLQG 130
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMA------GKIDISIKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 131 DSL----ELPGGpsQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVP 206
Cdd:cd07095 76 HERtgerATPMA--QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 207 KGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANF 286
Cdd:cd07095 154 PGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 287 LNQGQVCTNATRVFVQKGILA-SFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVR 365
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGAVGdAFLERLV-EAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 366 vhptGVEGGAYFEPAII--TGLSDEAravREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQ 443
Cdd:cd07095 313 ----LVAGTAFLSPGIIdvTDAADVP---DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420
....*....|....*....|....*....
gi 71995606 444 AGTVFIN-TYNDTEVNVPFGGFKNSGHGR 471
Cdd:cd07095 386 AGIVNWNrPTTGASSTAPFGGVGLSGNHR 414
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
32-472 |
7.41e-79 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 253.63 E-value: 7.41e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 32 IEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIA 111
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 112 SSADTFDFFGGIATAVLQGDSlELPGGPSQRIAYtrrEPYGVVGCIGAWNYPfqtcVWKV----APALAAGNAVVYKPSP 187
Cdd:PRK13968 92 KSANLCDWYAEHGPAMLKAEP-TLVENQQAVIEY---RPLGTILAIMPWNFP----LWQVmrgaVPILLAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 188 FAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKnVKPVTLELGGKSEII 267
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 268 IFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANI-----NEGHL 342
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFV-AAAAALKMGDPRDEENALGPMArfdlrDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 343 QrilgyVESAKQEGGVVLRGGVRVhptgvEG-GAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTY 421
Cdd:PRK13968 322 Q-----VEATLAEGARLLLGGEKI-----AGaGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 71995606 422 GLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRE 472
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
132-471 |
8.36e-71 |
|
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: 231.65 E-value: 8.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 132 SLELPGGPSQriAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAgVPKGVYN 211
Cdd:cd07087 84 SVPLLLQPAK--AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 212 VIQGEQEAGVALCEHNLvAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQ 291
Cdd:cd07087 161 VVEGGVEVATALLAEPF-DHIFFTGSPAVGKIVMEAAA-KHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 292 VCTNATRVFVQKGILASFTEAIVQEANDKLkvGDPLLEDTRVGANINEGHLQRILGYVESAKqeggvVLRGGvrvhpTGV 371
Cdd:cd07087 239 TCIAPDYVLVHESIKDELIEELKKAIKEFY--GEDPKESPDYGRIINERHFDRLASLLDDGK-----VVIGG-----QVD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 372 EGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVfinT 451
Cdd:cd07087 307 KEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV---C 383
|
330 340
....*....|....*....|....*
gi 71995606 452 YNDTEV-----NVPFGGFKNSGHGR 471
Cdd:cd07087 384 VNDVLLhaaipNLPFGGVGNSGMGA 408
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
32-472 |
1.06e-68 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 226.93 E-value: 1.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 32 IEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIA 111
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 112 SSADTFDFFGGIATAVLQGDSLELPGGPSQRiAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPA 191
Cdd:PRK09406 86 KCAKGFRYYAEHAEALLADEPADAAAVGASR-AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 192 SPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIIIFDD 271
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVA-AIAGDEIKKTVLELGGSDPFIVMPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 272 SDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHLQRILGYVES 351
Cdd:PRK09406 244 ADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFV-ARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 352 AKQEGGVVLRGGVRvhPTGveGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGN 431
Cdd:PRK09406 323 AVAAGATILCGGKR--PDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRD 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 71995606 432 LARGHRVAARLQAGTVFINTYNDTEVNVPFGGFKNSGHGRE 472
Cdd:PRK09406 399 EAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRE 439
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
25-472 |
1.02e-67 |
|
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: 224.78 E-value: 1.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 25 STETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAI---WEVktnGK 101
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKlvsLEM---GK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 102 PIYEARCDIASSADTFDFfggiatAVlqGDSLELPGG--PSQRIAYTRRE---PYGVVGCIGAWNYPFQTCVWKVAPALA 176
Cdd:cd07130 87 ILPEGLGEVQEMIDICDF------AV--GLSRQLYGLtiPSERPGHRMMEqwnPLGVVGVITAFNFPVAVWGWNAAIALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 177 AGNAVVYKPSPFAPASPV----LLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKN 252
Cdd:cd07130 159 CGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 253 VKpVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQeANDKLKVGDPLLEDTR 332
Cdd:cd07130 239 GR-SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKK-AYKQVRIGDPLDDGTL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 333 VGANINEGHLQRILGYVESAKQEGGVVLRGGVRVhptgVEGGAYFEPAIITGLSDeARAVREEIFGAVMLILPFETEEEV 412
Cdd:cd07130 317 VGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVI----DGPGNYVEPTIVEGLSD-APIVKEETFAPILYVLKFDTLEEA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995606 413 IARANNTTYGLAAGVFSGNLARGHRV--AARLQAGTVFINT-YNDTEVNVPFGGFKNSGHGRE 472
Cdd:cd07130 392 IAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIgTSGAEIGGAFGGEKETGGGRE 454
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
27-471 |
4.01e-67 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 223.68 E-value: 4.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 27 ETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEA 106
Cdd:PRK09457 15 EAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 107 RCDIASSAdtfdffGGIATAVLQGD------SLELPGGpsqrIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNA 180
Cdd:PRK09457 95 ATEVTAMI------NKIAISIQAYHertgekRSEMADG----AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 181 VVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNVKPVTLEL 260
Cdd:PRK09457 165 VVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILALEM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 261 GGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANDKLKVGDPLLEDTR-VGANINE 339
Cdd:PRK09457 245 GGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 340 GHLQRILGYVESAKQEGGVVLrggvrVHPTGVEGGAYF-EPAIITgLSDEARAVREEIFGAVMLILPFETEEEVIARANN 418
Cdd:PRK09457 325 QAAQGLVAAQAQLLALGGKSL-----LEMTQLQAGTGLlTPGIID-VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 71995606 419 TTYGLAAGVFSGNLARGHRVAARLQAGTVFIN-TYNDTEVNVPFGGFKNSGHGR 471
Cdd:PRK09457 399 TRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkPLTGASSAAPFGGVGASGNHR 452
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
30-487 |
1.73e-66 |
|
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: 221.14 E-value: 1.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 30 DVIEPRIGQVVAKCPKATADIVDQYVKAAADA---QSAWgeTTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEA 106
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALfldRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 107 RCDIASSADTFDFfggIATAVLQGDSLELPGGPSQ----RIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVV 182
Cdd:cd07148 80 KVEVTRAIDGVEL---AADELGQLGGREIPMGLTPasagRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 183 YKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAAtknvkPVT---LE 259
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-----PGTrcaLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 260 LGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVGDPLLEDTRVGANINE 339
Cdd:cd07148 232 HGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAA-EKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 340 GHLQRILGYVESAKQEGGVVLRGGVRVHPTgveggaYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNT 419
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDT------TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71995606 420 TYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVN-VPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07148 385 PVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYGTGGIPYTMHDMTQEKMA 453
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
145-470 |
6.76e-62 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 210.27 E-value: 6.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 145 YTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAgVPKGVYNVIQGEQEAGVALC 224
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 225 EHNLvAKVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKG 304
Cdd:PTZ00381 183 KEPF-DHIFFTGSPRVGKLVM-QAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 305 ILASFTEAIVQEAndKLKVGDPLLEDTRVGANINEGHLQRIlgyVESAKQEGGVVLRGGvrvhPTGVEgGAYFEPAIITG 384
Cdd:PTZ00381 261 IKDKFIEALKEAI--KEFFGEDPKKSEDYSRIVNEFHTKRL---AELIKDHGGKVVYGG----EVDIE-NKYVAPTIIVN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 385 LSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFIN--TYNDTEVNVPFG 462
Cdd:PTZ00381 331 PDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFG 410
|
....*...
gi 71995606 463 GFKNSGHG 470
Cdd:PTZ00381 411 GVGNSGMG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
144-472 |
6.81e-62 |
|
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: 208.49 E-value: 6.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 144 AYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVyNVIQGEQEAGVAL 223
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVVTGGADVAAAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 224 CE----HnLVakvsFTGSVASGEAVQRqAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRV 299
Cdd:cd07133 174 SSlpfdH-LL----FTGSTAVGRHVMR-AAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 300 FVQKGILASFTEAIVQEANdKL---KVGDPllEDTRVganINEGHLQRILGYVESAKQEGGVVlrggVRVHPTG--VEGG 374
Cdd:cd07133 248 LVPEDKLEEFVAAAKAAVA-KMyptLADNP--DYTSI---INERHYARLQGLLEDARAKGARV----IELNPAGedFAAT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 375 AYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFIntyND 454
Cdd:cd07133 318 RKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTI---ND 394
|
330 340
....*....|....*....|....*..
gi 71995606 455 TEVNV-----PFGGFKNSG----HGRE 472
Cdd:cd07133 395 TLLHVaqddlPFGGVGASGmgayHGKE 421
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
62-471 |
3.71e-61 |
|
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: 206.31 E-value: 3.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 62 QSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEAR-CDIASSADTFDFfggiATAVLQ--------GDS 132
Cdd:cd07134 11 ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEILPVLSEINH----AIKHLKkwmkpkrvRTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 133 LELPGGPSQrIAYtrrEPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVyNV 212
Cdd:cd07134 87 LLLFGTKSK-IRY---EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 213 IQGEQEAGVALCE----HnlvakVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLN 288
Cdd:cd07134 162 FEGDAEVAQALLElpfdH-----IFFTGSPAVGKIVM-AAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 289 QGQVCTNATRVFVQKGILASFTEAIVQE------ANDKLKVGDPLledTRVganINEGHLQRILGYVESAKQEGGVVLRG 362
Cdd:cd07134 236 AGQTCIAPDYVFVHESVKDAFVEHLKAEiekfygKDAARKASPDL---ARI---VNDRHFDRLKGLLDDAVAKGAKVEFG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 363 GVRvhptgVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARL 442
Cdd:cd07134 310 GQF-----DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
410 420 430
....*....|....*....|....*....|....
gi 71995606 443 QAGTVfinTYNDT-----EVNVPFGGFKNSGHGR 471
Cdd:cd07134 385 SSGGV---VVNDVvlhflNPNLPFGGVNNSGIGS 415
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
15-470 |
1.59e-60 |
|
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: 207.05 E-value: 1.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTtiESTETFDVIEP-RIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEE--- 90
Cdd:cd07125 36 IINGEET--ETGEGAPVIDPaDHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGElia 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 91 IAIWEVktnGKPIYEARCDIASSADTFDFFGGIATAVLQGDSLELPGGPSQRIAYtrrEPYGVVGCIGAWNYPFQTCVWK 170
Cdd:cd07125 114 LAAAEA---GKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLEL---HGRGVFVCISPWNFPLAIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 171 VAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAA 249
Cdd:cd07125 188 IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDgEEIGEALVAHPRIDGVIFTGSTETAKLINRALA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 250 TKNVKPVTL--ELGGKSEIIIfdDSD------VKSAVASAmlanFLNQGQVCTnATRV-FVQKGILASFTEAIVqEANDK 320
Cdd:cd07125 268 ERDGPILPLiaETGGKNAMIV--DSTalpeqaVKDVVQSA----FGSAGQRCS-ALRLlYLQEEIAERFIEMLK-GAMAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 321 LKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGgvrvhPTGVEGGAYFEPAI--ITGLSDearaVREEIFG 398
Cdd:cd07125 340 LKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPA-----PLDDGNGYFVAPGIieIVGIFD----LTTEVFG 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995606 399 AVMLILPFETE--EEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTyNDTE--VNV-PFGGFKNSGHG 470
Cdd:cd07125 411 PILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-NITGaiVGRqPFGGWGLSGTG 486
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
37-487 |
2.42e-60 |
|
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: 206.28 E-value: 2.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 37 GQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSADT 116
Cdd:cd07083 43 SEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 117 FDFFGGIATAvLQGDSLELPGGPSQrIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLL 196
Cdd:cd07083 123 IRYYARAALR-LRYPAVEVVPYPGE-DNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 197 GEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATK-----NVKPVTLELGGKSEIIIFD 270
Cdd:cd07083 201 FEIFHEAGFPPGVVQFLPGVgEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLapgqtWFKRLYVETGGKNAIIVDE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 271 DSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEaIVQEANDKLKVGDPLLEDTRVGANINEGHLQRILGYVE 350
Cdd:cd07083 281 TADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLE-RLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 351 SAKQEGGVVLRGGVrvhPTGVegGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEE--EVIARANNTTYGLAAGVF 428
Cdd:cd07083 360 HGKNEGQLVLGGKR---LEGE--GYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVY 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995606 429 SGNLARGHRVAARLQAGTVFINTyNDTEVNV---PFGGFKNSGHG-RENCIDTLRAHTQTKAI 487
Cdd:cd07083 435 SRKREHLEEARREFHVGNLYINR-KITGALVgvqPFGGFKLSGTNaKTGGPHYLRRFLEMKAV 496
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
144-472 |
4.22e-60 |
|
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: 204.28 E-value: 4.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 144 AYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYnVIQGEQEAGVAL 223
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA-VVEGGVEENQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 224 CEHNlVAKVSFTGSVASGEAVQRQAAtKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQK 303
Cdd:cd07136 173 LDQK-FDYIFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 304 GILASFTEAIVQEANDKLkvGDPLLEDTRVGANINEGHLQRILGYVESAKqeggVVLRGGVRvhptgvEGGAYFEPAIIT 383
Cdd:cd07136 251 SVKEKFIKELKEEIKKFY--GEDPLESPDYGRIINEKHFDRLAGLLDNGK----IVFGGNTD------RETLYIEPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 384 GLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFIntyNDTEV-----N 458
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCI---NDTIMhlanpY 395
|
330
....*....|....*...
gi 71995606 459 VPFGGFKNSG----HGRE 472
Cdd:cd07136 396 LPFGGVGNSGmgsyHGKY 413
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
77-471 |
5.35e-60 |
|
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: 203.61 E-value: 5.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 77 LHKVADLIREHAEEIAIWEVKTNGKPIYEARcdiasSADTFDFFGGIATAVLQGDSL---ELPGGPSQRI----AYTRRE 149
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETL-----LTEVSGVKNDILHMLKNLKKWakdEKVKDGPLAFmfgkPRIRKE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 150 PYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAgVPKGVYNVIQGEQEAGVALCEHNLv 229
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKF- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 230 AKVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASF 309
Cdd:cd07135 186 DKIFYTGSGRVGRIIA-EAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 310 TEAIVQEANDKLKVGDPLLED-TRVganINEGHLQRILGYVESAKqeGGVVLRGgvrvhpTGVEGGAYFEPAIITGLSDE 388
Cdd:cd07135 265 VEELKKVLDEFYPGGANASPDyTRI---VNPRHFNRLKSLLDTTK--GKVVIGG------EMDEATRFIPPTIVSDVSWD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 389 ARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVfinTYNDTEV-----NVPFGG 463
Cdd:cd07135 334 DSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGV---VINDTLIhvgvdNAPFGG 410
|
....*...
gi 71995606 464 FKNSGHGR 471
Cdd:cd07135 411 VGDSGYGA 418
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
14-490 |
1.05e-59 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 204.22 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 14 YFLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAI 93
Cdd:PLN00412 18 YYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 94 WEVKTNGKPIYEARCDIASSADTFDFFGGIATAVL-QGDSL---ELPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVW 169
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILgEGKFLvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 170 KVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGE-QEAGVALCEHNLVAKVSFTGSvASGEAVQRQA 248
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMHPGVNCISFTGG-DTGIAISKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 249 AtknVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEANdKLKVGDPlL 328
Cdd:PLN00412 257 G---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVA-KLTVGPP-E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 329 EDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRvhptgvEGGAYFePAIITGLSDEARAVREEIFGAVMLILPFET 408
Cdd:PLN00412 332 DDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR------EGNLIW-PLLLDNVRPDMRIAWEEPFGPVLPVIRINS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 409 EEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTYNDTEVN-VPFGGFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:PLN00412 405 VEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKST 484
|
...
gi 71995606 488 YVN 490
Cdd:PLN00412 485 VIN 487
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
36-470 |
3.87e-53 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 193.11 E-value: 3.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 36 IGQVVAkcpkATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSAD 115
Cdd:PRK11904 576 VGEVAF----ADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVD 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 116 TFDFFGGIATAVLqGDSLELPG--GPSQRIaytRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASP 193
Cdd:PRK11904 652 FCRYYAAQARRLF-GAPEKLPGptGESNEL---RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIA 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 194 VLLGEILTAAGVPKGVYNVIQGEQEA-GVALCEHNLVAKVSFTGSVASGEAVQRQAATKNVKPVTL--ELGGKSEIIIfd 270
Cdd:PRK11904 728 AEAVKLLHEAGIPKDVLQLLPGDGATvGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLiaETGGQNAMIV-- 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 271 DSD------VKSAVASAmlanFLNQGQVCTnATRV-FVQKGIlASFTEAIVQEANDKLKVGDPLLEDTRVGANINEGHLQ 343
Cdd:PRK11904 806 DSTalpeqvVDDVVTSA----FRSAGQRCS-ALRVlFVQEDI-ADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKA 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 344 RILGYVESAKQEGGVVLRGGVrvhPTGVEGGAYFEPAI--ITGLSDearaVREEIFGAVMLILPFETEE--EVIARANNT 419
Cdd:PRK11904 880 NLDAHIERMKREARLLAQLPL---PAGTENGHFVAPTAfeIDSISQ----LEREVFGPILHVIRYKASDldKVIDAINAT 952
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 71995606 420 TYGLAAGVFSGNLARGHRVAARLQAGTVFINTyNDTE--VNV-PFGGFKNSGHG 470
Cdd:PRK11904 953 GYGLTLGIHSRIEETADRIADRVRVGNVYVNR-NQIGavVGVqPFGGQGLSGTG 1005
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
15-464 |
6.14e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 188.42 E-value: 6.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 15 FLNGKRTTIESTETFDVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIW 94
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARCDIASSADTFDFFGGIATavLQGDSLeLPGGPSQRIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPA 174
Cdd:PLN02419 197 ITTEQGKTLKDSHGDIFRGLEVVEHACGMAT--LQMGEY-LPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 175 LAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNvK 254
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG-K 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 255 PVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTN-ATRVFVqkGILASFTEAIVQEANdKLKVGDPLLEDTRV 333
Cdd:PLN02419 353 RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFV--GDAKSWEDKLVERAK-ALKVTCGSEPDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 334 GANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVI 413
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAI 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 71995606 414 ARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTynDTEVNVPFGGF 464
Cdd:PLN02419 510 SIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSF 558
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
144-471 |
3.75e-50 |
|
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: 177.41 E-value: 3.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 144 AYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILtaagvPKGV----YNVIQGEQEA 219
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-----PKYLdkecYPVVLGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 220 GVALCEHNLvAKVSFTGSVASGEAVqRQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRV 299
Cdd:cd07132 169 TTELLKQRF-DYIFYTGSTSVGKIV-MQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 300 FVQKGILasftEAIVQEANDKLK--VGDPLLEDTRVGANINEGHLQRILGYVESAKqeggvVLRGGvrvhpTGVEGGAYF 377
Cdd:cd07132 247 LCTPEVQ----EKFVEALKKTLKefYGEDPKESPDYGRIINDRHFQRLKKLLSGGK-----VAIGG-----QTDEKERYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 378 EPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVfinTYNDTEV 457
Cdd:cd07132 313 APTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGV---CVNDTIM 389
|
330
....*....|....*....
gi 71995606 458 -----NVPFGGFKNSGHGR 471
Cdd:cd07132 390 hytldSLPFGGVGNSGMGA 408
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
32-490 |
6.44e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.49 E-value: 6.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 32 IEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIA 111
Cdd:PLN02315 39 VNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 112 SSADTFDFFGGIatavlqgdSLELPGG--PSQRIAYTRRE---PYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPS 186
Cdd:PLN02315 119 EIIDMCDFAVGL--------SRQLNGSiiPSERPNHMMMEvwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 187 PFAP----ASPVLLGEILTAAGVPKGVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNVKPVtLELGG 262
Cdd:PLN02315 191 PTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCL-LELSG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 263 KSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVqEANDKLKVGDPLLEDTRVGANINEGHL 342
Cdd:PLN02315 270 NNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLL-TVYKQVKIGDPLEKGTLLGPLHTPESK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 343 QRILGYVESAKQEGGVVLRGGVRVHPtgveGGAYFEPAIITgLSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYG 422
Cdd:PLN02315 349 KNFEKGIEIIKSQGGKILTGGSAIES----EGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQG 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995606 423 LAAGVFSgnlaRGHRVAARL------QAGTVFINT-YNDTEVNVPFGGFKNSGHGRENCIDTLRAHTQTKAIYVN 490
Cdd:PLN02315 424 LSSSIFT----RNPETIFKWigplgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTIN 494
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
37-470 |
1.09e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 171.59 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 37 GQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEE---IAIWEV-KTNGKPIYEARcdias 112
Cdd:PRK11905 578 DDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPElfaLAVREAgKTLANAIAEVR----- 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 113 saDTFDFFGGIATavlQGDSLELPggpsqriayTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPspfAPAS 192
Cdd:PRK11905 653 --EAVDFLRYYAA---QARRLLNG---------PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKP---AEQT 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 193 PVLLG---EILTAAGVPKGVYNVIQGEQEA-GVALCEHNLVAKVSFTGSVASGEAVQRQAATKNVKPVTL--ELGGKSEI 266
Cdd:PRK11905 716 PLIAAravRLLHEAGVPKDALQLLPGDGRTvGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAM 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 267 IIfdDSD------VKSAVASAmlanFLNQGQVCTnATRV-FVQKGILASFTEAIvQEANDKLKVGDPLLEDTRVGANINE 339
Cdd:PRK11905 796 IV--DSSalpeqvVADVIASA----FDSAGQRCS-ALRVlCLQEDVADRVLTML-KGAMDELRIGDPWRLSTDVGPVIDA 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 340 GHLQRILGYVESAKQEGGVVLRGGVrvhPTGVEGGAYFEPAII--TGLSDearaVREEIFGAVMLILPFETEE--EVIAR 415
Cdd:PRK11905 868 EAQANIEAHIEAMRAAGRLVHQLPL---PAETEKGTFVAPTLIeiDSISD----LEREVFGPVLHVVRFKADEldRVIDD 940
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995606 416 ANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTyndtevNV--------PFGGFKNSGHG 470
Cdd:PRK11905 941 INATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR------NIigavvgvqPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
36-470 |
1.56e-45 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 171.27 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 36 IGQVVAkcpkATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEI--------------AIWEVKtngk 101
Cdd:COG4230 584 VGTVVE----ATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELmallvreagktlpdAIAEVR---- 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 102 piyEArcdiassadtFDF---FGGIATAVLQGDslelpggpsqriayTRREPYGVVGCIGAWNYP---F--QtcvwkVAP 173
Cdd:COG4230 656 ---EA----------VDFcryYAAQARRLFAAP--------------TVLRGRGVFVCISPWNFPlaiFtgQ-----VAA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 174 ALAAGNAVVYKPspfAPASPvLLG----EILTAAGVPKGVYNVIQGEQEA-GVALCEHNLVAKVSFTGSVASGEAVQRQA 248
Cdd:COG4230 704 ALAAGNTVLAKP---AEQTP-LIAaravRLLHEAGVPADVLQLLPGDGETvGAALVADPRIAGVAFTGSTETARLINRTL 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 249 ATKNVKPVTL--ELGGKSEIIIfdDS---------DVksaVASAmlanFLNQGQVCtNATRV-FVQKGIlASFTEAIVQE 316
Cdd:COG4230 780 AARDGPIVPLiaETGGQNAMIV--DSsalpeqvvdDV---LASA----FDSAGQRC-SALRVlCVQEDI-ADRVLEMLKG 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 317 ANDKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVrvhPTGVEGGAYFEPAI--ITGLSDearaVRE 394
Cdd:COG4230 849 AMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPL---PEECANGTFVAPTLieIDSISD----LER 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 395 EIFGAVMLILPFETEE--EVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFINTyndtevNV--------PFGGF 464
Cdd:COG4230 922 EVFGPVLHVVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR------NIigavvgvqPFGGE 995
|
....*.
gi 71995606 465 KNSGHG 470
Cdd:COG4230 996 GLSGTG 1001
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
17-468 |
1.54e-43 |
|
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: 161.22 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 17 NGKRttIESTETFDVIEP-RIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIR-EHAEEIAIW 94
Cdd:cd07123 38 GGKE--VRTGNTGKQVMPhDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 95 EVKTNGKPIYEARCD-IASSADTFDFFGGIATAVLQGDSLELPGGPSQRIAYTRREpyGVVGCIGAWNYpfqTCV---WK 170
Cdd:cd07123 116 TMLGQGKNVWQAEIDaACELIDFLRFNVKYAEELYAQQPLSSPAGVWNRLEYRPLE--GFVYAVSPFNF---TAIggnLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 171 VAPALAaGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVYNVIQGEQEA-GVALCEHNLVAKVSFTGSVASGEAVQRQAA 249
Cdd:cd07123 191 GAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVvGDTVLASPHLAGLHFTGSTPTFKSLWKQIG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 250 T-----KNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGILASFTEAIVQEAnDKLKVG 324
Cdd:cd07123 270 EnldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEEL-KEIKMG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 325 DPLLEDTRVGANINEGHLQRILGYVESAKQEGGV-VLRGGvrvHPTGVEGgaYF-EPAIITGLSDEARAVREEIFGAVML 402
Cdd:cd07123 349 DPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAeIIAGG---KCDDSVG--YFvEPTVIETTDPKHKLMTEEIFGPVLT 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71995606 403 ILPFETE--EEVIARANNTT-YGLAAGVFSGNLA--RGHRVAARLQAGTVFINTYNDTEVnV---PFGGFKNSG 468
Cdd:cd07123 424 VYVYPDSdfEETLELVDTTSpYALTGAIFAQDRKaiREATDALRNAAGNFYINDKPTGAV-VgqqPFGGARASG 496
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
33-470 |
4.80e-43 |
|
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: 159.31 E-value: 4.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 33 EPRIgqVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIAS 112
Cdd:TIGR01238 60 DRRD--IVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVRE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 113 SADTFDFFGGIATAVLQGDSLElpggpsqriaytrrePYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPAS 192
Cdd:TIGR01238 138 AVDFCRYYAKQVRDVLGEFSVE---------------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 193 PVLLGEILTAAGVPKGVYNVIQGEQE-AGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNVKPVTL--ELGGKSEIIIF 269
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGAdVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 270 DDSDVKSAVASAMLANFLNQGQVCTNATRVFVQKGIlASFTEAIVQEANDKLKVGDPLLEDTRVGANINEGHLQRILGYV 349
Cdd:TIGR01238 283 STALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV-ADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 350 ESAKQEGGVVLRgGVRVHPTGVEGGAYFEPAIITglSDEARAVREEIFGAVMLILPFETEE--EVIARANNTTYGLAAGV 427
Cdd:TIGR01238 362 EHMSQTQKKIAQ-LTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGV 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71995606 428 FSGNLARGHRVAARLQAGTVFIN-TYNDTEVNV-PFGGFKNSGHG 470
Cdd:TIGR01238 439 HSRIETTYRWIEKHARVGNCYVNrNQVGAVVGVqPFGGQGLSGTG 483
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
149-487 |
1.25e-41 |
|
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: 154.11 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 149 EPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVyNVIQGEQEAGVALCEHNL 228
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI-KVIEGGVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 229 vAKVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANF-LNQGQVCTNATRVFVQKGILA 307
Cdd:cd07137 179 -DKIFFTGSPRVGRIIM-AAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 308 SFTEAIVQEAndKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRvhptgvEGGAYFEPAIITGLSD 387
Cdd:cd07137 257 TLIDALKNTL--EKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERD------EKNLYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 388 EARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVfinTYNDTEVNV-----PFG 462
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV---TFNDTVVQYaidtlPFG 405
|
330 340
....*....|....*....|....*
gi 71995606 463 GFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:cd07137 406 GVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
149-471 |
1.03e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 141.40 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 149 EPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVyNVIQGEQEAGVALCEHNL 228
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV-KVIEGGPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 229 vAKVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIII--FDDS-DVKSAVASAMLANFLN-QGQVCTNATRVFVQKG 304
Cdd:PLN02203 186 -DKIFFTGSPRVGRIIM-TAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 305 ILASFTEAIvqEANDKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRvhptgvEGGAYFEPAIITG 384
Cdd:PLN02203 264 FAPILIELL--KSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSID------EKKLFIEPTILLN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 385 LSDEARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVfinTYNDTEV-----NV 459
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAIIqyacdSL 412
|
330
....*....|..
gi 71995606 460 PFGGFKNSGHGR 471
Cdd:PLN02203 413 PFGGVGESGFGR 424
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
51-480 |
3.77e-32 |
|
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: 128.12 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARcDIASSADTFDFFGGIATA--VL 128
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYSyrIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 129 QGDSLELPGGPSQRIAYtRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAG-VPK 207
Cdd:cd07084 80 HEPGNHLGQGLKQQSHG-YRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 208 GVYNVIQGEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAATknvKPVTLELGGKSEIIIFDDSDVKSAVASAMLAN-F 286
Cdd:cd07084 159 EDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ---ARIYLELAGFNWKVLGPDAQAVDYVAWQCVQDmT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 287 LNQGQVCTNATRVFVQKgilASFTEAIVQEANDKLKVGDPllEDTRVGANINEGHLQRIlgyvESAKQEGGVVLRGG--- 363
Cdd:cd07084 236 ACSGQKCTAQSMLFVPE---NWSKTPLVEKLKALLARRKL--EDLLLGPVQTFTTLAMI----AHMENLLGSVLLFSgke 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 364 VRVHPTGVEGGAYFEPAIITgLSDEA----RAVREEIFGAVMLILPFETEEE--VIARANNTTYGLAAGVFSGNLARGHR 437
Cdd:cd07084 307 LKNHSIPSIYGACVASALFV-PIDEIlktyELVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71995606 438 VAARLQ-AGTVFINTYNDTEVNVP-FGGFKNSGHGRENCIDTLRA 480
Cdd:cd07084 386 LIGNLWvAGRTYAILRGRTGVAPNqNHGGGPAADPRGAGIGGPEA 430
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
149-487 |
4.56e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 125.54 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 149 EPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEILTAAGVPKGVyNVIQGEQEAGVALCEHNL 228
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAV-RVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 229 vAKVSFTGSVASGEAVQrQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANF-LNQGQVCTNATRVFVQKGILA 307
Cdd:PLN02174 190 -DKIFYTGSSKIGRVIM-AAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 308 SFTEAIVQEAnDKLKVGDPlLEDTRVGANINEGHLQRiLGYVESAKQEGGVVLRGGVRVHPTgveggAYFEPAIITGLSD 387
Cdd:PLN02174 268 KVIDAMKKEL-ETFYGKNP-MESKDMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGEKDREN-----LKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 388 EARAVREEIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLARGHRVAARLQAGTVFIntyNDTEVN-----VPFG 462
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVV---NDIAVHlalhtLPFG 416
|
330 340
....*....|....*....|....*
gi 71995606 463 GFKNSGHGRENCIDTLRAHTQTKAI 487
Cdd:PLN02174 417 GVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-470 |
3.90e-29 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 122.00 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 39 VVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARCDIASSADTFD 118
Cdd:PRK11809 672 IVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 119 FFGGIATAVLQGDslelpggpsqriayTRRePYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKP---SPFAPASPVl 195
Cdd:PRK11809 752 YYAGQVRDDFDND--------------THR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPaeqTPLIAAQAV- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 196 lgEILTAAGVPKGVYNVIQGEQEA-GVALCEHNLVAKVSFTGSVASGEAVQRQAATK---NVKPVTL--ELGGKSEIIIf 269
Cdd:PRK11809 816 --RILLEAGVPAGVVQLLPGRGETvGAALVADARVRGVMFTGSTEVARLLQRNLAGRldpQGRPIPLiaETGGQNAMIV- 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 270 dDSD------VKSAVASAmlanFLNQGQVCTnATRVF-VQKGIlASFTEAIVQEANDKLKVGDPLLEDTRVGANINEGHL 342
Cdd:PRK11809 893 -DSSalteqvVADVLASA----FDSAGQRCS-ALRVLcLQDDV-ADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAK 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 343 QRILGYVESAKQEGGVVLRgGVRVHPTGVEGGAYFEPAIITgLSDEARaVREEIFGAVMLILPFETEE--EVIARANNTT 420
Cdd:PRK11809 966 ANIERHIQAMRAKGRPVFQ-AARENSEDWQSGTFVPPTLIE-LDSFDE-LKREVFGPVLHVVRYNRNQldELIEQINASG 1042
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71995606 421 YGLAAGVFS---GNLArghRVAARLQAGTVFINTyndtevNV--------PFGGFKNSGHG 470
Cdd:PRK11809 1043 YGLTLGVHTridETIA---QVTGSAHVGNLYVNR------NMvgavvgvqPFGGEGLSGTG 1094
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
51-432 |
2.35e-27 |
|
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: 114.18 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEE-IAIWEVKTnGKPiyEARCD--IASSADTFDFFggiATAV 127
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDElVARAHAET-GLP--EARLQgeLGRTTGQLRLF---ADLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 128 LQGDSLEL-------PGGPSQRIAYTRRE-PYGVVGCIGAWNYPF-------QTcvwkvAPALAAGNAVVYKPSPFAPAS 192
Cdd:cd07129 75 REGSWLDAridpadpDRQPLPRPDLRRMLvPLGPVAVFGASNFPLafsvaggDT-----ASALAAGCPVVVKAHPAHPGT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 193 PVLLGEILTAA----GVPKGVYNVIQGEQ-EAGVALCEHNLVAKVSFTGSVASGEAVQRQAATKNV-KPVTLELGGKSEI 266
Cdd:cd07129 150 SELVARAIRAAlratGLPAGVFSLLQGGGrEVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 267 IIFDD--SDVKSAVASAMLANF-LNQGQVCTNATRVFVQKGI-LASFTEAIVQEANDklKVGDPLLedtrvGANINEGHL 342
Cdd:cd07129 230 FILPGalAERGEAIAQGFVGSLtLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAA--APAQTML-----TPGIAEAYR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 343 QRilgyVESAKQEGGVVLRGGVRVHPTGVEGGAY-FEPAIITGLSDEarAVREEIFGAVMLILPFETEEEVIAranntty 421
Cdd:cd07129 303 QG----VEALAAAPGVRVLAGGAAAEGGNQAAPTlFKVDAAAFLADP--ALQEEVFGPASLVVRYDDAAELLA------- 369
|
410
....*....|.
gi 71995606 422 glAAGVFSGNL 432
Cdd:cd07129 370 --VAEALEGQL 378
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
30-431 |
3.36e-22 |
|
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: 99.65 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 30 DVIEPRIGQVVAKCPKATADIVDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEE---IAIWevktNGkpiyea 106
Cdd:cd07128 18 TLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDlyaLSAA----TG------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 107 rcdiASSADT-FDFFGGI----------------ATAVLQGDSLELPGGPS---QRIAYTRRepyGVVGCIGAWNYPfqt 166
Cdd:cd07128 88 ----ATRRDSwIDIDGGIgtlfayaslgrrelpnAHFLVEGDVEPLSKDGTfvgQHILTPRR---GVAVHINAFNFP--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 167 cVW----KVAPALAAGNAVVYKPspfAPASPVL---LGEILTAAGV-PKGVYNVIQGeqeaGVA-LCEHnLVAK--VSFT 235
Cdd:cd07128 158 -VWgmleKFAPALLAGVPVIVKP---ATATAYLteaVVKDIVESGLlPEGALQLICG----SVGdLLDH-LGEQdvVAFT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 236 GSVASGEAVQRQAA-TKNVKPVTLE--------LG-----GKSEIIIFddsdVKSaVASAMLANflnQGQVCTNATRVFV 301
Cdd:cd07128 229 GSAATAAKLRAHPNiVARSIRFNAEadslnaaiLGpdatpGTPEFDLF----VKE-VAREMTVK---AGQKCTAIRRAFV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 302 QKGILASFTEAIvQEANDKLKVGDPLLEDTRVGANINEGHLQRILGYVESAKQEGGVVLRGGVRVHPTGV--EGGAYFEP 379
Cdd:cd07128 301 PEARVDAVIEAL-KARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGAdaEKGAFFPP 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 71995606 380 AIITGLS-DEARAVRE-EIFGAVMLILPFETEEEVIARANNTTYGLAAGVFSGN 431
Cdd:cd07128 380 TLLLCDDpDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
117-433 |
2.78e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 87.45 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 117 FDFFGGIAT---------------AVLQGDSLELPGGP---SQRIAYTRRepyGVVGCIGAWNYPFQTCVWKVAPALAAG 178
Cdd:PRK11903 100 VDIDGGIFTlgyyaklgaalgdarLLRDGEAVQLGKDPafqGQHVLVPTR---GVALFINAFNFPAWGLWEKAAPALLAG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 179 NAVVYKPspfAPASPVL---LGEILTAAGV-PKGVYNVIQGeQEAGV--ALCEHNLVakvSFTGSVASGE------AVQR 246
Cdd:PRK11903 177 VPVIVKP---ATATAWLtqrMVKDVVAAGIlPAGALSVVCG-SSAGLldHLQPFDVV---SFTGSAETAAvlrshpAVVQ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 247 QAATKNVKPVTLELGgkseiIIFDDSDVKSAVASAMLANFLNQ-----GQVCTNATRVFVQKGILASFTEAIVqEANDKL 321
Cdd:PRK11903 250 RSVRVNVEADSLNSA-----LLGPDAAPGSEAFDLFVKEVVREmtvksGQKCTAIRRIFVPEALYDAVAEALA-ARLAKT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 322 KVGDPLLEDTRVGANINEGHLQRILGYVEsAKQEGGVVLRGGVRVHPTGVE-GGAYFEPAIITGLSD--EARAVRE-EIF 397
Cdd:PRK11903 324 TVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADpAVAACVGPTLLGASDpdAATAVHDvEVF 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 71995606 398 GAVMLILPFETEEEVIARANNTTYGLAAGVFSGNLA 433
Cdd:PRK11903 403 GPVATLLPYRDAAHALALARRGQGSLVASVYSDDAA 438
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
134-416 |
7.56e-14 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 73.67 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 134 ELPGGPSQRIAYTRR---EPYGVVGCIGAWNYPfqtcVWKVAPA----LAAGNAVVYKPSPFA--PASPVL--LGEILTA 202
Cdd:cd07127 174 EKPQGKHDPLAMEKTftvVPRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPHPAAilPLAITVqvAREVLAE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 203 AGVPKGVYNVIQGEQEAGVA--LCEHNLVAKVSFTGSVASG---EAVQRQAAtknvkpVTLELGGKSEIIIFDDSDVKSA 277
Cdd:cd07127 250 AGFDPNLVTLAADTPEEPIAqtLATRPEVRIIDFTGSNAFGdwlEANARQAQ------VYTEKAGVNTVVVDSTDDLKAM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 278 VASAMLANFLNQGQVCTNATRVFVQK-GI-----LASFTE--AIVQEANDKLkVGDPLLEDTRVGANINEGHLQRIlgyv 349
Cdd:cd07127 324 LRNLAFSLSLYSGQMCTTPQNIYVPRdGIqtddgRKSFDEvaADLAAAIDGL-LADPARAAALLGAIQSPDTLARI---- 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995606 350 ESAKQEGGVVLRGGVRVHPTgVEGGAYFEPAIITGLSDEARAVREEIFGAVMLILPFETEEEVIARA 416
Cdd:cd07127 399 AEARQLGEVLLASEAVAHPE-FPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
51-337 |
3.64e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 61.90 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARC--DIASSADTFDFFGGIAT-AV 127
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVikNHFAAEYIYNVYKDEKTcGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 128 LQGDSlelPGGpsqriAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPVLLGEIL----TAA 203
Cdd:cd07081 81 LTGDE---NGG-----TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLlqaaVAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 204 GVPKGVYNVI-QGEQEAGVALCEHNLVAKVSFTGsvasGEAVQrQAATKNVKPVTLELGGKSEIIIFDDSDVKSAVASAM 282
Cdd:cd07081 153 GAPENLIGWIdNPSIELAQRLMKFPGIGLLLATG----GPAVV-KAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71995606 283 LANFLNQGQVCTNATRVFVQKGILASFTE------AIVQEANDKLKVGDPLLEDTRVGANI 337
Cdd:cd07081 228 KSKTFDNGVICASEQSVIVVDSVYDEVMRlfegqgAYKLTAEELQQVQPVILKNGDVNRDI 288
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
73-323 |
4.78e-10 |
|
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: 61.47 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 73 RGKVLHKVADLIREHAEEIAIWEVKTNGKPI------YEARCDIASSA--DTFDFFGGIATA------VLQGDSLELpgg 138
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAYIrslianWIAMMGCSESKlyKNIDTERGITASvghiqdVLLPDNGET--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 139 psqriaYTRREPYGVVGCIGAWNYPFqTCVWKVAPALAAGNAVVYKPSPFAPAS----PVLLGEILTAAGVPKGVYNVIQ 214
Cdd:cd07077 95 ------YVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTnralALLFQAADAAHGPKILVLYVPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 215 GEQEAGVALCEHNLVAKVSFTGSVASGEAVQRQAatkNVKPVTLELGGKSEIIIFDDSDVKSAVASAMLANFLNQGQVCT 294
Cdd:cd07077 168 PSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS---PHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACAS 244
|
250 260
....*....|....*....|....*....
gi 71995606 295 NATRVFVQKGILASFTEAIVQEANDKLKV 323
Cdd:cd07077 245 EQNLYVVDDVLDPLYEEFKLKLVVEGLKV 273
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
51-248 |
5.12e-06 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 48.77 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARcdIASSADTFDFFGGI---ATAV 127
Cdd:cd07121 6 VDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDK--IAKNHLAAEKTPGTedlTTTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 128 LQGDslelpGGpsqrIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPV----LLGEILTAA 203
Cdd:cd07121 84 WSGD-----NG----LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAyaveLINKAIAEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71995606 204 GVPKGVYNVIQGEQ-EAGVALCEHNLVAKVSFTGsvasGEAVQRQA 248
Cdd:cd07121 155 GGPDNLVVTVEEPTiETTNELMAHPDINLLVVTG----GPAVVKAA 196
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
51-248 |
3.18e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 46.43 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 51 VDQYVKAAADAQSAWGETTALDRGKVLHKVADLIREHAEEIAIWEVKTNGKPIYEARcdIASSADTFDFFGGI---ATAV 127
Cdd:PRK15398 38 VDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDK--IAKNVAAAEKTPGVedlTTEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995606 128 LQGDslelpGGpsqrIAYTRREPYGVVGCIGAWNYPFQTCVWKVAPALAAGNAVVYKPSPFAPASPV----LLGEILTAA 203
Cdd:PRK15398 116 LTGD-----NG----LTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLraieLLNEAIVAA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71995606 204 GVPKGVYNVI-QGEQEAGVALCEHNLVAKVSFTGsvasGEAVQRQA 248
Cdd:PRK15398 187 GGPENLVVTVaEPTIETAQRLMKHPGIALLVVTG----GPAVVKAA 228
|
|
| |
