|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
1-418 |
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: 886.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07090 41 MERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSF 160
Cdd:cd07090 121 AGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 161 TGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVK 240
Cdd:cd07090 201 TGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 241 QTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDpKLKDGYYMRPCVLTNCRDDMTCVKE 320
Cdd:cd07090 281 RTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPED-GLENGFYVSPCVLTDCTDDMTIVRE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 321 EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENG 400
Cdd:cd07090 360 EIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENG 439
|
410
....*....|....*...
gi 1475409330 401 RVTIEYYSQLKTVCVEMG 418
Cdd:cd07090 440 TAALEHYTQLKTVYVEMG 457
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-424 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 719.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNGKSIFEAR-LDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGV 79
Cdd:PRK13252 66 MERSRILRRAVDILRERNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVS 159
Cdd:PRK13252 146 CAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:PRK13252 226 FTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiYVPEDPKLKDGYYMRPCVLTNCRDDMTCVK 319
Cdd:PRK13252 306 ERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGG--ERLTEGGFANGAFVAPTVFTDCTDDMTIVR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGREN 399
Cdd:PRK13252 384 EEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGREN 463
|
410 420
....*....|....*....|....*
gi 1475409330 400 GRVTIEYYSQLKTVCVEMGDVESAF 424
Cdd:PRK13252 464 GIATLEHYTQIKSVQVEMGPFQSPF 488
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-415 |
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: 600.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLP-GGSFGYTRREPLGVC 80
Cdd:COG1012 66 ERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:COG1012 146 GAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGdGSEVGAALVAHPDVDKIS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:COG1012 226 FTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLV 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpEDPKLKDGYYMRPCVLTNCRDDMTCVK 319
Cdd:COG1012 306 AAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGG-----RRPDGEGGYFVEPTVLADVTPDMRIAR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV-ELPFGGYKKSGFGRE 398
Cdd:COG1012 381 EEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVpQAPFGGVKQSGIGRE 460
|
410
....*....|....*..
gi 1475409330 399 NGRVTIEYYSQLKTVCV 415
Cdd:COG1012 461 GGREGLEEYTETKTVTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1-413 |
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: 600.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:pfam00171 51 AERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:pfam00171 131 GAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGsGAEVGEALVEHPDVRKVS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:pfam00171 211 FTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpeDPKLKDGYYMRPCVLTNCRDDMTCVK 319
Cdd:pfam00171 291 EAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGG------EAGLDNGYFVEPTVLANVTPDMRIAQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVE-LPFGGYKKSGFGRE 398
Cdd:pfam00171 365 EEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGRE 444
|
410
....*....|....*
gi 1475409330 399 NGRVTIEYYSQLKTV 413
Cdd:pfam00171 445 GGPYGLEEYTEVKTV 459
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
1-411 |
0e+00 |
|
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: 582.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNGKSIFEARL-DIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGV 79
Cdd:TIGR01804 57 MERGRILRRAADLIRERNEELAKLETLDTGKTLQETIVaDMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKV 158
Cdd:TIGR01804 137 CVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGdGAEVGPLLVNHPDVAKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:TIGR01804 217 SFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvPEDPKLKDGYYMRPCVLTNCRDDMTCV 318
Cdd:TIGR01804 297 VERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGR--PENVGLQNGFFVEPTVFADCTDDMTIV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:TIGR01804 375 REEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRE 454
|
410
....*....|...
gi 1475409330 399 NGRVTIEYYSQLK 411
Cdd:TIGR01804 455 NGKAALAHYTEVK 467
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
2-415 |
0e+00 |
|
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: 562.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLP-GGSFGYTRREPLGVC 80
Cdd:cd07078 21 ERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPdPGELAIVRREPLGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07078 101 GAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGdGDEVGAALASHPRVDKIS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:cd07078 181 FTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvpedPKLKDGYYMRPCVLTNCRDDMTCVK 319
Cdd:cd07078 261 ERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKR-----LEGGKGYFVPPTVLTDVDPDMPIAQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV-ELPFGGYKKSGFGRE 398
Cdd:cd07078 336 EEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEpSAPFGGVKQSGIGRE 415
|
410
....*....|....*..
gi 1475409330 399 NGRVTIEYYSQLKTVCV 415
Cdd:cd07078 416 GGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
2-415 |
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: 532.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEAR-LDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07093 42 ERARILHKVADLIEARADELALLESLDTGKPITLARtRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07093 122 GLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLIS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:cd07093 202 FTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyVPEDPKLKDGYYMRPCVLTNCRDDMTCVK 319
Cdd:cd07093 282 ERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGG--RPELPDLEGGYFVEPTVITGLDNDSRVAQ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGREN 399
Cdd:cd07093 360 EEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREG 439
|
410
....*....|....*.
gi 1475409330 400 GRVTIEYYSQLKTVCV 415
Cdd:cd07093 440 GDYSLEFYTELKNVCI 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
2-413 |
0e+00 |
|
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: 529.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARL-DIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07091 66 ERGRLLNKLADLIERDRDELAALESLDNGKPLEESAKgDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVC 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07091 146 GQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAK-GIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07091 226 FTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYvpedpkLKDGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07091 306 KARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERH------GSKGYFIQPTVFTDVKDDMKIA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:cd07091 380 KEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRE 459
|
410
....*....|....*
gi 1475409330 399 NGRVTIEYYSQLKTV 413
Cdd:cd07091 460 LGEEGLEEYTQVKAV 474
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
2-413 |
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: 515.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGS-FGYTRREPLGVC 80
Cdd:cd07114 44 ERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVIPVDKGDyLNFTRREPLGVV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07114 124 AAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGfGPETGEALVEHPLVAKIA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:cd07114 204 FTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyVPEDPKLKDGYYMRPCVLTNCRDDMTCVK 319
Cdd:cd07114 284 ARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGE--RPSGADLGAGYFFEPTILADVTNDMRIAQ 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGREN 399
Cdd:cd07114 362 EEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGREN 441
|
410
....*....|....
gi 1475409330 400 GRVTIEYYSQLKTV 413
Cdd:cd07114 442 GIEAIREYTQTKSV 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
2-413 |
2.04e-179 |
|
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: 509.16 E-value: 2.04e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCV 81
Cdd:cd07119 60 ERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 82 GIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAAT-GQFLCQHPDVAKVSF 160
Cdd:cd07119 140 LITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATvGAELAESPDVDLVSF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 161 TGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVK 240
Cdd:cd07119 220 TGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 241 QTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyVPEDPKLKDGYYMRPCVLTNCRDDMTCVKE 320
Cdd:cd07119 300 RAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGK--RPTGDELAKGYFVEPTIFDDVDRTMRIVQE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 321 EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENG 400
Cdd:cd07119 378 EIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELG 457
|
410
....*....|...
gi 1475409330 401 RVTIEYYSQLKTV 413
Cdd:cd07119 458 PTGLEEYQETKHI 470
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
2-415 |
5.74e-170 |
|
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: 483.86 E-value: 5.74e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEAR-LDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07115 42 ERGRILWRLAELILANADELARLESLDTGKPIRAARrLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07115 122 GAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKIT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:cd07115 202 FTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpEDPKLKdGYYMRPCVLTNCRDDMTCVK 319
Cdd:cd07115 282 SLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGG-----KRPGAR-GFFVEPTIFAAVPPEMRIAQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGREN 399
Cdd:cd07115 356 EEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREM 435
|
410
....*....|....*.
gi 1475409330 400 GRVTIEYYSQLKTVCV 415
Cdd:cd07115 436 GREALDEYTEVKSVWV 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
2-415 |
2.42e-163 |
|
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: 467.10 E-value: 2.42e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCV 81
Cdd:cd07109 43 ERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 82 GIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVSF 160
Cdd:cd07109 123 HIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 161 TGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVK 240
Cdd:cd07109 203 TGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 241 QTQRIKIGdPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvPEDPkLKDGYYMRPCVLTNCRDDMTCVKE 320
Cdd:cd07109 283 RFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARARARGARIVAGGRI--AEGA-PAGGYFVAPTLLDDVPPDSRLAQE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 321 EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSP-VELPFGGYKKSGFGREN 399
Cdd:cd07109 359 EIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREK 438
|
410
....*....|....*.
gi 1475409330 400 GRVTIEYYSQLKTVCV 415
Cdd:cd07109 439 GLEALYNYTQTKTVAV 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
2-415 |
2.33e-162 |
|
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: 464.60 E-value: 2.33e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIA---TMEcinNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLP-GGSFGYTRREPL 77
Cdd:cd07103 42 ERAAILRRWADLIRERAEDLArllTLE---QGKPLAEARGEVDYAASFLEWFAEEARRIYGRTIPSPaPGKRILVIKQPV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 GVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVA 156
Cdd:cd07103 119 GVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:cd07103 199 KISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpeDPKLKDGYYMRPCVLTNCRDDMT 316
Cdd:cd07103 279 KLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGG------KRLGLGGYFYEPTVLTDVTDDML 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFG 396
Cdd:cd07103 353 IMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLG 432
|
410
....*....|....*....
gi 1475409330 397 RENGRVTIEYYSQLKTVCV 415
Cdd:cd07103 433 REGGKEGLEEYLETKYVSL 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
2-417 |
7.37e-161 |
|
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: 461.88 E-value: 7.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFE-ARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07144 69 ERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVC 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07144 149 GQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:cd07144 229 FTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQT-QRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDPKlkdGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07144 309 EHVkQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGK---GYFIPPTIFTDVPQDMRIV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:cd07144 386 KEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRE 465
|
410
....*....|....*....
gi 1475409330 399 NGRVTIEYYSQLKTVCVEM 417
Cdd:cd07144 466 LGEYGLETYTQTKAVHINL 484
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
2-415 |
2.46e-157 |
|
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: 452.96 E-value: 2.46e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARL-DIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07141 70 ERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLvDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVC 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07141 150 GQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAK-GIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07141 230 FTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRS 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvPEDPklkdGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07141 310 VERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKR--HGDK----GYFIQPTVFSDVTDDMRIA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:cd07141 384 KEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRE 463
|
410
....*....|....*..
gi 1475409330 399 NGRVTIEYYSQLKTVCV 415
Cdd:cd07141 464 LGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
2-413 |
3.13e-155 |
|
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: 446.80 E-value: 3.13e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASM---AGEHIQLPGGSF-GYTRREPL 77
Cdd:cd07110 42 ERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQLdakAERAVPLPSEDFkARVRREPV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 GVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVA 156
Cdd:cd07110 122 GVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGtGDEAGAPLAAHPGID 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:cd07110 202 KISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyVPEDpkLKDGYYMRPCVLTNCRDDMT 316
Cdd:cd07110 282 RLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGR--RPAH--LEKGYFIAPTVFADVPTDSR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFG 396
Cdd:cd07110 358 IWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIG 437
|
410
....*....|....*..
gi 1475409330 397 RENGRVTIEYYSQLKTV 413
Cdd:cd07110 438 RELGEWGLDNYLEVKQI 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
2-415 |
2.34e-152 |
|
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: 435.89 E-value: 2.34e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLP-GGSFGYTRREPLGVC 80
Cdd:cd06534 17 ERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPdPGGEAYVRREPLGVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd06534 97 GVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGDEVGAALLSHPRVDKIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:cd06534 177 FTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 kqtqrikigdplledtrmgplinrphlervlgfvkvakeqgakvlcggdiyvpedpklkdgyymrpCVLTNCRDDMTCVK 319
Cdd:cd06534 257 ------------------------------------------------------------------TVLVDVDPDMPIAQ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNV-SPVELPFGGYKKSGFGRE 398
Cdd:cd06534 271 EEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKNSGIGRE 350
|
410
....*....|....*..
gi 1475409330 399 NGRVTIEYYSQLKTVCV 415
Cdd:cd06534 351 GGPYGLEEYTRTKTVVI 367
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
2-415 |
2.55e-152 |
|
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: 439.07 E-value: 2.55e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEAR-LDIDISWQCLEYYAGLAASM----AGEHiqLPGGSfGYTRREP 76
Cdd:cd07092 42 ERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPGAVDNFRFFAGAARTLegpaAGEY--LPGHT-SMIRREP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEaGVPPGLFNVVQGGAA-TGQFLCQHPDV 155
Cdd:cd07092 119 IGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGAsAGDALVAHPRV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 AKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFT 235
Cdd:cd07092 198 RMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 236 EEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKeQGAKVLCGGDIyvPEDPklkdGYYMRPCVLTNCRDDM 315
Cdd:cd07092 278 AALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP-AHARVLTGGRR--AEGP----GYFYEPTVVAGVAQDD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 316 TCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGF 395
Cdd:cd07092 351 EIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGY 430
|
410 420
....*....|....*....|
gi 1475409330 396 GRENGRVTIEYYSQLKTVCV 415
Cdd:cd07092 431 GKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
2-413 |
7.59e-152 |
|
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: 438.19 E-value: 7.59e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEAR-LDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07112 49 ERKAVLLRLADLIEAHRDELALLETLDMGKPISDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07112 129 GAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKG-IKPVTLELGGKSPLIIFSDC-DMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEE 237
Cdd:cd07112 209 FTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 238 VVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDPklkdGYYMRPCVLTNCRDDMTC 317
Cdd:cd07112 289 VVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTETG----GFFVEPTVFDGVTPDMRI 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 318 VKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGR 397
Cdd:cd07112 365 AREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGR 444
|
410
....*....|....*.
gi 1475409330 398 ENGRVTIEYYSQLKTV 413
Cdd:cd07112 445 DKSLHALDKYTELKTT 460
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1-413 |
1.89e-149 |
|
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: 431.76 E-value: 1.89e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGE-HIQLPGGSFGYTRREPLGV 79
Cdd:cd07118 43 AERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDsYNNLGDDMLGLVLREPIGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKV 158
Cdd:cd07118 123 VGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07118 203 SFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEdpklkDGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07118 283 VARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASA-----AGLFYQPTIFTDVTPDMAIA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRE 437
|
410
....*....|....*
gi 1475409330 399 NGRVTIEYYSQLKTV 413
Cdd:cd07118 438 LGRYGVEEYTELKTV 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
2-415 |
5.92e-148 |
|
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: 429.07 E-value: 5.92e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARL-DIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07559 61 ERANILNKIADRIEENLELLAVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07559 141 GQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGfGSEAGKPLASHPRIAKLA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSD-----CDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKF 234
Cdd:cd07559 220 FTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 235 TEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDpkLKDGYYMRPCVLTNCRDD 314
Cdd:cd07559 300 IERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGG--LDKGYFYEPTLIKGGNND 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 315 MTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSG 394
Cdd:cd07559 378 MRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSG 457
|
410 420
....*....|....*....|.
gi 1475409330 395 FGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07559 458 IGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
1-415 |
7.84e-148 |
|
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: 427.95 E-value: 7.84e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07107 41 LERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07107 121 ARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGdGATAGAALVRHPDVKRIA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMA-NFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07107 200 LIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvPEDPKLKDGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07107 280 VERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGR--PEGPALEGGFYVEPTVFADVTPGMRIA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:cd07107 358 REEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGRE 437
|
410
....*....|....*..
gi 1475409330 399 NGRVTIEYYSQLKTVCV 415
Cdd:cd07107 438 ECLEELLSYTQEKNVNV 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
2-413 |
1.25e-146 |
|
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: 425.79 E-value: 1.25e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFE-ARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07143 69 KRGRCLSKLADLMERNLDYLASIEALDNGKTFGTaKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVC 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07143 149 GQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGyGRTCGNAISSHMDIDKVA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKG-IKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07143 229 FTGSTLVGRKVMEAAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEdpklkdGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07143 309 KEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNE------GYFIEPTIFTDVTEDMKIV 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:cd07143 383 KEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRE 462
|
410
....*....|....*
gi 1475409330 399 NGRVTIEYYSQLKTV 413
Cdd:cd07143 463 LGEYALENYTQIKAV 477
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
2-413 |
1.24e-144 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 420.47 E-value: 1.24e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDiDI--SWQCLEYYAG----LAASMAGEHIQlpggsfGYT--- 72
Cdd:PRK13473 62 ERAEALLKLADAIEENADEFARLESLNCGKPLHLALND-EIpaIVDVFRFFAGaarcLEGKAAGEYLE------GHTsmi 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 73 RREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQG-GAATGQFLCQ 151
Cdd:PRK13473 135 RRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGrGATVGDALVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 152 HPDVAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEIL 231
Cdd:PRK13473 214 HPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 232 DKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQG-AKVLCGGDIyvPEDPklkdGYYMRPCVLTN 310
Cdd:PRK13473 294 DDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEA--PDGK----GYYYEPTLLAG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 311 CRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGY 390
Cdd:PRK13473 368 ARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQ 447
|
410 420
....*....|....*....|...
gi 1475409330 391 KKSGFGRENGRVTIEYYSQLKTV 413
Cdd:PRK13473 448 KQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
2-413 |
3.31e-144 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 420.29 E-value: 3.31e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEH---IQLPGGSF-GYTRREPL 77
Cdd:PLN02467 73 VRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQkapVSLPMETFkGYVLKEPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 GVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVA 156
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvpEDPKLKDGYYMRPCVLTNCRDDMT 316
Cdd:PLN02467 313 KLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK----RPEHLKKGFFIEPTIITDVTTSMQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFG 396
Cdd:PLN02467 389 IWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFG 468
|
410
....*....|....*..
gi 1475409330 397 RENGRVTIEYYSQLKTV 413
Cdd:PLN02467 469 RELGEWGLENYLSVKQV 485
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
2-413 |
3.48e-144 |
|
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: 419.21 E-value: 3.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARL-DIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07142 66 ERSRILLRFADLLEKHADELAALETWDNGKPYEQARYaEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07142 146 GQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKG-IKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07142 226 FTGSTEVGKIIMQLAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvpedpKLKD-GYYMRPCVLTNCRDDMTC 317
Cdd:cd07142 306 KARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGD-------RIGSkGYYIQPTIFSDVKDDMKI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 318 VKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGR 397
Cdd:cd07142 379 ARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGR 458
|
410
....*....|....*.
gi 1475409330 398 ENGRVTIEYYSQLKTV 413
Cdd:cd07142 459 EKGIYALNNYLQVKAV 474
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
2-413 |
8.34e-144 |
|
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: 417.82 E-value: 8.34e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQ--LPGGSFgYTRREPLGV 79
Cdd:cd07088 58 ERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPsdRPNENI-FIFKVPIGV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKV 158
Cdd:cd07088 137 VAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGrGSVVGDALVAHPKVGMI 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07088 217 SLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvpedPKLKDGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07088 297 VEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKR-----PEGEKGYFYEPTVLTNVRQDMEIV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:cd07088 372 QEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGA 451
|
410
....*....|....*
gi 1475409330 399 NGRVTIEYYSQLKTV 413
Cdd:cd07088 452 DGKHGLEEYLQTKVV 466
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
3-415 |
1.85e-142 |
|
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: 414.82 E-value: 1.85e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 3 RCRILLEAARIIREREDEIA---TMECinnGKSIFEARLDIDISWQCLEYYAGLAASMAGEHI--QLPGgSFGYTRREPL 77
Cdd:cd07131 61 RAEYLFRAAELLKKRKEELArlvTREM---GKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVpsELPN-KDAMTRRQPI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 GVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVA 156
Cdd:cd07131 137 GVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:cd07131 217 VVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvPEDPKLKDGYYMRPCVLTNCRDDMT 316
Cdd:cd07131 297 RFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGER--LTGGGYEKGYFVEPTVFTDVTPDMR 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNV-SPVELPFGGYKKSGF 395
Cdd:cd07131 375 IAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGN 454
|
410 420
....*....|....*....|.
gi 1475409330 396 G-RENGRVTIEYYSQLKTVCV 415
Cdd:cd07131 455 GhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
1-415 |
6.40e-142 |
|
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: 411.92 E-value: 6.40e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIAtmECINN------GKSIFEARLDIDISWQCleyyAGLAASMAGEHIQ-LPGGSFGYTR 73
Cdd:cd07104 22 QERAAILRKAAEILEERRDEIA--DWLIResgstrPKAAFEVGAAIAILREA----AGLPRRPEGEILPsDVPGKESMVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 74 REPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVS-ALLLAEIYSEAGVPPGLFNVVQGGAA-TGQFLCQ 151
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSeIGDALVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 152 HPDVAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEIL 231
Cdd:cd07104 176 HPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 232 DKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvpedpklkDGYYMRPCVLTNC 311
Cdd:cd07104 256 DEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY---------EGLFYQPTVLSDV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 312 RDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVS--PVeLPFGG 389
Cdd:cd07104 327 TPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNdePH-VPFGG 405
|
410 420
....*....|....*....|....*.
gi 1475409330 390 YKKSGFGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07104 406 VKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
2-413 |
2.06e-141 |
|
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: 411.90 E-value: 2.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIA---TME--CINNGKSIFEARLDIDIswqcLEYYAGLAASMAGEHiqLPGGSFgyTRREP 76
Cdd:cd07138 59 ERAALLERIAEAYEARADELAqaiTLEmgAPITLARAAQVGLGIGH----LRAAADALKDFEFEE--RRGNSL--VVREP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPF-QIASwKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPD 154
Cdd:cd07138 131 IGVCGLITPWNWPLnQIVL-KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 155 VAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKF 234
Cdd:cd07138 210 VDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 235 TEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvPEDPK-LKDGYYMRPCVLTNCRD 313
Cdd:cd07138 290 EEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG----PGRPEgLERGYFVKPTVFADVTP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 314 DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPvELPFGGYKKS 393
Cdd:cd07138 366 DMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQS 444
|
410 420
....*....|....*....|
gi 1475409330 394 GFGRENGRVTIEYYSQLKTV 413
Cdd:cd07138 445 GNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
2-413 |
9.42e-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: 409.23 E-value: 9.42e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIA---TMEcinNGKSIFEARLDIDISWQCLEYYAGLaaSMAGEHIQLPGGSFGYTRREPLG 78
Cdd:cd07106 42 ERRAALLAIADAIEANAEELArllTLE---QGKPLAEAQFEVGGAVAWLRYTASL--DLPDEVIEDDDTRRVELRRKPLG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 79 VCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQGGAATGQFLCQHPDVAKV 158
Cdd:cd07106 117 VVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07106 196 SFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEAL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyVPEDPklkdGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07106 276 VALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGE--PLDGP----GYFIPPTIVDDPPEGSRIV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNY-NVSPvELPFGGYKKSGFGR 397
Cdd:cd07106 350 DEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHgALDP-DAPFGGHKQSGIGV 428
|
410
....*....|....*.
gi 1475409330 398 ENGRVTIEYYSQLKTV 413
Cdd:cd07106 429 EFGIEGLKEYTQTQVI 444
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
2-413 |
3.43e-140 |
|
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: 408.89 E-value: 3.43e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSI-FEARLDIDISWQCLEYYAGLAASMA-GEHIQLPGGSFGYTRREPLGV 79
Cdd:cd07139 61 ERAAVLRRLADALEARADELARLWTAENGMPIsWSRRAQGPGPAALLRYYAALARDFPfEERRPGSGGGHVLVRREPVGV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVS 159
Cdd:cd07139 141 VAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:cd07139 221 FTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvPEDPKLKDGYYMRPCVLTNCRDDMTCVK 319
Cdd:cd07139 301 AAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGG----GRPAGLDRGWFVEPTLFADVDNDMRIAQ 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVeLPFGGYKKSGFGREN 399
Cdd:cd07139 377 EEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG-APFGGFKQSGIGREG 455
|
410
....*....|....
gi 1475409330 400 GRVTIEYYSQLKTV 413
Cdd:cd07139 456 GPEGLDAYLETKSI 469
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
2-415 |
4.72e-140 |
|
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: 407.75 E-value: 4.72e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQL---PGGS--FGYTRREP 76
Cdd:cd07149 44 ERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKRLAGETIPFdasPGGEgrIGFTIREP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAAT-GQFLCQHPDV 155
Cdd:cd07149 124 IGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETvGDALVTDPRV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 AKVSFTGSVPTGMKIMEMSakGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFT 235
Cdd:cd07149 204 RMISFTGSPAVGEAIARKA--GLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 236 EEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpedpkLKDGYYMRPCVLTNCRDDM 315
Cdd:cd07149 282 ERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGG---------KRDGAILEPTVLTDVPPDM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 316 TCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFIN---NYNVSpvELPFGGYKK 392
Cdd:cd07149 353 KVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdssTFRVD--HMPYGGVKE 430
|
410 420
....*....|....*....|...
gi 1475409330 393 SGFGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07149 431 SGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
1-413 |
5.69e-139 |
|
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: 405.86 E-value: 5.69e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQ-LPGGSFGYTRREPLGV 79
Cdd:cd07097 59 EARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 cVG-IGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAK 157
Cdd:cd07097 139 -VGlITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 158 VSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEE 237
Cdd:cd07097 218 VSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 238 VVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDPklkdGYYMRPCVLTNCRDDMTC 317
Cdd:cd07097 298 LVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDE----GYYLAPALFAGVTNDMRI 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 318 VKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFIN------NYNVspvelPFGGYK 391
Cdd:cd07097 374 AREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptagvDYHV-----PFGGRK 448
|
410 420
....*....|....*....|...
gi 1475409330 392 KSGFG-RENGRVTIEYYSQLKTV 413
Cdd:cd07097 449 GSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
2-417 |
9.00e-138 |
|
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: 402.99 E-value: 9.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARL-DIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07117 61 ERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07117 141 GQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGkGSKSGEYLLNHPGLDKLA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVV 239
Cdd:cd07117 220 FTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 240 KQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDpkLKDGYYMRPCVLTNCRDDMTCVK 319
Cdd:cd07117 300 EKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENG--LDKGFFIEPTLIVNVTNDMRVAQ 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 320 EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGREN 399
Cdd:cd07117 378 EEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRET 457
|
410
....*....|....*...
gi 1475409330 400 GRVTIEYYSQLKTVCVEM 417
Cdd:cd07117 458 HKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
2-415 |
1.02e-137 |
|
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: 402.98 E-value: 1.02e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEAR-LDIDISWQCLEYYAGLAASMAGEHIQL----PGGS--FGYTRR 74
Cdd:cd07113 61 ERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRaFEVGQSANFLRYFAGWATKINGETLAPsipsMQGEryTAFTRR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPD 154
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 155 VAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKF 234
Cdd:cd07113 221 VAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDEL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 235 TEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVpedpklKDGYYMRPCVLTNCRDD 314
Cdd:cd07113 301 VTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA------GEGYFVQPTLVLARSAD 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 315 MTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSG 394
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSG 454
|
410 420
....*....|....*....|.
gi 1475409330 395 FGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07113 455 IGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
2-415 |
2.22e-136 |
|
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: 398.66 E-value: 2.22e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSI-FEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07108 42 ERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07108 122 GAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGyGEECGAALVDHPDVDKVT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMA-NFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07108 201 FTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKE-QGAKVLCGGDIyvPEDPKLKDGYYMRPCVLTNCRDDMTC 317
Cdd:cd07108 281 VAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLStSGATVLRGGPL--PGEGPLADGFFVQPTIFSGVDNEWRL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 318 VKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGR 397
Cdd:cd07108 359 AREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGR 438
|
410
....*....|....*....
gi 1475409330 398 ENG-RVTIEYYSQLKTVCV 415
Cdd:cd07108 439 EASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
2-416 |
3.05e-135 |
|
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: 396.87 E-value: 3.05e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEA-RLDIDISWQCLEYYAGLAASMAGEHIQL----PGGSFGYTRREP 76
Cdd:cd07140 68 DRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPInqarPNRNLTLTKREP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDV 155
Cdd:cd07140 148 IGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGsGSLVGQRLSDHPDV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 AKVSFTGSVPTGMKIMEMSAKG-IKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKF 234
Cdd:cd07140 228 RKLGFTGSTPIGKHIMKSCAVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEF 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 235 TEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiYVPedpklKDGYYMRPCVLTNCRDD 314
Cdd:cd07140 308 VRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGK-QVD-----RPGFFFEPTVFTDVEDH 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 315 MTCVKEEIFGPVMSILSF---DTEAeVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYK 391
Cdd:cd07140 382 MFIAKEESFGPIMIISKFddgDVDG-VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFK 460
|
410 420
....*....|....*....|....*
gi 1475409330 392 KSGFGRENGRVTIEYYSQLKTVCVE 416
Cdd:cd07140 461 QSGFGKDLGEEALNEYLKTKTVTIE 485
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
2-413 |
4.09e-134 |
|
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: 392.76 E-value: 4.09e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEAR-LDIDISWQCLEYYAGLAASMAGEHI-----QLPGGSFGYTRRE 75
Cdd:cd07089 43 ERARCLRQLHEALEARKEELRALLVAEVGAPVMTARaMQVDGPIGHLRYFADLADSFPWEFDlpvpaLRGGPGRRVVRRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 PLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGG-AATGQFLCQHPD 154
Cdd:cd07089 123 PVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSdNAVGEALTTDPR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 155 VAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKF 234
Cdd:cd07089 203 VDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 235 TEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvPEDpkLKDGYYMRPCVLTNCRDD 314
Cdd:cd07089 283 VEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAG--LDKGFYVEPTLFADVDND 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 315 MTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSG 394
Cdd:cd07089 359 MRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSG 438
|
410
....*....|....*....
gi 1475409330 395 FGRENGRVTIEYYSQLKTV 413
Cdd:cd07089 439 LGRENGIEGLEEFLETKSI 457
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
2-413 |
2.17e-133 |
|
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: 390.94 E-value: 2.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFG-----YTRREP 76
Cdd:cd07145 44 KRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNerriaFTVREP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDV 155
Cdd:cd07145 124 IGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGyGSEVGDEIVTNPKV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 AKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFT 235
Cdd:cd07145 204 NMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 236 EEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpedpKLKDGYYMRPCVLTNCRDDM 315
Cdd:cd07145 284 KLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGG--------KRDEGSFFPPTVLENDTPDM 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 316 TCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYN-VSPVELPFGGYKKSG 394
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTrFRWDNLPFGGFKKSG 435
|
410
....*....|....*....
gi 1475409330 395 FGRENGRVTIEYYSQLKTV 413
Cdd:cd07145 436 IGREGVRYTMLEMTEEKTI 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
2-413 |
8.46e-132 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 388.41 E-value: 8.46e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARL-DIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:PLN02766 83 ERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:PLN02766 163 GHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKG-IKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:PLN02766 243 FTGSTEVGRKIMQAAATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvpedPKLKDGYYMRPCVLTNCRDDMTCV 318
Cdd:PLN02766 323 VEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK------PCGDKGYYIEPTIFTDVTEDMKIA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:PLN02766 397 QDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRD 476
|
410
....*....|....*
gi 1475409330 399 NGRVTIEYYSQLKTV 413
Cdd:PLN02766 477 QGMDALDKYLQVKSV 491
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
2-415 |
1.19e-130 |
|
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: 382.96 E-value: 1.19e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASM-AGEHIQLPGGSfGYTRREPLGVC 80
Cdd:cd07100 22 ERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFlADEPIETDAGK-AYVRYEPLGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPF-QIASWkSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLF-NVVQGGAATGQFLcQHPDVAKV 158
Cdd:cd07100 101 LGIMPWNFPFwQVFRF-AAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFqNLLIDSDQVEAII-ADPRVRGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07100 179 TLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvPEDPklkdGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07100 259 VEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKR--PDGP----GAFYPPTVLTDVTPGMPAY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:cd07100 333 DEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRSGYGRE 412
|
410
....*....|....*..
gi 1475409330 399 NGRVTIEYYSQLKTVCV 415
Cdd:cd07100 413 LGRFGIREFVNIKTVWV 429
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
2-413 |
2.69e-129 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 383.39 E-value: 2.69e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSiFE--ARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGV 79
Cdd:PLN02466 120 ERSRILLRFADLLEKHNDELAALETWDNGKP-YEqsAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKV 158
Cdd:PLN02466 199 AGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKG-IKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEE 237
Cdd:PLN02466 279 AFTGSTDTGKIVLELAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 238 VVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEdpklkdGYYMRPCVLTNCRDDMTC 317
Cdd:PLN02466 359 AKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSK------GYYIQPTVFSNVQDDMLI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 318 VKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGR 397
Cdd:PLN02466 433 AQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGR 512
|
410
....*....|....*.
gi 1475409330 398 ENGRVTIEYYSQLKTV 413
Cdd:PLN02466 513 EKGIYSLNNYLQVKAV 528
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
2-415 |
1.83e-128 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 379.80 E-value: 1.83e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPggsFGYTR----REPL 77
Cdd:PLN02278 85 ERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSP---FPDRRllvlKQPV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 GVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGA-ATGQFLCQHPDVA 156
Cdd:PLN02278 162 GVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDApEIGDALLASPKVR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:PLN02278 242 KITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpEDPKLKDGYYmRPCVLTNCRDDMT 316
Cdd:PLN02278 322 AFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGG-----KRHSLGGTFY-EPTVLGDVTEDML 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFG 396
Cdd:PLN02278 396 IFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLG 475
|
410
....*....|....*....
gi 1475409330 397 RENGRVTIEYYSQLKTVCV 415
Cdd:PLN02278 476 REGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
1-415 |
3.31e-128 |
|
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: 377.44 E-value: 3.31e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNG----KSIFEARLDIDIswqcLEYYAGLAASMAGEHIQ-LPGGSFGYTRRE 75
Cdd:cd07150 43 SERERILLKAAEIMERRADDLIDLLIDEGGstygKAWFETTFTPEL----LRAAAGECRRVRGETLPsDSPGTVSMSVRR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 PLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPD 154
Cdd:cd07150 119 PLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGgGAEVGDELVDDPR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 155 VAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKF 234
Cdd:cd07150 199 VRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 235 TEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvpedpklKDGYYMRPCVLTNCRDD 314
Cdd:cd07150 279 VKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGGK---------YDGNFYQPTVLTDVTPD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 315 MTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNV-SPVELPFGGYKKS 393
Cdd:cd07150 350 MRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTIlDEAHVPFGGVKAS 429
|
410 420
....*....|....*....|..
gi 1475409330 394 GFGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07150 430 GFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
2-401 |
8.08e-128 |
|
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: 377.51 E-value: 8.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEAR-LDIDISWQCLEYYAGLAASMAGEhiqLPGgsfgytrREPLGVC 80
Cdd:cd07111 82 VRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLDTE---LAG-------WKPVGVV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSF 160
Cdd:cd07111 152 GQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 161 TGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVK 240
Cdd:cd07111 232 TGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 241 QTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAkvlcggDIYVPEDPKLKDGYYMRPCVLTNCRDDMTCVKE 320
Cdd:cd07111 312 RMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGA------DVFQPGADLPSKGPFYPPTLFTNVPPASRIAQE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 321 EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENG 400
Cdd:cd07111 386 EIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGG 465
|
.
gi 1475409330 401 R 401
Cdd:cd07111 466 K 466
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-415 |
4.93e-125 |
|
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: 370.36 E-value: 4.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 3 RCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHI--QLPGgSFGYTRREPLGVC 80
Cdd:cd07086 59 RGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIpsERPG-HRLMEQWNPLGVV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA----GVPPGLFNVVQGGAATGQFLCQHPDVA 156
Cdd:cd07086 138 GVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:cd07086 218 LVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDPklkdGYYMRPCVLTNCRDDMT 316
Cdd:cd07086 298 RLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEP----GNYVEPTIVTGVTDDAR 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVV--AELQAGtcfINNYNVSP----VELPFGGY 390
Cdd:cd07086 374 IVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCG---IVNVNIPTsgaeIGGAFGGE 450
|
410 420
....*....|....*....|....*
gi 1475409330 391 KKSGFGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07086 451 KETGGGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
2-400 |
3.30e-124 |
|
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: 367.32 E-value: 3.30e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHiQLPGGSF-----GYTRREP 76
Cdd:cd07099 41 GRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVLAPR-KVPTGLLmpnkkATVEYRP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPdVA 156
Cdd:cd07099 120 YGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:cd07099 199 KVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpeDPKLKDGYYMRPCVLTNCRDDMT 316
Cdd:cd07099 279 RLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGG------ARSNGGGPFYEPTVLTDVPHDMD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN--YNVSPVELPFGGYKKSG 394
Cdd:cd07099 353 VMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSG 432
|
....*.
gi 1475409330 395 FGRENG 400
Cdd:cd07099 433 GGRRHG 438
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
3-415 |
1.46e-119 |
|
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: 355.50 E-value: 1.46e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 3 RCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCVG 82
Cdd:cd07120 44 RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 83 IGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA-GVPPGLFNVV-QGGAATGQFLCQHPDVAKVSF 160
Cdd:cd07120 124 IVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFtESGSEGAAHLVASPDVDVISF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 161 TGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVK 240
Cdd:cd07120 204 TGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 241 QTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvPEDPKLKDGYYMRPCVLTNCRDDMTCVKE 320
Cdd:cd07120 284 RLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGG---PVTEGLAKGAFLRPTLLEVDDPDADIVQE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 321 EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENG 400
Cdd:cd07120 361 EIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHG 440
|
410
....*....|....*
gi 1475409330 401 RVTIEYYSQLKTVCV 415
Cdd:cd07120 441 VAALEDFIEYKHIYL 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
2-416 |
4.31e-119 |
|
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: 354.69 E-value: 4.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQ--LPGGSfGYTRREPLGV 79
Cdd:cd07151 55 ERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPsdVPGKE-NRVYREPLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 cVG-IGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSA-LLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPdVA 156
Cdd:cd07151 134 -VGvISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHP-VP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KV-SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFT 235
Cdd:cd07151 212 RLiSFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 236 EEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvpedpklkDGYYMRPCVLTNCRDDM 315
Cdd:cd07151 292 EKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEA---------EGNVLEPTVLSDVTNDM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 316 TCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNV--SPvELPFGGYKKS 393
Cdd:cd07151 363 EIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVndEP-HVPFGGEKNS 441
|
410 420
....*....|....*....|...
gi 1475409330 394 GFGRENGRVTIEYYSQLKTVCVE 416
Cdd:cd07151 442 GLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
2-415 |
8.84e-118 |
|
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: 352.14 E-value: 8.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEA-RLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:cd07116 61 ERANILNKIADRMEANLEMLAVAETWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:cd07116 141 GQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDM------NNAVKGALMANFlTQGQVCCNGTRVFVQKEILDK 233
Cdd:cd07116 220 FTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADVMDaddaffDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 234 FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDpKLKDGYYMRPCVLTNcrD 313
Cdd:cd07116 299 FMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGG-LLGGGYYVPTTFKGG--N 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 314 DMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKS 393
Cdd:cd07116 376 KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQS 455
|
410 420
....*....|....*....|..
gi 1475409330 394 GFGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07116 456 GIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
2-413 |
2.16e-117 |
|
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: 349.18 E-value: 2.16e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHI-QLPGGSFGYTRREPLGVC 80
Cdd:cd07105 23 ERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIpSDKPGTLAMVVKEPVGVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQ-----GGAATGQFLcQHPDV 155
Cdd:cd07105 103 LGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVThspedAPEVVEALI-AHPAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 AKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFT 235
Cdd:cd07105 182 RKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 236 EEVVKQTQRIKIGDPLLedtrmGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpEDPKLKDGYYMRPCVLTNCRDDM 315
Cdd:cd07105 262 EKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGG-----LADESPSGTSMPPTILDNVTPDM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 316 TCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNV--SPVeLPFGGYKKS 393
Cdd:cd07105 332 DIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVhdEPT-LPHGGVKSS 410
|
410 420
....*....|....*....|
gi 1475409330 394 GFGRENGRVTIEYYSQLKTV 413
Cdd:cd07105 411 GYGRFNGKWGIDEFTETKWI 430
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
7-413 |
8.34e-114 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 339.40 E-value: 8.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 7 LLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQ--LPGGSFgYTRREPLGVCVGIG 84
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQsdRPGENI-LLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 85 AWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVSFTGS 163
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGrGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 164 VPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVKQTQ 243
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 244 RIKIGDPLLEDT-RMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvpedpKLKDGYYMRPCVLTNCRDDMTCVKEEI 322
Cdd:PRK10090 240 AVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKA------VEGKGYYYPPTLLLDVRQEMSIMHEET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 323 FGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRV 402
Cdd:PRK10090 314 FGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKH 393
|
410
....*....|.
gi 1475409330 403 TIEYYSQLKTV 413
Cdd:PRK10090 394 GLHEYLQTQVV 404
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
2-409 |
4.29e-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: 338.88 E-value: 4.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNG----KSIFEARLDIDISWQCleyyAGLAASMAGEHIQLPGGSFGYTRREPL 77
Cdd:cd07152 36 ERAAVLRRAADLLEEHADEIADWIVRESGsirpKAGFEVGAAIGELHEA----AGLPTQPQGEILPSAPGRLSLARRVPL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 GVcVG-IGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSA-LLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDV 155
Cdd:cd07152 112 GV-VGvISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 AKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFT 235
Cdd:cd07152 191 AMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 236 EEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvpedpklkDGYYMRPCVLTNCRDDM 315
Cdd:cd07152 271 AKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY---------DGLFYRPTVLSGVKPGM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 316 TCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVS-PVELPFGGYKKSG 394
Cdd:cd07152 342 PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNdEPHNPFGGMGASG 421
|
410
....*....|....*.
gi 1475409330 395 FG-RENGRVTIEYYSQ 409
Cdd:cd07152 422 NGsRFGGPANWEEFTQ 437
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
2-415 |
4.52e-113 |
|
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: 339.02 E-value: 4.52e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLP-----GGSFGYTRREP 76
Cdd:cd07094 44 ERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDV 155
Cdd:cd07094 124 VGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGeREVLGDAFAADERV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 AKVSFTGSVPTGMKIMEMSakGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFT 235
Cdd:cd07094 204 AMLSFTGSAAVGEALRANA--GGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 236 EEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvpedpklKDGYYMRPCVLTNCRDDM 315
Cdd:cd07094 282 EAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGE---------RDGALFKPTVLEDVPRDT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 316 TCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVE-LPFGGYKKSG 394
Cdd:cd07094 353 KLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESG 432
|
410 420
....*....|....*....|.
gi 1475409330 395 FGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07094 433 VGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
2-411 |
1.68e-112 |
|
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: 337.68 E-value: 1.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQL---PGGS--FGYTRREP 76
Cdd:cd07147 44 RRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIYGEVLPLdisARGEgrQGLVRRFP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVA 156
Cdd:cd07147 124 IGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKgiKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:cd07147 204 LLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvpedpklkDGYYMRPCVLTNCRDDMT 316
Cdd:cd07147 282 RLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR---------DGALLEPTILEDVPPDME 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN---YNVSPveLPFGGYKKS 393
Cdd:cd07147 353 VNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDvptFRVDH--MPYGGVKDS 430
|
410
....*....|....*...
gi 1475409330 394 GFGRENGRVTIEYYSQLK 411
Cdd:cd07147 431 GIGREGVRYAIEEMTEPR 448
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
2-413 |
2.56e-109 |
|
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: 329.32 E-value: 2.56e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLP-----GGSFGYTRREP 76
Cdd:cd07146 41 QRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAA-TGQFLCQHPDV 155
Cdd:cd07146 121 LGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGeIGDELITHPDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 AKVSFTGSVPTGMKIMEMSakGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFT 235
Cdd:cd07146 201 DLVTFTGGVAVGKAIAATA--GYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 236 EEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvpedpklKDGYYMRPCVLTNCRDDM 315
Cdd:cd07146 279 DLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQ---------RQGALYAPTVLDHVPPDA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 316 TCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVEL-PFGGYKKSG 394
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSELsPFGGVKDSG 429
|
410 420
....*....|....*....|
gi 1475409330 395 FG-RENGRVTIEYYSQLKTV 413
Cdd:cd07146 430 LGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
2-413 |
7.12e-109 |
|
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: 329.09 E-value: 7.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHiqLPGGSFG---YTRREPLG 78
Cdd:cd07085 61 KRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEY--LENVARGidtYSYRQPLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 79 VCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKV 158
Cdd:cd07085 139 VVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07085 219 SFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPedPKLKDGYYMRPCVLTNCRDDMTCV 318
Cdd:cd07085 299 VERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKV--PGYENGNFVGPTILDNVTPDMKIY 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFInnyNVS-PVELP---FGGYKKSG 394
Cdd:cd07085 377 KEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGI---NVPiPVPLAffsFGGWKGSF 453
|
410 420
....*....|....*....|.
gi 1475409330 395 FGREN--GRVTIEYYSQLKTV 413
Cdd:cd07085 454 FGDLHfyGKDGVRFYTQTKTV 474
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
2-413 |
2.09e-107 |
|
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: 324.58 E-value: 2.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSF-GYTRREPLGVC 80
Cdd:cd07102 41 ERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGFeRYIRREPLGVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSF 160
Cdd:cd07102 121 LIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 161 TGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMN----NAVKGAlmanFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:cd07102 201 TGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDaaaeSLVDGA----FFNSGQSCCSIERIYVHESIYDAFVE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDPKlkdGYYMRPCVLTNCRDDMT 316
Cdd:cd07102 277 AFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPEDKAG---GAYLAPTVLTNVDHSMR 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFIN--NYnVSPvELPFGGYKKSG 394
Cdd:cd07102 354 VMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcDY-LDP-ALAWTGVKDSG 431
|
410
....*....|....*....
gi 1475409330 395 FGRENGRVTIEYYSQLKTV 413
Cdd:cd07102 432 RGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-414 |
2.70e-107 |
|
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: 326.10 E-value: 2.70e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCV 81
Cdd:cd07124 92 ERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 82 GIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVSF 160
Cdd:cd07124 172 VISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGpGEEVGDYLVEHPDVRFIAF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 161 TGSVPTGMKIMEMSAKG------IKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKF 234
Cdd:cd07124 252 TGSREVGLRIYERAAKVqpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEF 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 235 TEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGaKVLCGGDIyvpeDPKLKDGYYMRPCVLTNCRDD 314
Cdd:cd07124 332 LERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEV----LELAAEGYFVQPTIFADVPPD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 315 MTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSP-VEL-PFGGYKK 392
Cdd:cd07124 407 HRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGAlVGRqPFGGFKM 486
|
410 420
....*....|....*....|...
gi 1475409330 393 SGFG-RENGRVTIEYYSQLKTVC 414
Cdd:cd07124 487 SGTGsKAGGPDYLLQFMQPKTVT 509
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
2-413 |
8.94e-105 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 319.15 E-value: 8.94e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEA-RLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC 80
Cdd:PRK09847 82 KRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKVS 159
Cdd:PRK09847 162 AAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKG-IKPVTLELGGKSPLIIFSDC-DMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEE 237
Cdd:PRK09847 242 FTGSTRTGKQLLKDAGDSnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLAL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 238 VVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEdpklkdgyYMRPCVLTNCRDDMTC 317
Cdd:PRK09847 322 LKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAA--------AIGPTIFVDVDPNASL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 318 VKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGR 397
Cdd:PRK09847 394 SREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGR 473
|
410
....*....|....*.
gi 1475409330 398 ENGRVTIEYYSQLKTV 413
Cdd:PRK09847 474 DKSLHALEKFTELKTI 489
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
2-415 |
1.81e-101 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 310.30 E-value: 1.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIqlPGGSFG---YTRREPLG 78
Cdd:PRK11241 71 ERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTI--PGHQADkrlIVIKQPIG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 79 VCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGA-ATGQFLCQHPDVAK 157
Cdd:PRK11241 149 VTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 158 VSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEE 237
Cdd:PRK11241 229 LSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 238 VVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpeDPKLKDGYYMRPCVLTNCRDDMTC 317
Cdd:PRK11241 309 LQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGG------KAHELGGNFFQPTILVDVPANAKV 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 318 VKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGR 397
Cdd:PRK11241 383 AKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGR 462
|
410
....*....|....*...
gi 1475409330 398 ENGRVTIEYYSQLKTVCV 415
Cdd:PRK11241 463 EGSKYGIEDYLEIKYMCI 480
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
2-415 |
6.68e-98 |
|
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: 299.99 E-value: 6.68e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGK---SIFEARLDIDISwqcLEYYAGLAASMAGEHiQLPGGSFGYTR----R 74
Cdd:cd07101 41 ERAAVFLRFHDLVLERRDELLDLIQLETGKarrHAFEEVLDVAIV---ARYYARRAERLLKPR-RRRGAIPVLTRttvnR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 EPLGVcVG-IGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQH 152
Cdd:cd07101 117 RPKGV-VGvISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGpGSEVGGAIVDN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 153 PDVakVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILD 232
Cdd:cd07101 196 ADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 233 KFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvpEDPKLkdG-YYMRPCVLTNC 311
Cdd:cd07101 274 EFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGR----ARPDL--GpYFYEPTVLTGV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 312 RDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN-YNVS--PVELPFG 388
Cdd:cd07101 348 TEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEgYAAAwaSIDAPMG 427
|
410 420
....*....|....*....|....*..
gi 1475409330 389 GYKKSGFGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07101 428 GMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
2-413 |
3.04e-97 |
|
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: 299.10 E-value: 3.04e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEhiQLPGGSF-------GYTRR 74
Cdd:cd07082 62 ERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGD--SLPGDWFpgtkgkiAQVRR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHP 153
Cdd:cd07082 140 EPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 154 DVAKVSFTGSVPTGMKIMEMSakGIKPVTLELGGKSPLIIFSDCDMNNAVK----GALMANfltqGQVCCNGTRVFVQKE 229
Cdd:cd07082 220 RIDVISFTGSTEVGNRLKKQH--PMKRLVLELGGKDPAIVLPDADLELAAKeivkGALSYS----GQRCTAIKRVLVHES 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 230 ILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGdiyvpedpKLKDGYYMRPCVLT 309
Cdd:cd07082 294 VADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG--------GREGGNLIYPTLLD 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 310 NCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNY-NVSPVELPFG 388
Cdd:cd07082 366 PVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcQRGPDHFPFL 445
|
410 420
....*....|....*....|....*
gi 1475409330 389 GYKKSGFGRENGRVTIEYYSQLKTV 413
Cdd:cd07082 446 GRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-415 |
1.45e-95 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 296.40 E-value: 1.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKS---IFEARLDIDIswqCLEYYAGLAASMAGEHIQ---LPGGSFGYTRRE 75
Cdd:PRK09407 77 ERAAVLLRFHDLVLENREELLDLVQLETGKArrhAFEEVLDVAL---TARYYARRAPKLLAPRRRagaLPVLTKTTELRQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 PLGVcVG-IGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHP 153
Cdd:PRK09407 154 PKGV-VGvISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGpGPVVGTALVDNA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 154 DVakVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK 233
Cdd:PRK09407 233 DY--LMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 234 FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGG----DIyvpedpklkdG-YYMRPCVL 308
Cdd:PRK09407 311 FVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGkarpDL----------GpLFYEPTVL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 309 TNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN-YNVS--PVEL 385
Cdd:PRK09407 381 TGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgYAAAwgSVDA 460
|
410 420 430
....*....|....*....|....*....|
gi 1475409330 386 PFGGYKKSGFGRENGRVTIEYYSQLKTVCV 415
Cdd:PRK09407 461 PMGGMKDSGLGRRHGAEGLLKYTESQTIAT 490
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
2-401 |
1.22e-90 |
|
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: 281.88 E-value: 1.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARL-DI-----DISWQCLEYYAGLAASmagehiQLPGGSFGYTRR- 74
Cdd:cd07098 41 ERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLgEIlvtceKIRWTLKHGEKALRPE------SRPGGLLMFYKRa 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 ----EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA----GVPPGLFNVVQGGAATG 146
Cdd:cd07098 115 rveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 147 QFLCQHPDVAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFV 226
Cdd:cd07098 195 EALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 227 QKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYV-PEDPKlkdGYYMRP 305
Cdd:cd07098 275 HEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPhPEYPQ---GHYFPP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 306 CVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVS--PV 383
Cdd:cd07098 352 TLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQ 431
|
410
....*....|....*...
gi 1475409330 384 ELPFGGYKKSGFGRENGR 401
Cdd:cd07098 432 QLPFGGVKGSGFGRFAGE 449
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-394 |
9.93e-88 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 275.66 E-value: 9.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLD----IDIswqcLEYYA----GLAA-----SMAGEHIQLpggs 68
Cdd:PRK03137 96 DRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADtaeaIDF----LEYYArqmlKLADgkpveSRPGEHNRY---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 69 fgytRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQ 147
Cdd:PRK03137 168 ----FYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGsGSEVGD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 148 FLCQHPDVAKVSFTGSVPTGMKIMEMSAK---G---IKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNG 221
Cdd:PRK03137 244 YLVDHPKTRFITFTGSREVGLRIYERAAKvqpGqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSAC 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 222 TRVFVQKEILDKFTEEVVKQTQRIKIGDPlLEDTRMGPLINRPHLERVLGFVKVAKEQGaKVLCGGDiyvpEDPklKDGY 301
Cdd:PRK03137 324 SRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGE----GDD--SKGY 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 302 YMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFIN----- 376
Cdd:PRK03137 396 FIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgctg 475
|
410 420
....*....|....*....|.
gi 1475409330 377 ---NYNvspvelPFGGYKKSG 394
Cdd:PRK03137 476 aivGYH------PFGGFNMSG 490
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
2-413 |
2.86e-85 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 269.43 E-value: 2.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMA--GEHIQLPGGSFGYTRrEPLGV 79
Cdd:TIGR01237 92 ERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAkgKPVNSREGETNQYVY-TPTGV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKV 158
Cdd:TIGR01237 171 TVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGsGSEVGDYLVDHPKTSLI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAK------GIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILD 232
Cdd:TIGR01237 251 TFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 233 KFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGaKVLCGGDiyvpEDPklKDGYYMRPCVLTNCR 312
Cdd:TIGR01237 331 EVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGC----GDD--SKGYFIGPTIFADVD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 313 DDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV--ELPFGGY 390
Cdd:TIGR01237 404 RKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIvgYQPFGGF 483
|
410 420
....*....|....*....|....
gi 1475409330 391 KKSGFG-RENGRVTIEYYSQLKTV 413
Cdd:TIGR01237 484 KMSGTDsKAGGPDYLALFMQAKTV 507
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-413 |
2.05e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 265.45 E-value: 2.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASM-AGEHIQLP--GGSFGYTRREPLG 78
Cdd:PRK09406 46 QRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALlADEPADAAavGASRAYVRYQPLG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 79 VCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKV 158
Cdd:PRK09406 126 VVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:PRK09406 206 TLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyVPEDPklkdGYYMRPCVLTNCRDDMTCV 318
Cdd:PRK09406 286 VARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGK--RPDGP----GWFYPPTVITDITPDMRLY 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRE 398
Cdd:PRK09406 360 TEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRE 439
|
410
....*....|....*
gi 1475409330 399 NGRVTIEYYSQLKTV 413
Cdd:PRK09406 440 LSAHGIREFCNIKTV 454
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
3-415 |
1.53e-81 |
|
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: 257.07 E-value: 1.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 3 RCRILLEAARIIREREDEIATMECINNGKSIFEARL--------DIDISWQCLEYYaglaasMAGEHIQLPGGSF---GY 71
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLteiavvlgEIDHALKHLKKW------MKPRRVSVPLLLQpakAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 72 TRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQGGAATGQFLCQ 151
Cdd:cd07087 96 VIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 152 HP-DvaKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI 230
Cdd:cd07087 175 EPfD--HIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 231 LDKFTEEVVKQTQRiKIGDPLLEDTRMGPLINRPHLERVLGFVkvakeQGAKVLCGGDIyvpeDPKLKdgyYMRPCVLTN 310
Cdd:cd07087 253 KDELIEELKKAIKE-FYGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQV----DKEER---YIAPTILDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 311 CRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFIN--NYNVSPVELPFG 388
Cdd:cd07087 320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvLLHAAIPNLPFG 399
|
410 420
....*....|....*....|....*..
gi 1475409330 389 GYKKSGFGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07087 400 GVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
2-406 |
5.32e-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: 253.35 E-value: 5.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLD-------IDISWQCLEYYAGLAASMAGEHIqlpggsfGYTRR 74
Cdd:cd07095 23 ERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEvaamagkIDISIKAYHERTGERATPMAQGR-------AVLRH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPD 154
Cdd:cd07095 96 RPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRETGEALAAHEG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 155 VAKVSFTGSVPTGMKIMEMSA-KGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFV-QKEILD 232
Cdd:cd07095 176 IDGLLFTGSAATGLLLHRQFAgRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVpDGAVGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 233 KFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVpedpklKDGYYMRPCVL--TN 310
Cdd:cd07095 256 AFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV------AGTAFLSPGIIdvTD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 311 CRDdmtCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGtcfINNYNV----SPVELP 386
Cdd:cd07095 330 AAD---VPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG---IVNWNRpttgASSTAP 403
|
410 420
....*....|....*....|
gi 1475409330 387 FGGYKKSGFGRENGRVTIEY 406
Cdd:cd07095 404 FGGVGLSGNHRPSAYYAADY 423
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
15-400 |
1.31e-78 |
|
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: 250.97 E-value: 1.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 15 REREDEIATMECINNGKSIFEARLD----IDIswqClEYYAGLAASMAGEHI--QLPGGSFgYTRREPLGVCVGIGAWNY 88
Cdd:cd07130 70 RKKKEALGKLVSLEMGKILPEGLGEvqemIDI---C-DFAVGLSRQLYGLTIpsERPGHRM-MEQWNPLGVVGVITAFNF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 89 PFQIASWKSAPALACGNAMVFKPSPFTPVSAL----LLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSV 164
Cdd:cd07130 145 PVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGST 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 165 PTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVKQTQR 244
Cdd:cd07130 225 AVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 245 IKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVpedpklKDGYYMRPCVLTNcRDDMTCVKEEIFG 324
Cdd:cd07130 305 VRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVID------GPGNYVEPTIVEG-LSDAPIVKEETFA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 325 PVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAelQAGT-CFINNYNVSP--VEL--PFGGYKKSGFGREN 399
Cdd:cd07130 378 PILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLG--PKGSdCGIVNVNIGTsgAEIggAFGGEKETGGGRES 455
|
.
gi 1475409330 400 G 400
Cdd:cd07130 456 G 456
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
2-413 |
1.32e-76 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 245.54 E-value: 1.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCV 81
Cdd:PRK13968 52 YRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTIL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 82 GIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFT 161
Cdd:PRK13968 132 AIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 162 GSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVKQ 241
Cdd:PRK13968 212 GSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 242 TQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEdpklkdGYYMRPCVLTNCRDDMTCVKEE 321
Cdd:PRK13968 292 AAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGA------GNYYAPTVLANVTPEMTAFREE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 322 IFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGR 401
Cdd:PRK13968 366 LFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSH 445
|
410
....*....|..
gi 1475409330 402 VTIEYYSQLKTV 413
Cdd:PRK13968 446 FGLHEFCNIQTV 457
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
2-413 |
2.33e-76 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 245.18 E-value: 2.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHI-QLPGGSFGYTRREPLGVC 80
Cdd:TIGR01722 61 QRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETStQVATRVDVYSIRQPLGVC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSF 160
Cdd:TIGR01722 141 AGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 161 TGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEIlDKFTEEVVK 240
Cdd:TIGR01722 221 VGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 241 QTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDpkLKDGYYMRPCVLTNCRDDMTCVKE 320
Cdd:TIGR01722 300 RAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDG--YEEGNWVGPTLLERVPPTMKAYQE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 321 EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINnyNVSPVELP---FGGYKKSGFGR 397
Cdd:TIGR01722 378 EIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN--VPIPVPLPyfsFTGWKDSFFGD 455
|
410
....*....|....*...
gi 1475409330 398 EN--GRVTIEYYSQLKTV 413
Cdd:TIGR01722 456 HHiyGKQGTHFYTRGKTV 473
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
7-413 |
8.64e-73 |
|
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: 234.81 E-value: 8.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 7 LLEAARIIREREDEIATMECINNGKSIFEARLdIDISWQ---CLEYYAGLAASMAGEHIQ--LPGGSFG--YTRREPLGV 79
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETLL-TEVSGVkndILHMLKNLKKWAKDEKVKdgPLAFMFGkpRIRKEPLGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQGGAA-TGQFLCQHPDvaKV 158
Cdd:cd07135 112 VLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPeTTALLEQKFD--KI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEV 238
Cdd:cd07135 189 FYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEEL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPlLEDTRMGPLINRPHLERVlgfVKVAKEQGAKVLCGGdiyvPEDPKLKdgyYMRPCVLTNCRDDMTCV 318
Cdd:cd07135 269 KKVLDEFYPGGA-NASPDYTRIVNPRHFNRL---KSLLDTTKGKVVIGG----EMDEATR---FIPPTIVSDVSWDDSLM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 319 KEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN--YNVSPVELPFGGYKKSGFG 396
Cdd:cd07135 338 SEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDtlIHVGVDNAPFGGVGDSGYG 417
|
410
....*....|....*..
gi 1475409330 397 RENGRVTIEYYSQLKTV 413
Cdd:cd07135 418 AYHGKYGFDTFTHERTV 434
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
2-396 |
1.92e-72 |
|
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: 234.62 E-value: 1.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHI-----QLPGGSFGYTRREP 76
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIpmgltPASAGRIAFTTREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 77 LGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVA 156
Cdd:cd07148 125 IGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAKGIKpVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTE 236
Cdd:cd07148 205 FFSFIGSARVGWMLRSKLAPGTR-CALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 237 EVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDiyvpedpKLKDGYYmRPCVLTNCRDDMT 316
Cdd:cd07148 284 RLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGK-------RLSDTTY-APTVLLDPPRDAK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 317 CVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVE-LPFGGYKKSGF 395
Cdd:cd07148 356 VSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGY 435
|
.
gi 1475409330 396 G 396
Cdd:cd07148 436 G 436
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
67-413 |
2.64e-69 |
|
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: 225.85 E-value: 2.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 67 GSFGYTRREPLGVCVGIGAWNYPFQIASwksAP---ALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQGGA 143
Cdd:cd07136 91 PSKSYIYYEPYGVVLIIAPWNYPFQLAL---APligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 144 ATGQFLCQHP-DvaKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGT 222
Cdd:cd07136 167 EENQELLDQKfD--YIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 223 RVFVQKEILDKFTEEVVKQTQRIKIGDPlLEDTRMGPLINRPHLERVLGFVKvakeqGAKVLCGGDIYvpedpklKDGYY 302
Cdd:cd07136 245 YVLVHESVKEKFIKELKEEIKKFYGEDP-LESPDYGRIINEKHFDRLAGLLD-----NGKIVFGGNTD-------RETLY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 303 MRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN--YNV 380
Cdd:cd07136 312 IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDtiMHL 391
|
330 340 350
....*....|....*....|....*....|...
gi 1475409330 381 SPVELPFGGYKKSGFGRENGRVTIEYYSQLKTV 413
Cdd:cd07136 392 ANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
67-413 |
3.14e-69 |
|
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: 225.57 E-value: 3.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 67 GSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQGGAATG 146
Cdd:cd07134 91 GTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 147 QFLCQHPdVAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFV 226
Cdd:cd07134 170 QALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 227 QKEILDKFTEEVVKQTQRIKIGDPLLEDTR-MGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIyvpeDPklkDGYYMRP 305
Cdd:cd07134 249 HESVKDAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF----DA---AQRYIAP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 306 CVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN--YNVSPV 383
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDvvLHFLNP 401
|
330 340 350
....*....|....*....|....*....|
gi 1475409330 384 ELPFGGYKKSGFGRENGRVTIEYYSQLKTV 413
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
63-414 |
2.33e-68 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 224.91 E-value: 2.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 63 QLPGGSfgYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQGG 142
Cdd:PTZ00381 98 FGPGKS--YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 143 AATGQFLCQHP-DVakVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNG 221
Cdd:PTZ00381 175 VEVTTELLKEPfDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 222 TRVFVQKEILDKFTEEVvkQTQRIK-IGDPLLEDTRMGPLINRPHLERVLGFVkvaKEQGAKVLCGGDIYVPEDpklkdg 300
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEAL--KEAIKEfFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGGEVDIENK------ 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 301 yYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN--Y 378
Cdd:PTZ00381 322 -YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvF 400
|
330 340 350
....*....|....*....|....*....|....*.
gi 1475409330 379 NVSPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVC 414
Cdd:PTZ00381 401 HLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
2-400 |
1.51e-65 |
|
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: 217.83 E-value: 1.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPG--GSFGYTRREPLGV 79
Cdd:cd07083 78 DRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPypGEDNESFYVGLGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVAKV 158
Cdd:cd07083 158 GVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGvGEEVGAYLTEHERIRGI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 159 SFTGSVPTGMKIMEMSAK------GIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILD 232
Cdd:cd07083 238 NFTGSLETGKKIYEAAARlapgqtWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 233 KFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGaKVLCGGdiyvpedpKLKD--GYYMRPCVLTN 310
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGG--------KRLEgeGYFVAPTVVEE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 311 CRDDMTCVKEEIFGPVMSILSF--DTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV--ELP 386
Cdd:cd07083 389 VPPKARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQP 468
|
410
....*....|....
gi 1475409330 387 FGGYKKSGFGRENG 400
Cdd:cd07083 469 FGGFKLSGTNAKTG 482
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
2-413 |
2.41e-65 |
|
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: 215.43 E-value: 2.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIAtmECIN---NGKSIFEARL-DIDISWQCLEYYA-GLAASMAGE----HIQLPGGSfGYT 72
Cdd:cd07133 21 ERRDRLDRLKALLLDNQDALA--EAISadfGHRSRHETLLaEILPSIAGIKHARkHLKKWMKPSrrhvGLLFLPAK-AEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 73 RREPLGVcVGI-GAWNYPFQIASwksAP---ALACGN-AMVfKPSPFTPVSALLLAEIYSEAGvPPGLFNVVQGGAATGQ 147
Cdd:cd07133 98 EYQPLGV-VGIiVPWNYPLYLAL---GPliaALAAGNrVMI-KPSEFTPRTSALLAELLAEYF-DEDEVAVVTGGADVAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 148 FLCQHP-DvaKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFV 226
Cdd:cd07133 172 AFSSLPfD--HLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 227 QKEILDKFTEEVVKQTQRIkIGDpLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVL-CGgdiyvPEDPKLKDGYYMRP 305
Cdd:cd07133 250 PEDKLEEFVAAAKAAVAKM-YPT-LADNPDYTSIINERHYARLQGLLEDARAKGARVIeLN-----PAGEDFAATRKLPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 306 CVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN--YNVSPV 383
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDtlLHVAQD 402
|
410 420 430
....*....|....*....|....*....|
gi 1475409330 384 ELPFGGYKKSGFGRENGRVTIEYYSQLKTV 413
Cdd:cd07133 403 DLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
3-423 |
2.14e-64 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 217.31 E-value: 2.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 3 RCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHiqLPGGSFG---YTRREPLGV 79
Cdd:PLN02419 175 RQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEY--LPNVSNGvdtYSIREPLGV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 80 CVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVS 159
Cdd:PLN02419 253 CAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 160 FTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCN-GTRVFVQKEilDKFTEEV 238
Cdd:PLN02419 333 FVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDA--KSWEDKL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 239 VKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGG-DIYVPEDPKlkdGYYMRPCVLTNCRDDMTC 317
Cdd:PLN02419 411 VERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGrDIVVPGYEK---GNFIGPTILSGVTPDMEC 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 318 VKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINnyNVSPVELP---FGGYKKSG 394
Cdd:PLN02419 488 YKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN--VPIPVPLPffsFTGNKASF 565
|
410 420 430
....*....|....*....|....*....|.
gi 1475409330 395 FGREN--GRVTIEYYSQLKTVCVEMGDVESA 423
Cdd:PLN02419 566 AGDLNfyGKAGVDFFTQIKLVTQKQKDIHSP 596
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1-400 |
1.04e-62 |
|
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: 210.51 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 1 MERCRILLEAARIIREREDEIATMECINNGKSIFEA----RLDIDIswqcLEYYAGLA-ASMAgeHIQLPGgSFGYTRR- 74
Cdd:cd07125 91 EERAEILEKAADLLEANRGELIALAAAEAGKTLADAdaevREAIDF----CRYYAAQArELFS--DPELPG-PTGELNGl 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 --EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQ 151
Cdd:cd07125 164 elHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGdGEEIGEALVA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 152 HPDVAKVSFTGSVPTGMKIMEMSAK---GIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVcCNGTRV-FVQ 227
Cdd:cd07125 244 HPRIDGVIFTGSTETAKLINRALAErdgPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQR-CSALRLlYLQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 228 KEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKvaKEQG-AKVLCggdiyvPEDPKLKDGYYMRPC 306
Cdd:cd07125 323 EEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTE--LMRGeAWLIA------PAPLDDGNGYFVAPG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 307 VLTNCRDDmtCVKEEIFGPVMSILSFDTE--AEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVE 384
Cdd:cd07125 395 IIEIVGIF--DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIV 472
|
410
....*....|....*...
gi 1475409330 385 L--PFGGYKKSGFGRENG 400
Cdd:cd07125 473 GrqPFGGWGLSGTGPKAG 490
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-412 |
1.11e-57 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 196.90 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIAtmECI--NNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRRE---- 75
Cdd:PLN00412 76 KRAELLHKAAAILKEHKAPIA--ECLvkEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGKFLVSDSFPGNERNkycl 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 ----PLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLC 150
Cdd:PLN00412 154 tskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGkGSEIGDFLT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 151 QHPDVAKVSFTGSvPTGMKImemSAK-GIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKE 229
Cdd:PLN00412 234 MHPGVNCISFTGG-DTGIAI---SKKaGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMES 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 230 ILDKFTEEVVKQTQRIKIGDPLlEDTRMGPLINRPHLERVLGFVKVAKEQGAKvLCggdiyvpeDPKLKDGYYMRPCVLT 309
Cdd:PLN00412 310 VADALVEKVNAKVAKLTVGPPE-DDCDITPVVSESSANFIEGLVMDAKEKGAT-FC--------QEWKREGNLIWPLLLD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 310 NCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNV-SPVELPFG 388
Cdd:PLN00412 380 NVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPArGPDHFPFQ 459
|
410 420
....*....|....*....|....
gi 1475409330 389 GYKKSGFGRENGRVTIEYYSQLKT 412
Cdd:PLN00412 460 GLKDSGIGSQGITNSINMMTKVKS 483
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
71-415 |
3.98e-57 |
|
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: 193.98 E-value: 3.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 71 YTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIyseagVP----PGLFNVVQGGAA-T 145
Cdd:cd07132 95 YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPkyldKECYPVVLGGVEeT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 146 GQFLCQHPDvaKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVF 225
Cdd:cd07132 170 TELLKQRFD--YIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 226 VQKEILDKFTEEvVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKvakeqGAKVLCGGDIyvpeDPKLKdgyYMRP 305
Cdd:cd07132 248 CTPEVQEKFVEA-LKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLS-----GGKVAIGGQT----DEKER---YIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 306 CVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINN--YNVSPV 383
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDtiMHYTLD 394
|
330 340 350
....*....|....*....|....*....|..
gi 1475409330 384 ELPFGGYKKSGFGRENGRVTIEYYSQLKTVCV 415
Cdd:cd07132 395 SLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLV 426
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
2-394 |
4.41e-56 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 192.48 E-value: 4.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLD-------IDISWQCLEYYAGLAAS-MAGEHIQLpggsfgytR 73
Cdd:PRK09457 60 ERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEvtaminkIAISIQAYHERTGEKRSeMADGAAVL--------R 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 74 REPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHP 153
Cdd:PRK09457 132 HRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 154 DVAKVSFTGSVPTGMKI-MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEIL- 231
Cdd:PRK09457 212 DIDGLLFTGSANTGYLLhRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQg 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 232 DKFTEEVVKQTQRIKIGDPLLEDTR-MGPLINRPHLERVLGFVKVAKEQGAKVLCggdiyvpEDPKLKDGY-YMRPCVLt 309
Cdd:PRK09457 292 DAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLL-------EMTQLQAGTgLLTPGII- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 310 ncrdDMTCVK----EEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGtcfINNYNV----S 381
Cdd:PRK09457 364 ----DVTGVAelpdEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAG---IVNWNKpltgA 436
|
410
....*....|...
gi 1475409330 382 PVELPFGGYKKSG 394
Cdd:PRK09457 437 SSAAPFGGVGASG 449
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
11-413 |
5.11e-52 |
|
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: 180.30 E-value: 5.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 11 ARIIREREDEIATMECINNGKSIFEARLDiDISwqCLEYYAGLAAS-----MAGEHIQLPGGSF---GYTRREPLGVCVG 82
Cdd:cd07137 31 LRLVDENEDDIFAALRQDLGKPSAESFRD-EVS--VLVSSCKLAIKelkkwMAPEKVKTPLTTFpakAEIVSEPLGVVLV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 83 IGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAgVPPGLFNVVQGGAATGQFLCQHP-DvaKVSFT 161
Cdd:cd07137 108 ISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTALLEQKwD--KIFFT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 162 GSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANF-LTQGQVCCNGTRVFVQKEILDKFTEEVVK 240
Cdd:cd07137 185 GSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 241 QTQRIkIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQgAKVLCGGDIyvpEDPKLkdgyYMRPCVLTNCRDDMTCVKE 320
Cdd:cd07137 265 TLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGER---DEKNL----YIEPTILLDPPLDSSIMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 321 EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV--ELPFGGYKKSGFGRE 398
Cdd:cd07137 336 EIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAidTLPFGGVGESGFGAY 415
|
410
....*....|....*
gi 1475409330 399 NGRVTIEYYSQLKTV 413
Cdd:cd07137 416 HGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
12-413 |
6.56e-49 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 172.99 E-value: 6.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 12 RIIREREDEIATMECINNGKSIFEARLD--------IDISWQCLEYYaglaasMAGEHIQLPGGSFGYTRR---EPLGVC 80
Cdd:PLN02203 39 RLLKDNEEAIFKALHQDLGKHRVEAYRDevgvltksANLALSNLKKW------MAPKKAKLPLVAFPATAEvvpEPLGVV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 81 VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAeiyseAGVPPGL----FNVVQGGAATGQFLCQHP-Dv 155
Cdd:PLN02203 113 LIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPKYLdskaVKVIEGGPAVGEQLLQHKwD- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 156 aKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLI---IFSDCDMNNAVKGALMANFLT-QGQVCCNGTRVFVQKEIL 231
Cdd:PLN02203 187 -KIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 232 dKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQgAKVLCGGDIyvpeDPKlkdGYYMRPCVLTNC 311
Cdd:PLN02203 266 -PILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSI----DEK---KLFIEPTILLNP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 312 RDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV--ELPFGG 389
Cdd:PLN02203 337 PLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSLPFGG 416
|
410 420
....*....|....*....|....
gi 1475409330 390 YKKSGFGRENGRVTIEYYSQLKTV 413
Cdd:PLN02203 417 VGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
76-419 |
1.27e-48 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 173.10 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 PLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSAL----LLAEIYSEAGVPPGLFNVVQGGAATGQFLCQ 151
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 152 HPDVAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEIL 231
Cdd:PLN02315 234 DTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIY 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 232 DKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEdpklkdGYYMRPCVLtNC 311
Cdd:PLN02315 314 DDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESE------GNFVQPTIV-EI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 312 RDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAElQAGTCFINNYNV----SPVELPF 387
Cdd:PLN02315 387 SPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGP-LGSDCGIVNVNIptngAEIGGAF 465
|
330 340 350
....*....|....*....|....*....|..
gi 1475409330 388 GGYKKSGFGRENGRVTIEYYSQLKTVCVEMGD 419
Cdd:PLN02315 466 GGEKATGGGREAGSDSWKQYMRRSTCTINYGN 497
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
2-394 |
1.63e-48 |
|
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: 172.77 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIR-EREDEI--ATMecINNGKSIFEARLD-----IDIswqcLEYYAGLAASM-AGEHIQLPGGSFGYT 72
Cdd:cd07123 92 DRAAIFLKAADLLSgKYRYELnaATM--LGQGKNVWQAEIDaacelIDF----LRFNVKYAEELyAQQPLSSPAGVWNRL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 73 RREPL-GVCVGIGAWNYPFQIASWKSAPALAcGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLC 150
Cdd:cd07123 166 EYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGdGPVVGDTVL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 151 QHPDVAKVSFTGSVPTGMKIMEMSAKGIK-----P-VTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRV 224
Cdd:cd07123 245 ASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 225 FVQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQ-GAKVLCGGDiyvPEDPKlkdGYYM 303
Cdd:cd07123 325 YVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK---CDDSV---GYFV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 304 RPCVL--TNCRDDMtcVKEEIFGPVMSILSFDTE--AEVLERANDTT-FGLAAGVFTRD---IQRAHRVVAElQAGTCFI 375
Cdd:cd07123 399 EPTVIetTDPKHKL--MTEEIFGPVLTVYVYPDSdfEETLELVDTTSpYALTGAIFAQDrkaIREATDALRN-AAGNFYI 475
|
410 420
....*....|....*....|.
gi 1475409330 376 NNYNVSPV--ELPFGGYKKSG 394
Cdd:cd07123 476 NDKPTGAVvgQQPFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
2-396 |
6.67e-44 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 164.22 E-value: 6.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGK----SIFEARLDIDIswqcLEYYAGLAASMAGEHIQLPG--GSFGYTRRE 75
Cdd:PRK11904 608 ERAAILERAADLLEANRAELIALCVREAGKtlqdAIAEVREAVDF----CRYYAAQARRLFGAPEKLPGptGESNELRLH 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 PLGVCVGIGAWNYP---F--QIASwksapALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFL 149
Cdd:PRK11904 684 GRGVFVCISPWNFPlaiFlgQVAA-----ALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGdGATVGAAL 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 150 CQHPDVAKVSFTGSVPTGMKI-MEMSAKGIKPVTL--ELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVcCNGTRV-F 225
Cdd:PRK11904 759 TADPRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQR-CSALRVlF 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 226 VQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINR-------PHLERVlgfvkvakEQGAKVLCGGDIyvPEDpkLK 298
Cdd:PRK11904 838 VQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAeakanldAHIERM--------KREARLLAQLPL--PAG--TE 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 299 DGYYMRPCV--LtncrDDMTCVKEEIFGPVMSILSFDTE--AEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCF 374
Cdd:PRK11904 906 NGHFVAPTAfeI----DSISQLEREVFGPILHVIRYKASdlDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVY 981
|
410 420
....*....|....*....|....
gi 1475409330 375 INNYNVSPV--ELPFGGYKKSGFG 396
Cdd:PRK11904 982 VNRNQIGAVvgVQPFGGQGLSGTG 1005
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
2-400 |
2.82e-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: 158.15 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGK----SIFEARLDIDIswqcLEYYAGLAasmagEHIqlpggsFGYTRREPL 77
Cdd:TIGR01238 97 ERAAKLDRLADLLELHMPELMALCVREAGKtihnAIAEVREAVDF----CRYYAKQV-----RDV------LGEFSVESR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 GVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVA 156
Cdd:TIGR01238 162 GVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGrGADVGAALTSDPRIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKIMEMSAK-GIKPVTL--ELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDK 233
Cdd:TIGR01238 242 GVAFTGSTEVAQLINQTLAQrEDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 234 FTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVlcgGDIYVPEDPKLKDGYYMRPCVLTncRD 313
Cdd:TIGR01238 322 VLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKI---AQLTLDDSRACQHGTFVAPTLFE--LD 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 314 DMTCVKEEIFGPVMSILSF--DTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV--ELPFGG 389
Cdd:TIGR01238 397 DIAELSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVvgVQPFGG 476
|
410
....*....|.
gi 1475409330 390 YKKSGFGRENG 400
Cdd:TIGR01238 477 QGLSGTGPKAG 487
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
75-413 |
3.92e-43 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 157.52 E-value: 3.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYsEAGVPPGLFNVVQGGAA-TGQFLCQHP 153
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTeTTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 154 DvaKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANF-LTQGQVCCNGTRVFVQKEILD 232
Cdd:PLN02174 190 D--KIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 233 KFTEEVVKQTQRIKIGDPlLEDTRMGPLINRPHLERVLGFVKvAKEQGAKVLCGGDiyvpedpKLKDGYYMRPCVLTNCR 312
Cdd:PLN02174 268 KVIDAMKKELETFYGKNP-MESKDMSRIVNSTHFDRLSKLLD-EKEVSDKIVYGGE-------KDRENLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 313 DDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV--ELPFGGY 390
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGV 418
|
330 340
....*....|....*....|...
gi 1475409330 391 KKSGFGRENGRVTIEYYSQLKTV 413
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
2-396 |
1.07e-36 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 143.08 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKS----IFEARLDIDIswqcLEYYAGLAASMAGEhiqlpggsfgyTRREPL 77
Cdd:PRK11905 613 ERAAILERAADLMEAHMPELFALAVREAGKTlanaIAEVREAVDF----LRYYAAQARRLLNG-----------PGHKPL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 GVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHPDVA 156
Cdd:PRK11905 678 GPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGdGRTVGAALVADPRIA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 157 KVSFTGSVPTGMKI-MEMSAKGIKPVTL--ELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVcCNGTRV-FVQKEILD 232
Cdd:PRK11905 758 GVMFTGSTEVARLIqRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQR-CSALRVlCLQEDVAD 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 233 KFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVlcggdiY-VPEDPKLKDGYYMRPCV--LT 309
Cdd:PRK11905 837 RVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV------HqLPLPAETEKGTFVAPTLieID 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 310 NCRDdmtcVKEEIFGPVMSILSFDTE--AEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV--EL 385
Cdd:PRK11905 911 SISD----LEREVFGPVLHVVRFKADelDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVvgVQ 986
|
410
....*....|.
gi 1475409330 386 PFGGYKKSGFG 396
Cdd:PRK11905 987 PFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
2-396 |
6.13e-36 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 140.84 E-value: 6.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDE---IATME---CINNGksIFEARLDIDIswqcLEYYAGLAASMAGEHiqlpggsfgyTRRE 75
Cdd:COG4230 616 ERAAILERAADLLEAHRAElmaLLVREagkTLPDA--IAEVREAVDF----CRYYAAQARRLFAAP----------TVLR 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 PLGVCVGIGAWNYP---F--QIASwksapALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFL 149
Cdd:COG4230 680 GRGVFVCISPWNFPlaiFtgQVAA-----ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGdGETVGAAL 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 150 CQHPDVAKVSFTGSVPTGMKI-MEMSAKGIKPVTL--ELGGKspliifsdcdmnNA------------VKGALMANFLTQ 214
Cdd:COG4230 755 VADPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQ------------NAmivdssalpeqvVDDVLASAFDSA 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 215 GQVcCNGTRV-FVQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKvlcggdIY-VP 292
Cdd:COG4230 823 GQR-CSALRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRL------VHqLP 895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 293 EDPKLKDGYYMRPCV--LtncrDDMTCVKEEIFGPVMSILSFDTE--AEVLERANDTTFGLAAGVFTRDIQRAHRVVAEL 368
Cdd:COG4230 896 LPEECANGTFVAPTLieI----DSISDLEREVFGPVLHVVRYKADelDKVIDAINATGYGLTLGVHSRIDETIDRVAARA 971
|
410 420 430
....*....|....*....|....*....|..
gi 1475409330 369 QAGTCFINNyN----VSPVElPFGGYKKSGFG 396
Cdd:COG4230 972 RVGNVYVNR-NiigaVVGVQ-PFGGEGLSGTG 1001
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
3-400 |
1.36e-34 |
|
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: 133.52 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 3 RCRILLEAARIIREREDEIATMECINNGKSIFEArLDIDISWQCLEYYAGLAASmaGEHIQLPGGSFGYTR-------RE 75
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIYS--YRIPHEPGNHLGQGLkqqshgyRW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 PLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAG-VPPGLFNVVQGGAATGQFLCQHPD 154
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTMQALLLHPN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 155 VAKVSFTGSVPTGMKIMEMSAKGikPVTLELGGKSPLIIFSDCDMNNAVKGALMAN-FLTQGQVCCNGTRVFV-QKEILD 232
Cdd:cd07084 180 PKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDmTACSGQKCTAQSMLFVpENWSKT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 233 KFTEEVVKQTQRIKIGDPLLedtrmGPLINRPHLERVlgfVKVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCR 312
Cdd:cd07084 258 PLVEKLKALLARRKLEDLLL-----GPVQTFTTLAMI---AHMENLLGSVLLFSGKELKNHSIPSIYGACVASALFVPID 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 313 DDMTC---VKEEIFGPVMSILSF--DTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQ-AGTCFINNY---NVSPV 383
Cdd:cd07084 330 EILKTyelVTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGRTYAILRgrtGVAPN 409
|
410
....*....|....*..
gi 1475409330 384 ELPFGGYKKSGFGRENG 400
Cdd:cd07084 410 QNHGGGPAADPRGAGIG 426
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
2-368 |
1.60e-32 |
|
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: 128.54 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDE---IAtmecINNGKSIFEARLDIDISWQCLEYYAGLAASMA--------GEHIQLP-GGSF 69
Cdd:cd07128 60 ERAAMLKALAKYLMERKEDlyaLS----AATGATRRDSWIDIDGGIGTLFAYASLGRRELpnahflveGDVEPLSkDGTF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 70 G----YTRREplGVCVGIGAWNYPfqiaSW----KSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGV-PPGLFNVVQ 140
Cdd:cd07128 136 VgqhiLTPRR--GVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLIC 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 141 GGaaTGQFL--CQHPDVakVSFTGSVPTGMKIM---EMSAKGIkPVTLELGGKSPLIIFSDcdmnnAVKG----AL---- 207
Cdd:cd07128 210 GS--VGDLLdhLGEQDV--VAFTGSAATAAKLRahpNIVARSI-RFNAEADSLNAAILGPD-----ATPGtpefDLfvke 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 208 MANFLTQ--GQVCCNGTRVFVQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLC 285
Cdd:cd07128 280 VAREMTVkaGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 286 GGDIYVPEDPKLKDGYYMRPCVLTnCRDDM--TCVKE-EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAH 362
Cdd:cd07128 360 GPDRFEVVGADAEKGAFFPPTLLL-CDDPDaaTAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAR 438
|
....*.
gi 1475409330 363 RVVAEL 368
Cdd:cd07128 439 ELVLGA 444
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
2-368 |
2.07e-30 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 122.89 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIqLPGGSFGYTRREPL---- 77
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARL-LRDGEAVQLGKDPAfqgq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 78 -------GVCVGIGAWNYPfqiaSW----KSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGV-PPGLFNVVQGGAAT 145
Cdd:PRK11903 143 hvlvptrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 146 GQFLCQHPDVakVSFTGSVPTGMKIMEMSA---KGIKpVTLELGGKSPLIIFSDCDMNNAVKGALMANF---LTQ--GQV 217
Cdd:PRK11903 219 LLDHLQPFDV--VSFTGSAETAAVLRSHPAvvqRSVR-VNVEADSLNSALLGPDAAPGSEAFDLFVKEVvreMTVksGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 218 CCNGTRVFVQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQgAKVLCGGDIYVPEDPKL 297
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGFALVDADP 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475409330 298 KDGYYMRPCVL-TNCRDDMTCVKE-EIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAEL 368
Cdd:PRK11903 375 AVAACVGPTLLgASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
2-396 |
1.70e-26 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 112.76 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 2 ERCRILLEAARIIrerEDEIATMECI---NNGKS----IFEARLDIDIswqcLEYYAGLAAsmagehiqlpgGSFGYTRR 74
Cdd:PRK11809 705 ERAAILERAADLM---EAQMQTLMGLlvrEAGKTfsnaIAEVREAVDF----LRYYAGQVR-----------DDFDNDTH 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQG-GAATGQFLCQHP 153
Cdd:PRK11809 767 RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGrGETVGAALVADA 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 154 DVAKVSFTGSVPTGMKIME-----MSAKGiKPVTL--ELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVcCNGTRVF- 225
Cdd:PRK11809 847 RVRGVMFTGSTEVARLLQRnlagrLDPQG-RPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQR-CSALRVLc 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 226 VQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLcggDIYVPEDPKLKDGYYMRP 305
Cdd:PRK11809 925 LQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVF---QAARENSEDWQSGTFVPP 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 306 CVLTncRDDMTCVKEEIFGPVMSILSFDTEA--EVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPV 383
Cdd:PRK11809 1002 TLIE--LDSFDELKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAV 1079
|
410
....*....|....*
gi 1475409330 384 --ELPFGGYKKSGFG 396
Cdd:PRK11809 1080 vgVQPFGGEGLSGTG 1094
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
73-343 |
4.72e-19 |
|
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: 88.75 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 73 RREPLG-VCVgIGAWNYP--FQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA----GVPPGLFNVVQG-GAA 144
Cdd:cd07129 102 MLVPLGpVAV-FGASNFPlaFSVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGgGRE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 145 TGQFLCQHPDVAKVSFTGSVPTGMKIMEMSAK---GIkPVTLELGGKSPLIIFSdcdmnNAVK---GALMANF---LTQ- 214
Cdd:cd07129 181 VGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpePI-PFYAELGSVNPVFILP-----GALAergEAIAQGFvgsLTLg 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 215 -GQVCCNGTRVFVQK-EILDKFTEEVVKqtqrikigdpLLEDTRMGPLINRPHLERVL-GFVKVAKEQGAKVLCGGdiyv 291
Cdd:cd07129 255 aGQFCTNPGLVLVPAgPAGDAFIAALAE----------ALAAAPAQTMLTPGIAEAYRqGVEALAAAPGVRVLAGG---- 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1475409330 292 pedPKLKDGYYMRPCVLT----NCRDDMTcVKEEIFGPVMSILSFDTEAEVLERAN 343
Cdd:cd07129 321 ---AAAEGGNQAAPTLFKvdaaAFLADPA-LQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
76-371 |
5.48e-12 |
|
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: 67.50 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 76 PLGVCVGIGAWNYPfqiaSWKSAPA----LACGNAMVFKPSPFTPVSALLLA----EIYSEAGVPPGLFNVV--QGGAAT 145
Cdd:cd07127 193 PRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFDPNLVTLAadTPEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 146 GQFLCQHPDVAKVSFTGSVPTGmKIMEMSAKGiKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVF 225
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFG-DWLEANARQ-AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 226 VQKEIL---------DKFTEEVVKQTQRIkIGDPLLEDTRMGPLINRPHLERVlgfvkVAKEQGAKVLCGGDIYvpEDPK 296
Cdd:cd07127 347 VPRDGIqtddgrksfDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI-----AEARQLGEVLLASEAV--AHPE 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1475409330 297 LKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTF---GLAAGVFTRDIQRAHRVV-AELQAG 371
Cdd:cd07127 419 FPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTDPEVVERVQeAALDAG 497
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
75-364 |
5.50e-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: 60.74 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPG-----LFNVVQGGAATGQFL 149
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGapenlIGWIDNPSIELAQRL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 150 CQHPDVAKVSFTGsvptGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKE 229
Cdd:cd07081 174 MKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 230 ILDKFTEE-------VVKQTQRIKIGDPLLEDTRMGP-LINRPHlervlgfVKVAKEQGAKvlcggdiyVPEDPKLKDGY 301
Cdd:cd07081 250 VYDEVMRLfegqgayKLTAEELQQVQPVILKNGDVNRdIVGQDA-------YKIAAAAGLK--------VPQETRILIGE 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1475409330 302 ymrpcvlTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERA----NDTTFGLAAGVFTRDIQRAHRV 364
Cdd:cd07081 315 -------VTSLAEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIENM 374
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
71-260 |
2.00e-08 |
|
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: 56.08 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 71 YTRREPLGVCVGIGAWNYPFqIASWKSAPALACGNAMVFKPSPFTPVS----ALLLAEIYSEAGVPPGLFNVVQGGAATG 146
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTnralALLFQAADAAHGPKILVLYVPHPSDELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 147 QFLCQHPDVAKVSFTGSvPTGMKIMEMSAKGIkPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTqgQVCCNGTRVFV 226
Cdd:cd07077 174 EELLSHPKIDLIVATGG-RDAVDAAVKHSPHI-PVIGFGAGNSPVVVDETADEERASGSVHDSKFFD--QNACASEQNLY 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1475409330 227 ---------QKEILDKFTEEVVK--QTQRIKIGDPLLED-----TRMGPL 260
Cdd:cd07077 250 vvddvldplYEEFKLKLVVEGLKvpQETKPLSKETTPSFddealESMTPL 299
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
75-376 |
3.62e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 49.03 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 75 EPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEA----GVPPGLFNVVQGG--AATGQf 148
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEPsiELTQE- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 149 LCQHPDVAKVSFTGsvptGMKIMEMSAKGIKPVtleLG---GKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVF 225
Cdd:cd07122 173 LMKHPDVDLILATG----GPGMVKAAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 226 VQKEILDKFTEEVVKQ-------TQRIKIGDPLLEDTRM--GPLINRP--HLERVLGFvKVAKeqGAKVLCGGDIYV-PE 293
Cdd:cd07122 246 VDDEIYDEVRAELKRRgayflneEEKEKLEKALFDDGGTlnPDIVGKSaqKIAELAGI-EVPE--DTKVLVAEETGVgPE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409330 294 DPklkdgyYMRpcvltncrddmtcvkeEIFGPVMSILSFDTEAEVLERAND-TTFGLA---AGVFTRDIQRAHRVVAELQ 369
Cdd:cd07122 323 EP------LSR----------------EKLSPVLAFYRAEDFEEALEKARElLEYGGAghtAVIHSNDEEVIEEFALRMP 380
|
....*..
gi 1475409330 370 AGTCFIN 376
Cdd:cd07122 381 VSRILVN 387
|
|
| |
