|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
41-497 |
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: 839.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADV 120
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 121 LSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTAL 200
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 201 ILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVTLELGGKSALIVFDDADI 280
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 281 DSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAE 360
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 361 GATKLCGGDRVAVH-GLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSR 439
Cdd:cd07090 320 GAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 440 SYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVNTG 497
Cdd:cd07090 400 AHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
34-492 |
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: 643.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 34 PSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPI 113
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 114 AEAKADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSP 193
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 194 LSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSAL 272
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 273 IVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEG 352
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 353 YISTAIAEGATKLCGGDRvavhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGL 432
Cdd:pfam00171 323 YVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972260679 433 VTKDLSRSYRVSEQLNAGNVYVNTYNDVSP-LVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
19-503 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 640.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 19 LELSSHFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHC 98
Cdd:PRK13252 4 QPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 99 NDIAYWECISNGKPIAEAK-ADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKT 177
Cdd:PRK13252 84 DELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 178 APALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMkACADR 257
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVM-AAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 258 NIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQ 337
Cdd:PRK13252 243 SLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 338 VGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEA 417
Cdd:PRK13252 323 FGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 418 IKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVNTG 497
Cdd:PRK13252 403 IARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMG 482
|
....*.
gi 1972260679 498 TCPNPF 503
Cdd:PRK13252 483 PFQSPF 488
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
24-496 |
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: 625.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAY 103
Cdd:COG1012 8 LFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 104 WECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPLDASRY-AYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALA 182
Cdd:COG1012 88 LLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTrAYVRREPLGVVGAITPWNFPLALAAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 183 CGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKP 261
Cdd:COG1012 168 AGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA-ENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 262 VTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSH 341
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 342 ISAEHRNKVEGYISTAIAEGATKLCGGDRVAVhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIA 421
Cdd:COG1012 327 ISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972260679 422 NDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDV-SPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVNT 496
Cdd:COG1012 404 NDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
25-490 |
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: 551.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW 104
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 105 ECISNGKPIAEA-KADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALAC 183
Cdd:TIGR01804 81 ETLDTGKTLQETiVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 184 GNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPV 262
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDgAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 263 TLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHI 342
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 343 SAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAN 422
Cdd:TIGR01804 320 SAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 423 DTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLK 490
Cdd:TIGR01804 400 DTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
62-494 |
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: 536.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 62 DLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQH 141
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 142 VPL-DASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQ 220
Cdd:cd07078 81 IPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 221 GDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVC 299
Cdd:cd07078 161 GDGDEVgAALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 300 SNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVavhGLENG 379
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL---EGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 380 FYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYND 459
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 1972260679 460 -VSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07078 397 gAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
41-494 |
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: 520.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQ--WAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA 118
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQHVPLDASRY-AYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPV 197
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYlNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 198 TALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFD 276
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-ENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 277 DADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYIST 356
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 357 AIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKD 436
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 437 LSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
41-492 |
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: 516.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA-D 119
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTA 199
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 200 LILAEILKSAGLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVTLELGGKSALIVFDDA 278
Cdd:cd07093 161 WLLAELANEAGLPPGVVNVVHGFGPEAGAaLVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 279 DIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAI 358
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 359 AEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLS 438
Cdd:cd07093 320 AEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 439 RSYRVSEQLNAGNVYVNTYNdVSPL-VPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07093 400 RAHRVARRLEAGTVWVNCWL-VRDLrTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
25-492 |
1.63e-180 |
|
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: 514.84 E-value: 1.63e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 YWECISNGKPIAE-AKADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPAL 181
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 182 ACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLI-HHDGVSKVSFTGSIPTGKKIMKACADRNIK 260
Cdd:cd07091 167 AAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAIsSHMDVDKIAFTGSTAVGRTIMEAAAKSNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 261 PVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGS 340
Cdd:cd07091 247 KVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 341 HISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKI 420
Cdd:cd07091 327 QVSKAQFDKILSYIESGKKEGATLLTGGERHG----SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972260679 421 ANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
41-495 |
9.41e-173 |
|
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: 494.27 E-value: 9.41e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAK-AD 119
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTA 199
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 200 LILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVTLELGGKSALIVFDDA 278
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVAgAALVEHPDVDKITFTGSTAVGRKIMQGAAG-NLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 279 DIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAI 358
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 359 AEGATKLCGGDRVAVHGlengFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLS 438
Cdd:cd07115 320 EEGARLLTGGKRPGARG----FFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1972260679 439 RSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
37-494 |
5.26e-169 |
|
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: 485.18 E-value: 5.26e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 37 RKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIA 114
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 115 EAKA-DVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSP 193
Cdd:cd07112 82 DALAvDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 194 LSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIKPVTLELGGKSAL 272
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHTAgEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 273 IVFDDA-DIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVE 351
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 352 GYISTAIAEGATKLCGGDRVAVHGleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAG 431
Cdd:cd07112 322 GYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972260679 432 LVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
41-492 |
5.91e-168 |
|
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: 481.93 E-value: 5.91e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAywECIS--NGKPIAEAKA 118
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLA--RLLTleQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQHVPLDA-SRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPV 197
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 198 TALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVTLELGGKSALIVFD 276
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSpAEIGEALCASPRVRKISFTGSTAVGKLLMAQAAD-TVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 277 DADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYIST 356
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 357 AIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKD 436
Cdd:cd07103 318 AVAKGAKVLTGGKRLG----LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1972260679 437 LSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
25-496 |
6.23e-166 |
|
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: 477.96 E-value: 6.23e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 YWECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALA 182
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 183 CGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKP 261
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAG-NVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 262 VTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSH 341
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 342 ISAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIA 421
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 422 NDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVNT 496
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
41-492 |
1.20e-161 |
|
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: 466.06 E-value: 1.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADV 120
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 121 LSCVDTFYFYSGIASDL---LGQHVPLDASRY-AYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSP 196
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 197 VTALILAEILKSAGLPDGVFNVIQGDA-ETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVF 275
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGdEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 276 DDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYIS 355
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 356 TAIAEGATKLCGGDRVAvhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTK 435
Cdd:cd07110 320 RGKEEGARLLCGGRRPA--HLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1972260679 436 DLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
44-494 |
1.58e-158 |
|
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: 457.95 E-value: 1.58e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 44 PRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVL 121
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 122 SCVDTFYFYSGIASDLLGQ-HVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTAL 200
Cdd:cd07118 84 GAADLWRYAASLARTLHGDsYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 201 ILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDAD 279
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 280 IDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIA 359
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 360 EGATKLCGGDRVAVhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSR 439
Cdd:cd07118 323 EGATLLLGGERLAS---AAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 440 SYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
25-494 |
3.32e-156 |
|
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: 452.80 E-value: 3.32e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 ywECIS--NGKPIAEAK-ADVLSCVDTFYFYSGIASDL-LGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTA 178
Cdd:cd07139 82 --RLWTaeNGMPISWSRrAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 179 PALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRn 258
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 259 IKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQV 338
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 339 GSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAI 418
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGRPA--GLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972260679 419 KIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYnDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07139 397 RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
41-494 |
2.19e-155 |
|
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: 450.15 E-value: 2.19e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWA-KSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKAD 119
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTA 199
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 200 LILAEILKSAGLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVTLELGGKSALIVFDDA 278
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 279 DIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLkEDTQVGSHISAEHRNKVEGYISTAI 358
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 359 AEGATKLCGGdRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLS 438
Cdd:cd07109 319 ARGARIVAGG-RIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1972260679 439 RSYRVSEQLNAGNVYVNTYNDVSPL-VPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAGGGIeLPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-494 |
5.90e-155 |
|
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: 449.78 E-value: 5.90e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEFPSDRkfEVIEP-RSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07097 3 NYIDGEWVAGGDGE--ENRNPsDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 ywECIS--NGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVP-LDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAP 179
Cdd:cd07097 81 --RLLTreEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 180 ALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRN 258
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSgSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 259 IKpVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQV 338
Cdd:cd07097 239 AR-VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 339 GSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAI 418
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLK--RPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 419 KIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVN-TYNDVSPLVPFGGVGESGFG-RENGTAVLEHYTHLKSVFV 494
Cdd:cd07097 396 AIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
25-495 |
4.67e-152 |
|
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: 442.62 E-value: 4.67e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA-QKQWAKSSWMERSEILKKTGDLLKTHCNDIAY 103
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 104 WECISNGKPI-AEAKADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALA 182
Cdd:cd07144 91 IEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 183 CGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKP 261
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-QNLKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 262 VTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHT-QKMKIGDPLKEDTQVGS 340
Cdd:cd07144 250 VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 341 HISAEHRNKVEGYISTAIAEGAtKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKI 420
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGA-KLVYGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKK 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 421 ANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:cd07144 409 ANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHIN 483
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
24-493 |
8.24e-152 |
|
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: 441.17 E-value: 8.24e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAY 103
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 104 WECISNGKPIAEAK-ADVLSCVDTFyfysGIASDLLGQhvpldasrYAYTRRL--------PVGVVAAIGAWNYPIQTCS 174
Cdd:cd07138 81 AITLEMGAPITLARaAQVGLGIGHL----RAAADALKD--------FEFEERRgnslvvrePIGVCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 175 WKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKA 253
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 254 CADRnIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLK 333
Cdd:cd07138 229 AADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 334 EDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGG-DRVAvhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFD 412
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRPE--GLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 413 TEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNtYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
.
gi 1972260679 493 F 493
Cdd:cd07138 465 Q 465
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
25-495 |
9.28e-152 |
|
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: 441.97 E-value: 9.28e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA-QKQWAKS-SWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 YWECISNGKPI-AEAKADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPAL 181
Cdd:cd07143 90 SIEALDNGKTFgTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 182 ACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIK 260
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 261 PVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGS 340
Cdd:cd07143 250 KVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 341 HISAEHRNKVEGYISTAIAEGATKLCGGDRvavHGLEnGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKI 420
Cdd:cd07143 330 QVSQIQYERIMSYIESGKAEGATVETGGKR---HGNE-GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 421 ANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:cd07143 406 ANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
25-496 |
1.02e-151 |
|
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: 441.78 E-value: 1.02e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW 104
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 105 ECISNGKPIAEAK-ADVLSCVDTF-YFYSGIASDLlGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALA 182
Cdd:cd07559 84 ETLDNGKPIRETLaADIPLAIDHFrYFAGVIRAQE-GSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 183 CGNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKP 261
Cdd:cd07559 163 AGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 262 VTLELGGKSALIVFDDA-----DIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDT 336
Cdd:cd07559 241 VTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 337 QVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDE 416
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 417 AIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVNT 496
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
61-490 |
1.58e-151 |
|
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: 439.27 E-value: 1.58e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 61 VDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW---ECisnGKPIAEAKADVLSCVDTFYFYSGIASDL 137
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWlirES---GSTRPKAAFEVGAAIAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 138 LGQHVPLD-ASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVT-ALILAEILKSAGLPDGV 215
Cdd:cd07104 79 EGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 216 FNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYS 294
Cdd:cd07104 159 LNVVPGGGSEIGDaLVEHPRVRMISFTGSTAVGRHIGELAG-RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 295 QGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRvavh 374
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 375 gleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYV 454
Cdd:cd07104 314 ---EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 1972260679 455 N--TYNDvSPLVPFGGVGESGFGRENGTAVLEHYTHLK 490
Cdd:cd07104 391 NdqTVND-EPHVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-495 |
2.43e-151 |
|
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: 440.63 E-value: 2.43e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEFPSDRKFEVIEPRSGKPM-ATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 YW---ECisnGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPLD-ASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTA 178
Cdd:cd07131 81 RLvtrEM---GKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 179 PALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACADR 257
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 258 NiKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQ 337
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 338 VGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEA 417
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 418 IKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNtyndvSPLV------PFGGVGESGFG-RENGTAVLEHYTHLK 490
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN-----APTIgaevhlPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
....*
gi 1972260679 491 SVFVN 495
Cdd:cd07131 472 AVYVD 476
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
25-492 |
8.30e-151 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 440.32 E-value: 8.30e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA-----QKQWAKSSWMERSEILKKTGDLLKTHCN 99
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 100 DIAYWECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLG-QHVPLD---ASRYAYTRRLPVGVVAAIGAWNYPIQTCSW 175
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkQKAPVSlpmETFKGYVLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 176 KTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIPTGKKIMKAC 254
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 255 AdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKE 334
Cdd:PLN02467 251 A-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 335 DTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRvaVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTE 414
Cdd:PLN02467 330 GCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 415 DEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:PLN02467 408 DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
41-494 |
1.81e-149 |
|
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: 434.65 E-value: 1.81e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADV 120
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 121 LSCVDTFYFYSGIasDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTAL 200
Cdd:cd07106 81 GGAVAWLRYTASL--DLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 201 ILAEILKSAgLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVTLELGGKSALIVFDDADI 280
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 281 DSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAE 360
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 361 GATKLCGGDRVAVHGlengFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRS 440
Cdd:cd07106 317 GAKVLAGGEPLDGPG----YFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1972260679 441 YRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
35-494 |
1.95e-147 |
|
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: 430.62 E-value: 1.95e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 35 SDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQ---WAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGK 111
Cdd:cd07141 20 SGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 112 PIAEAK-ADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYK 190
Cdd:cd07141 100 PFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 191 PSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIKPVTLELGGK 269
Cdd:cd07141 180 PAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAgAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRVTLELGGK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 270 SALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNK 349
Cdd:cd07141 260 SPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 350 VEGYISTAIAEGATKLCGGDRvavHGlENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLA 429
Cdd:cd07141 340 ILELIESGKKEGAKLECGGKR---HG-DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 430 AGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07141 416 AAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
25-492 |
6.68e-147 |
|
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: 429.22 E-value: 6.68e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 YWECISNGKPIAEAK-ADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPAL 181
Cdd:cd07142 87 ALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 182 ACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLI-HHDGVSKVSFTGSIPTGKKIMKACADRNIK 260
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIaSHMDVDKVAFTGSTEVGKIIMQLAAKSNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 261 PVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGS 340
Cdd:cd07142 247 PVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 341 HISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKI 420
Cdd:cd07142 327 QVDKEQFEKILSYIEHGKEEGATLITGGDRIG----SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKR 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972260679 421 ANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07142 403 ANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
66-494 |
2.93e-144 |
|
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: 418.56 E-value: 2.93e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 66 KEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPL- 144
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 145 DASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDA- 223
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 224 ETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNAS 303
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 304 KVLVHKSVLKEFTKKLVdhtqkmkigdplkedtqvgshisaehrnkvegyistaiaegatklcggdrvavhglengfyls 383
Cdd:cd06534 240 RLLVHESIYDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 384 pCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYND-VSP 462
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 1972260679 463 LVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
41-494 |
1.66e-143 |
|
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: 419.84 E-value: 1.66e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPI-AEAKAD 119
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTA 199
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 200 LILAEILkSAGLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRnIKPVTLELGGKSALIVFDDA 278
Cdd:cd07108 161 LLLAEIL-AQVLPAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR-LIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 279 DIDSAVSCAMMA-NFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTA 357
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 358 IAE-GATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKD 436
Cdd:cd07108 319 LSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1972260679 437 LSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENG-TAVLEHYTHLKSVFV 494
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
41-494 |
1.75e-143 |
|
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: 419.73 E-value: 1.75e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWME-RSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA- 118
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTDAEeRARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 --DVLscVDTFYFYSGIASDLLGQH-VPLDASRYAYTRRL----PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKP 191
Cdd:cd07089 81 qvDGP--IGHLRYFADLADSFPWEFdLPVPALRGGPGRRVvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 192 SPLSPVTALILAEILKSAGLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVTLELGGKS 270
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGsDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 271 ALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKV 350
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 351 EGYISTAIAEGATKLCGGDRVAvhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAA 430
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPA--GLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972260679 431 GLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07089 396 GVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
39-492 |
3.31e-141 |
|
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: 413.92 E-value: 3.31e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 39 FEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA 118
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQHVPLDAS-----RYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSP 193
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDASpggegRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 194 LSPVTALILAEILKSAGLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKACAdrnIKPVTLELGGKSAL 272
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDaLVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 273 IVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEG 352
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 353 YISTAIAEGATKLCGGDRvavhgleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGL 432
Cdd:cd07149 318 WVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972260679 433 VTKDLSRSYRVSEQLNAGNVYVntyNDVSPL----VPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMI---NDSSTFrvdhMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
41-494 |
4.66e-141 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 413.26 E-value: 4.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKAD- 119
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQhvplDASRYA-----YTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPL 194
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGP----AAGEYLpghtsMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 195 SPVTALILAEILKSaGLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVTLELGGKSALI 273
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDaLVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 274 VFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGY 353
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 354 ISTAiAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLV 433
Cdd:cd07092 315 VERA-PAHARVLTGGRRAE----GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVW 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972260679 434 TKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07092 390 TRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
25-496 |
1.58e-140 |
|
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: 413.00 E-value: 1.58e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW 104
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 105 ECISNGKPIAEAKA-DVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALAC 183
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 184 GNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIkPV 262
Cdd:cd07117 164 GNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI-PA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 263 TLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHI 342
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 343 SAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAN 422
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972260679 423 DTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVNT 496
Cdd:cd07117 402 DSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
41-495 |
4.52e-140 |
|
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: 411.00 E-value: 4.52e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 41 VIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADV 120
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 121 LSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTAL 200
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 201 ILAEILKSAgLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKACADRnIKPVTLELGGKSALIVFDDAD 279
Cdd:cd07107 161 RLAELAREV-LPPGVFNILPGDGATAGAaLVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 280 IDSAVSCAMMA-NFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAI 358
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 359 AEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLS 438
Cdd:cd07107 319 REGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1972260679 439 RSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
39-495 |
9.45e-139 |
|
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: 408.49 E-value: 9.45e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 39 FEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA 118
Cdd:cd07086 15 FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQHVPLD-ASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPV 197
Cdd:cd07086 95 EVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 198 TAL----ILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNiKPVTLELGGKSALI 273
Cdd:cd07086 175 TAIavtkILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF-GRVLLELGGNNAII 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 274 VFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGY 353
Cdd:cd07086 254 VMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 354 ISTAIAEGATKLCGGDRVAvhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLV 433
Cdd:cd07086 334 IEIAKSQGGTVLTGGKRID--GGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIF 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 434 TKDLSRSYRVSEQ--LNAGNVYVNTyndvsPLV------PFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:cd07086 412 TEDLREAFRWLGPkgSDCGIVNVNI-----PTSgaeiggAFGGEKETGGGRESGSDAWKQYMRRSTCTIN 476
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
25-497 |
4.64e-138 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 406.60 E-value: 4.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGnhvefpSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW 104
Cdd:PRK13473 11 LVAG------EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 105 ECISNGKPIAEAKAD-VLSCVDTFYFYSGIASDLLGQhvplDASRYA--YT---RRLPVGVVAAIGAWNYPIQTCSWKTA 178
Cdd:PRK13473 85 ESLNCGKPLHLALNDeIPAIVDVFRFFAGAARCLEGK----AAGEYLegHTsmiRRDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 179 PALACGNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADr 257
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 258 NIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQ 337
Cdd:PRK13473 239 SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 338 VGSHISAEHRNKVEGYISTAIAEG-ATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDE 416
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPD----GKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 417 AIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYndvSPLV---PFGGVGESGFGRENGTAVLEHYTHLKSVF 493
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTH---FMLVsemPHGGQKQSGYGKDMSLYGLEDYTVVRHVM 471
|
....
gi 1972260679 494 VNTG 497
Cdd:PRK13473 472 VKHT 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
24-494 |
2.59e-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: 404.90 E-value: 2.59e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA-QKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 YWECISNGKPIAEAKADVLSCVDTFY-FYSGIASDLLGQ----HVPL-DASRY-AYTRRLPVGVVAAIGAWNYPIQTCSW 175
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLrYFAGWATKINGEtlapSIPSmQGERYtAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 176 KTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACA 255
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 256 DrNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKED 335
Cdd:cd07113 242 S-DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 336 TQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTED 415
Cdd:cd07113 321 VMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA----GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972260679 416 EAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
25-495 |
3.36e-136 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 402.92 E-value: 3.36e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW 104
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 105 ECISNGKPIAEAKADVL---SCVDtfyFYSGIASDLLGQHVPL-DASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPA 180
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAygaSFLE---YFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 181 LACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKACADrNI 259
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDaLLASPKVRKITFTGSTAVGKKLMAGAAA-TV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 260 KPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVG 339
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 340 SHISAEHRNKVEGYISTAIAEGATKLCGGDRvavHGLENGFYLsPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIK 419
Cdd:PLN02278 344 PLINEAAVQKVESHVQDAVSKGAKVLLGGKR---HSLGGTFYE-PTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972260679 420 IANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLG 495
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
44-492 |
5.23e-136 |
|
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: 400.44 E-value: 5.23e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 44 PRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVLSC 123
Cdd:cd07099 3 PATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 124 VDTFYFYSGIASDLLGQHV----PLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTA 199
Cdd:cd07099 83 LEAIDWAARNAPRVLAPRKvptgLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 200 LILAEILKSAGLPDGVFNVIQGDAETAQDLIHHdGVSKVSFTGSIPTGKKIMKACADRNIkPVTLELGGKSALIVFDDAD 279
Cdd:cd07099 163 ELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLI-PVVLELGGKDPMIVLADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 280 IDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIA 359
Cdd:cd07099 241 LERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 360 EGATKLCGGDRVAVHGLengfYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSR 439
Cdd:cd07099 321 KGAKALTGGARSNGGGP----FYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 440 SYRVSEQLNAGNVYVN--TYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07099 397 AEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
25-494 |
6.05e-136 |
|
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: 400.87 E-value: 6.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW 104
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 105 ECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPLD-ASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALAC 183
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 184 GNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPV 262
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRgSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 263 TLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHI 342
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 343 SAEHRNKVEGYISTAIAEGATKLCGGDRVAVhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAN 422
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKRPEG---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972260679 423 DTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNdVSPLVPF-GGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINREN-FEAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
16-492 |
1.13e-134 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 398.81 E-value: 1.13e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 16 TKLlelsshFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEILKKTGDL 93
Cdd:PLN02766 21 TKL------FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 94 LKTHCNDIAYWECISNGKPIAEAKA-DVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQT 172
Cdd:PLN02766 95 IEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 173 CSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLI-HHDGVSKVSFTGSIPTGKKIM 251
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIaSHMDVDKVSFTGSTEVGRKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 252 KACADRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDP 331
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 332 LKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPF 411
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCG----DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKF 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 412 DTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKS 491
Cdd:PLN02766 411 KTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKS 490
|
.
gi 1972260679 492 V 492
Cdd:PLN02766 491 V 491
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
39-494 |
2.01e-134 |
|
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: 396.32 E-value: 2.01e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 39 FEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA 118
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQHVPLD-ASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPV 197
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 198 TALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFD 276
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGgAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 277 DADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYIST 356
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 357 AIAEGATKLCGGDRvavhgleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKD 436
Cdd:cd07150 320 AVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 437 LSRSYRVSEQLNAGNVYVN--TYNDvSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07150 393 LQRAFKLAERLESGMVHINdpTILD-EAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
61-494 |
2.02e-134 |
|
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: 395.68 E-value: 2.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 61 VDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAywECISN--GKPIAEAKADVLSCVDTFYFYSGIASDLL 138
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELA--RLITLemGKPIAEARAEVEKCAWICRYYAENAEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 139 -GQHVPLDASRyAYTRRLPVGVVAAIGAWNYPIqtcsWKT----APALACGNAVIYKPSPLSPVTALILAEILKSAGLPD 213
Cdd:cd07100 79 aDEPIETDAGK-AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 214 GVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKImKACADRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFY 293
Cdd:cd07100 154 GVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 294 SQGQVCsNASK-VLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVA 372
Cdd:cd07100 233 NAGQSC-IAAKrFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 373 vhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNV 452
Cdd:cd07100 312 ----GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1972260679 453 YVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07100 388 FINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
55-488 |
9.91e-134 |
|
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: 394.35 E-value: 9.91e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 55 YATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVLSCVDTFYFYSGIA 134
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 135 SDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTA-LILAEILKSAGLPD 213
Cdd:cd07152 89 TQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 214 GVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFY 293
Cdd:cd07152 169 GVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 294 SQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRvav 373
Cdd:cd07152 248 HQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 374 hgleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVY 453
Cdd:cd07152 325 ----DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLH 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 1972260679 454 VN--TYNDvSPLVPFGGVGESGFG-RENGTAVLEHYTH 488
Cdd:cd07152 401 INdqTVND-EPHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
39-477 |
6.79e-132 |
|
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: 390.17 E-value: 6.79e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 39 FEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA 118
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQHVPLDA-----SRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSP 193
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 194 LSPVTALILAEILKSAGLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKAcADRNIKPVTLELGGKSAL 272
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDeIVTNPKVNMISFTGSTAVGLLIASK-AGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 273 IVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEG 352
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 353 YISTAIAEGATKLCGGDRvavhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGL 432
Cdd:cd07145 320 LVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1972260679 433 VTKDLSRSYRVSEQLNAGNVYVNTyndvSPLV-----PFGGVGESGFGRE 477
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVIND----STRFrwdnlPFGGFKKSGIGRE 439
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-492 |
1.69e-129 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 386.86 E-value: 1.69e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 19 LELSSHFVAGNHVEFPSDRKFEVIEPRSGKPMAtwHYATRDQVDLT--VKEAKKA--QKQWAKSSWMERSEILKKTGDLL 94
Cdd:PLN02466 55 VSYTQLLINGQFVDAASGKTFPTLDPRTGEVIA--HVAEGDAEDVNraVAAARKAfdEGPWPKMTAYERSRILLRFADLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 95 KTHCNDIAYWECISNGKPIAE-AKADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTC 173
Cdd:PLN02466 133 EKHNDELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 174 SWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMK 252
Cdd:PLN02466 213 AWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAgAALASHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 253 ACADRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPL 332
Cdd:PLN02466 293 LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPF 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 333 KEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFD 412
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 413 TEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
39-492 |
5.27e-129 |
|
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: 382.75 E-value: 5.27e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 39 FEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA 118
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQHVPLDAS-----RYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSP 193
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 194 LSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKiMKACADRniKPVTLELGGKSALI 273
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWD-LKARAGK--KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 274 VFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGY 353
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 354 ISTAIAEGATKLCGGDRvavhgleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLV 433
Cdd:cd07147 318 VNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972260679 434 TKDLSRSYRVSEQLNAGNVYVntyNDVSPL----VPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVI---NDVPTFrvdhMPYGGVKDSGIGREGVRYAIEEMTEPRLL 450
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
25-494 |
5.07e-127 |
|
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: 378.76 E-value: 5.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 YWECISNGKPIAEA-KADVLSCVDTFYFYSGIASDLLGQHVPLDASR----YAYTRRLPVGVVAAIGAWNYPIQTCSWKT 177
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARpnrnLTLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 178 APALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACAD 256
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKSCAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 257 RNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDT 336
Cdd:cd07140 249 SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRST 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 337 QVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTED- 415
Cdd:cd07140 329 DHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVD----RPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDv 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 416 -EAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07140 405 dGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
24-486 |
8.15e-127 |
|
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: 378.28 E-value: 8.15e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEfPSDRK-FEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07111 24 HFINGKWVK-PENRKsFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 YWECISNGKPIAEAK-ADVLSCVDTFYFYSGIAsdllgqhvplDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPAL 181
Cdd:cd07111 103 VLESLDNGKPIRESRdCDIPLVARHFYHHAGWA----------QLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 182 ACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNiKP 261
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG-KK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 262 VTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSH 341
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 342 ISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIA 421
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 422 NDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHY 486
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
28-494 |
1.99e-124 |
|
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: 371.25 E-value: 1.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 28 GNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECI 107
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 108 SNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPLDA---SRYAYtrRLPVGVVAAIGAWNYPIQTCSWKTAPALACG 184
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVpgkENRVY--REPLGVVGVISPWNFPLHLSMRSVAPALALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 185 NAVIYKPSPLSPVTA-LILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPV 262
Cdd:cd07151 159 NAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAgSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG-RHLKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 263 TLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHI 342
Cdd:cd07151 238 ALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 343 SAEHRNKVEGYISTAIAEGATKLCGGDRvavhgleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAN 422
Cdd:cd07151 318 NESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972260679 423 DTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVN--TYNDvSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVND-EPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
10-494 |
5.13e-123 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 368.84 E-value: 5.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 10 LNSLTETKLlelsshFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKA--QKQWAKSSWMERSEIL 87
Cdd:PRK09847 14 LSLAIENRL------FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 88 KKTGDLLKTHCNDIAYWECISNGKPIAEA-KADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAW 166
Cdd:PRK09847 88 NKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 167 NYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIP 245
Cdd:PRK09847 168 NFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 246 TGKKIMKACADRNIKPVTLELGGKSALIVFDDA-DIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQ 324
Cdd:PRK09847 248 TGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 325 KMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEGatklcggdRVAVHGLENGF--YLSPCILTGITPKMTVYREEIF 402
Cdd:PRK09847 328 NWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG--------QLLLDGRNAGLaaAIGPTIFVDVDPNASLSREEIF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 403 GSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAV 482
Cdd:PRK09847 400 GPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHA 479
|
490
....*....|..
gi 1972260679 483 LEHYTHLKSVFV 494
Cdd:PRK09847 480 LEKFTELKTIWI 491
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-492 |
1.12e-122 |
|
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: 366.37 E-value: 1.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 40 EVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKAD 119
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQHVPLDAS-----RYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPL 194
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDATqgsdnRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 195 SPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdrnIKPVTLELGGKSALI 273
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 274 VFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGY 353
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 354 ISTAIAEGATKLCGGDRvavhgleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLV 433
Cdd:cd07094 319 VEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 434 TKDLSRSYRVSEQLNAGNVYVNTYNDV-SPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFrTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
25-494 |
1.23e-120 |
|
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: 362.15 E-value: 1.23e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW 104
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 105 ECISNGKPIAEA-KADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALAC 183
Cdd:cd07116 84 ETWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 184 GNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQG-DAETAQDLIHHDGVSKVSFTGSIPTGKKIMKAcADRNIKPV 262
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY-ASENIIPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 263 TLELGGKSALIVF------DDADIDSAVSCAMMANFySQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDT 336
Cdd:cd07116 242 TLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 337 QVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGiTPKMTVYREEIFGSVLLIIPFDTEDE 416
Cdd:cd07116 321 MIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 417 AIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07116 400 ALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
60-492 |
6.26e-118 |
|
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: 353.42 E-value: 6.26e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 60 QVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLG 139
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 140 QHVPLDAS-RYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNV 218
Cdd:cd07105 81 GSIPSDKPgTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 219 IQGDAETAQD----LIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYS 294
Cdd:cd07105 161 VTHSPEDAPEvveaLIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 295 QGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDplkedTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGdrvAVH 374
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGG---LAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 375 GLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYV 454
Cdd:cd07105 312 ESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1972260679 455 N--TYNDvSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07105 392 NgmTVHD-EPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
24-492 |
4.77e-117 |
|
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: 352.97 E-value: 4.77e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAY 103
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 104 WECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPLDASRY-AYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALA 182
Cdd:cd07085 83 LITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIdTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 183 CGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIM-KACAdrNIKP 261
Cdd:cd07085 163 CGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYeRAAA--NGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 262 VTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSH 341
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 342 ISAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIA 421
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 422 NDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNtyndVSPLVP-----FGGVGESGFGREN--GTAVLEHYTHLKSV 492
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFGDLHfyGKDGVRFYTQTKTV 474
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
42-492 |
5.52e-116 |
|
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: 349.24 E-value: 5.52e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 42 IEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAywECISN--GKPIAEAKAD 119
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIA--EELTWqmGRPIAQAGGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQH-VPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVT 198
Cdd:cd07102 79 IRGMLERARYMISIAEEALADIrVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 199 ALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRnIKPVTLELGGKSALIVFDDA 278
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGR-FIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 279 DIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAI 358
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 359 AEGATKLCGGDRVAVhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLS 438
Cdd:cd07102 318 AKGARALIDGALFPE-DKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1972260679 439 RSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
32-496 |
5.57e-114 |
|
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: 346.13 E-value: 5.57e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 32 EFPSDRKFEVIEP-RSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNG 110
Cdd:cd07124 41 EVRTEEKIESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 111 KPIAEAKADVLSCVDTFYFYSGIASDLLGQ---HVPLDASRYAYTrrlPVGVVAAIGAWNYPIQTCSWKTAPALACGNAV 187
Cdd:cd07124 121 KNWAEADADVAEAIDFLEYYAREMLRLRGFpveMVPGEDNRYVYR---PLGVGAVISPWNFPLAILAGMTTAALVTGNTV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 188 IYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKACA-----DRNIKP 261
Cdd:cd07124 198 VLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDyLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgQKWLKR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 262 VTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSH 341
Cdd:cd07124 278 VIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 342 ISAEHRNKVEGYISTAIAEGaTKLCGGDRVAvhGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIA 421
Cdd:cd07124 358 IDKGARDRIRRYIEIGKSEG-RLLLGGEVLE--LAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIA 434
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972260679 422 NDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTyNDVSPLV---PFGGVGESGFG-RENGTAVLEHYTHLKSVFVNT 496
Cdd:cd07124 435 NDTEYGLTGGVFSRSPEHLERARREFEVGNLYANR-KITGALVgrqPFGGFKMSGTGsKAGGPDYLLQFMQPKTVTENF 512
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
42-494 |
4.25e-111 |
|
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: 337.01 E-value: 4.25e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 42 IEPRSGKPMATWHYATRDQVDLTVKEAKKAQK--QWAKSSWMeRSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKAD 119
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTA 199
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 200 LILAEILKSA-GLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRnIKPVTLELGGKSALIVFDD 277
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT-LKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 278 ADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTA 357
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 358 IAEGATKLCGGDRVaVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDL 437
Cdd:cd07120 320 IAAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1972260679 438 SRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
35-492 |
1.17e-109 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 335.69 E-value: 1.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 35 SDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCN---DIAYWEcisNGK 111
Cdd:PRK09407 30 AGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREellDLVQLE---TGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 112 PIAEAKADVLSCVDTFYFYSGIASDLLGQH-----VPLdASRyAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNA 186
Cdd:PRK09407 107 ARRHAFEEVLDVALTARYYARRAPKLLAPRrragaLPV-LTK-TTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 187 VIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIhhDGVSKVSFTGSIPTGKKIMKACADRNIkPVTLE 265
Cdd:PRK09407 185 VVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPgPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLI-GFSLE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 266 LGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAE 345
Cdd:PRK09407 262 LGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 346 HRNKVEGYISTAIAEGATKLCGGdrVAVHGLENGFYlSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTD 425
Cdd:PRK09407 342 QLETVSAHVDDAVAKGATVLAGG--KARPDLGPLFY-EPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTP 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972260679 426 MGLAAGLVTKDLSRSYRVSEQLNAGNVYVN-----TYNDVSplVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:PRK09407 419 YGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
40-492 |
8.35e-108 |
|
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: 328.16 E-value: 8.35e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 40 EVIEPRSGKPMATWHYATRDQVDlTVKEAKKAQKqwAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKAD 119
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALR-EALALAASYR--STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQHVPLDAS-----RYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPL 194
Cdd:cd07146 79 VGRAADVLRFAAAEALRDDGESFSCDLTangkaRKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 195 SPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIkpvTLELGGKSALI 273
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQ---LLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 274 VFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGY 353
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 354 ISTAIAEGATKLCGGDRvavhgleNGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLV 433
Cdd:cd07146 316 VEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVC 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972260679 434 TKDLSRSYRVSEQLNAGNVYVntyNDV----SPLVPFGGVGESGFG-RENGTAVLEHYTHLKSV 492
Cdd:cd07146 389 TNDLDTIKRLVERLDVGTVNV---NEVpgfrSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
42-492 |
1.11e-107 |
|
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: 328.11 E-value: 1.11e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 42 IEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCN---DIAYWECisnGKPIAEAKA 118
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDellDLIQLET---GKARRHAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQH-----VPLdASRYAYTRRlPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSP 193
Cdd:cd07101 78 EVLDVAIVARYYARRAERLLKPRrrrgaIPV-LTRTTVNRR-PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 194 LSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIhhDGVSKVSFTGSIPTGKKIMKACADRNIkPVTLELGGKSAL 272
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPgSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLI-GCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 273 IVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEG 352
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 353 YISTAIAEGATKLCGGdrVAVHGLENGFYLsPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGL 432
Cdd:cd07101 313 HVDDAVAKGATVLAGG--RARPDLGPYFYE-PTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 433 VTKDLSRSYRVSEQLNAGNVYVN-----TYNDVSplVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
25-495 |
6.55e-102 |
|
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: 313.74 E-value: 6.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEfpSDRKF-EVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAK-SSWMERSEILKKTGDLLKTHCNDIA 102
Cdd:cd07082 5 LINGEWKE--SSGKTiEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 103 ---YWEcisNGKPIAEAKADVLSCVDtfYFYSGIAS--DLLGQHVPLDASR-----YAYTRRLPVGVVAAIGAWNYPIQT 172
Cdd:cd07082 83 nllMWE---IGKTLKDALKEVDRTID--YIRDTIEElkRLDGDSLPGDWFPgtkgkIAQVRREPLGVVLAIGPFNYPLNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 173 CSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIM 251
Cdd:cd07082 158 TVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 252 KACAdrnIKPVTLELGGKSALIVFDDADIDSAVS-CAMMANFYSqGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGD 330
Cdd:cd07082 238 KQHP---MKRLVLELGGKDPAIVLPDADLELAAKeIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 331 PLKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRvavhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIP 410
Cdd:cd07082 314 PWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR------EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 411 FDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLV-PFGGVGESGFGRENGTAVLEHYTHL 489
Cdd:cd07082 388 VNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDALRSMTRR 467
|
....*.
gi 1972260679 490 KSVFVN 495
Cdd:cd07082 468 KGIVIN 473
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
25-490 |
1.90e-100 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 310.30 E-value: 1.90e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 25 FVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYW 104
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 105 ECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVP-LDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALAC 183
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 184 GNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDA-ETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdRNIKPV 262
Cdd:PRK11241 174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA-KDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 263 TLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHI 342
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 343 SAEHRNKVEGYISTAIAEGATKLCGGDrvaVHGLENGFYlSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAN 422
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGK---AHELGGNFF-QPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 423 DTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLK 490
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
43-495 |
4.19e-100 |
|
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: 308.84 E-value: 4.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 43 EPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAK-ADVL 121
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 122 ScvdtfyfysgIASDL--LGQHVP------------LDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAV 187
Cdd:cd07098 82 V----------TCEKIrwTLKHGEkalrpesrpgglLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 188 IYKPSPLSPVTAL----ILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADrNIKPVT 263
Cdd:cd07098 152 VVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAE-SLTPVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 264 LELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHIS 343
Cdd:cd07098 231 LELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 344 AEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAND 423
Cdd:cd07098 311 PARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANS 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 424 TDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNdVSPLV---PFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:cd07098 391 TEYGLGASVFGKDIKRARRIASQLETGMVAINDFG-VNYYVqqlPFGGVKGSGFGRFAGEEGLRGLCNPKSVTED 464
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
42-494 |
2.70e-98 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 303.97 E-value: 2.70e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 42 IEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVL 121
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 122 SCVDTFYFYSGIASDLLgQHVPLD-----ASRyAYTRRLPVGVVAAIGAWNYPIqtcsWKT----APALACGNAVIYKPS 192
Cdd:PRK09406 86 KCAKGFRYYAEHAEALL-ADEPADaaavgASR-AYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLLKHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 193 PLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKImKACADRNIKPVTLELGGKSAL 272
Cdd:PRK09406 160 SNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 273 IVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEG 352
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 353 YISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGL 432
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPD----GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972260679 433 VTKDLSRSYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
20-492 |
2.79e-90 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 285.29 E-value: 2.79e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 20 ELSSHF---VAGNHVEfpSDRKFEVIEPrSGKPMATWHY--ATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLL 94
Cdd:PRK03137 32 ELGQDYpliIGGERIT--TEDKIVSINP-ANKSEVVGRVskATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAII 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 95 KTHCNDIAYWECISNGKPIAEAKADVLSCVDTFYFYSGIASDLL-GQHV---PLDASRYAYTrrlPVGVVAAIGAWNYPI 170
Cdd:PRK03137 109 RRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLAdGKPVesrPGEHNRYFYI---PLGVGVVISPWNFPF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 171 QTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKK 249
Cdd:PRK03137 186 AIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSgSEVGDYLVDHPKTRFITFTGSREVGLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 250 IMKACA-----DRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQ 324
Cdd:PRK03137 266 IYERAAkvqpgQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 325 KMKIGDPlKEDTQVGSHISAEHRNKVEGYISTAIAEGATkLCGGDRvavhGLENGFYLSPCILTGITPKMTVYREEIFGS 404
Cdd:PRK03137 346 ELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEGRL-VLGGEG----DDSKGYFIQPTIFADVDPKARIMQEEIFGP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 405 VLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTyNDVSPLV---PFGGVGESGF-GRENGT 480
Cdd:PRK03137 420 VVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNR-GCTGAIVgyhPFGGFNMSGTdSKAGGP 498
|
490
....*....|..
gi 1972260679 481 AVLEHYTHLKSV 492
Cdd:PRK03137 499 DYLLLFLQAKTV 510
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
42-495 |
3.07e-89 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 280.98 E-value: 3.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 42 IEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAywECISN--GKPIAEAKAD 119
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMA--QMITRemGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 120 VLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTA 199
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 200 LILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKImKACADRNIKPVTLELGGKSALIVFDDAD 279
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAI-GAQAGAALKKCVLELGGSDPFIVLNDAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 280 IDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIA 359
Cdd:PRK13968 249 LELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 360 EGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSR 439
Cdd:PRK13968 329 EGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQ 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1972260679 440 SYRVSEQLNAGNVYVNTYNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:PRK13968 405 ARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKD 460
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
110-496 |
2.17e-88 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 277.00 E-value: 2.17e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 110 GKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPLD-ASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVI 188
Cdd:PRK10090 24 GKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDrPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 189 YKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAET-AQDLIHHDGVSKVSFTGSIPTGKKIMKAcADRNIKPVTLELG 267
Cdd:PRK10090 104 IKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETvGQELAGNPKVAMVSMTGSVSAGEKIMAA-AAKNITKVCLELG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 268 GKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDT-QVGSHISAEH 346
Cdd:PRK10090 183 GKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDiAMGPLINAAA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 347 RNKVEGYISTAIAEGATKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDM 426
Cdd:PRK10090 263 LERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDY 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972260679 427 GLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNdVSPLVPF-GGVGESGFGRENGTAVLEHYTHLKSVFVNT 496
Cdd:PRK10090 339 GLTSSIYTQNLNVAMKAIKGLKFGETYINREN-FEAMQGFhAGWRKSGIGGADGKHGLHEYLQTQVVYLQS 408
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
60-476 |
1.10e-87 |
|
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: 275.69 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 60 QVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAywECIS--NGKPIAEAKADVLSCVDTFYFYSGIASDL 137
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELA--RLISreTGKPLWEAQTEVAAMAGKIDISIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 138 LGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFN 217
Cdd:cd07095 79 TGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 218 VIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQ 297
Cdd:cd07095 159 LVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 298 VCSNASKVLVHKSVL-KEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLcggdRVAVHGL 376
Cdd:cd07095 239 RCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL----LAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 377 ENGFYLSPCILTgITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVN- 455
Cdd:cd07095 315 AGTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNr 393
|
410 420
....*....|....*....|.
gi 1972260679 456 TYNDVSPLVPFGGVGESGFGR 476
Cdd:cd07095 394 PTTGASSTAPFGGVGLSGNHR 414
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
24-492 |
2.69e-87 |
|
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: 276.38 E-value: 2.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAY 103
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 104 WECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPLDASRY-AYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALA 182
Cdd:TIGR01722 83 LITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVdVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 183 CGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKAcADRNIKPV 262
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTT-GSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 263 TLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVlKEFTKKLVDHTQKMKIGDPLKEDTQVGSHI 342
Cdd:TIGR01722 242 QALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 343 SAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAN 422
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALIN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972260679 423 DTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVS-PLVPFGGVGESGFGREN--GTAVLEHYTHLKSV 492
Cdd:TIGR01722 401 ASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPlPYFSFTGWKDSFFGDHHiyGKQGTHFYTRGKTV 473
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
39-479 |
4.45e-87 |
|
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: 275.62 E-value: 4.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 39 FEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA 118
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIASDLLGQHVPldaSRYAYTRRL----PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPL 194
Cdd:cd07130 94 EVQEMIDICDFAVGLSRQLYGLTIP---SERPGHRMMeqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 195 SPVTAL----ILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIKpVTLELGGKS 270
Cdd:cd07130 171 TPLTAIavtkIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR-SLLELGGNN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 271 ALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKV 350
Cdd:cd07130 250 AIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 351 EGYISTAIAEGATKLCGGDRVAVHglenGFYLSPCILTGiTPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAA 430
Cdd:cd07130 330 LAAIEEAKSQGGTVLFGGKVIDGP----GNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSS 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 431 GLVTKDLSRSYRVSEQLNA--GNVYVNtyndvsplVP---------FGGVGESGFGRENG 479
Cdd:cd07130 405 SIFTTDLRNAFRWLGPKGSdcGIVNVN--------IGtsgaeiggaFGGEKETGGGRESG 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
40-479 |
2.02e-80 |
|
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: 259.44 E-value: 2.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 40 EVIEP-RSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKA 118
Cdd:cd07125 49 PVIDPaDHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 119 DVLSCVDTFYFYSGIA------SDLLGQHVPLDASRYaytrrLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPS 192
Cdd:cd07125 129 EVREAIDFCRYYAAQArelfsdPELPGPTGELNGLEL-----HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 193 PLSPVTALILAEILKSAGLPDGVFNVIQGDAETA-QDLIHHDGVSKVSFTGSIPTGKKIMKACADRN--IKPVTLELGGK 269
Cdd:cd07125 204 EQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRALAERDgpILPLIAETGGK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 270 SALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNK 349
Cdd:cd07125 284 NAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 350 VEGYistaiaegaTKLCGGDRVAVH----GLENGFYLSPCI--LTGItpkmTVYREEIFGSVLLIIPFDTE--DEAIKIA 421
Cdd:cd07125 364 LRAH---------TELMRGEAWLIApaplDDGNGYFVAPGIieIVGI----FDLTTEVFGPILHVIRFKAEdlDEAIEDI 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972260679 422 NDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTyNDVSPLV---PFGGVGESGFGRENG 479
Cdd:cd07125 431 NATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-NITGAIVgrqPFGGWGLSGTGPKAG 490
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
150-494 |
1.59e-78 |
|
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: 251.68 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 150 AYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQGDAETAQDL 229
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 230 IHH--DgvsKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLV 307
Cdd:cd07087 173 LAEpfD---HIFFTGSPAVGKIVMEAAA-KHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 308 HKSVLKEFTKKLVDHTQKMkIGDPLKEDTQVGSHISAEHRNKVEGYIstaiaEGATKLCGGDRvavhgLENGFYLSPCIL 387
Cdd:cd07087 249 HESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQV-----DKEERYIAPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 388 TGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVyvnTYNDV-----SP 462
Cdd:cd07087 318 DDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV---CVNDVllhaaIP 394
|
330 340 350
....*....|....*....|....*....|..
gi 1972260679 463 LVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07087 395 NLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
40-475 |
8.32e-76 |
|
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: 245.79 E-value: 8.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 40 EVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQwaKSSWM---ERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEA 116
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLD--RNNWLpahERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 117 KADVLSCVDTFYFYSGIASDLLGQHVPLD-----ASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKP 191
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 192 SPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACAdrnikPVT---LELGG 268
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-----PGTrcaLEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 269 KSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRN 348
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 349 KVEGYISTAIAEGATKLCGGDRvavhgLENGFYlSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGL 428
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKR-----LSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1972260679 429 AAGLVTKDLSRSYRVSEQLNAGNVYVntyNDVSPL----VPFGGVGESGFG 475
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMV---NDHTAFrvdwMPFAGRRQSGYG 436
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
150-492 |
4.20e-70 |
|
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: 230.47 E-value: 4.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 150 AYTRRLPVGVVAAIGAWNYPIQTCswkTAP---ALACGNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQGDAETA 226
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 227 QDLIHHDgVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVL 306
Cdd:cd07136 170 QELLDQK-FDYIFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 307 VHKSVLKEFTKKLVDHTQKMKIGDPLKEDTqVGSHISAEHRNKVEGYIstaiaEGATKLCGGDrvavhGLENGFYLSPCI 386
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFYGEDPLESPD-YGRIINEKHFDRLAGLL-----DNGKIVFGGN-----TDRETLYIEPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 387 LTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVntyND-----VS 461
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCI---NDtimhlAN 393
|
330 340 350
....*....|....*....|....*....|.
gi 1972260679 462 PLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:cd07136 394 PYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
156-494 |
1.27e-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: 229.04 E-value: 1.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 156 PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFnVIQGDAETAQDLI----- 230
Cdd:cd07134 100 PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEGDAEVAQALLelpfd 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 231 HhdgvskVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKS 310
Cdd:cd07134 179 H------IFFTGSPAVGKIVMAAAA-KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 311 VLKEFTKKLVDHTQKMKIGDPLKEDT-QVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAvhgleNGFYLSPCILTG 389
Cdd:cd07134 252 VKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDA-----AQRYIAPTVLTN 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 390 ITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNT--YNDVSPLVPFG 467
Cdd:cd07134 327 VTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDvvLHFLNPNLPFG 406
|
330 340
....*....|....*....|....*..
gi 1972260679 468 GVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07134 407 GVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
26-479 |
2.19e-69 |
|
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: 230.16 E-value: 2.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 26 VAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWE 105
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 106 CISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHvPLDASRYAYTRRL---PVGVVAAIGAWNYPIQTCSWKTAPALA 182
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPA-VEVVPYPGEDNESfyvGLGAGVVISPWNFPVAIFTGMIVAPVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 183 CGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFTGSIPTGKKIMKACADR---- 257
Cdd:cd07083 181 VGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAyLTEHERIRGINFTGSLETGKKIYEAAARLapgq 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 258 -NIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDT 336
Cdd:cd07083 261 tWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 337 QVGSHISAEHRNKVEGYISTAIAEGaTKLCGGDRVAvhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTED- 415
Cdd:cd07083 341 DLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE----GEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDf 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 416 -EAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTyNDVSPLV---PFGGVGESGFGRENG 479
Cdd:cd07083 416 aEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINR-KITGALVgvqPFGGFKLSGTNAKTG 482
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-473 |
4.42e-69 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 229.07 E-value: 4.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 22 SSHFVAGNHVEFPSDRkFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDI 101
Cdd:PRK09457 1 MTLWINGDWIAGQGEA-FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 102 AywECIS--NGKPIAEAKADVLSCVDTfyfysgIASDLLGQHV-------PLDASRyAYTRRLPVGVVAAIGAWNYPIQT 172
Cdd:PRK09457 80 A--EVIAreTGKPLWEAATEVTAMINK------IAISIQAYHErtgekrsEMADGA-AVLRHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 173 CSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMK 252
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 253 ACADRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVL-KEFTKKLVDHTQKMKIGDP 331
Cdd:PRK09457 231 QFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 332 lKEDTQ--VGSHISAEHRNKVEGYISTAIAEGATKLcggdrVAVHGLENGF-YLSPCILTgITPKMTVYREEIFGSVLLI 408
Cdd:PRK09457 311 -DAEPQpfMGAVISEQAAQGLVAAQAQLLALGGKSL-----LEMTQLQAGTgLLTPGIID-VTGVAELPDEEYFGPLLQV 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972260679 409 IPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNT-YNDVSPLVPFGGVGESG 473
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKpLTGASSAAPFGGVGASG 449
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
150-494 |
7.13e-68 |
|
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: 224.29 E-value: 7.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 150 AYTRRLPVGVVAAIGAWNYPIQTCswkTAP---ALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVfNVIQGDAETA 226
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVVTGGADVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 227 QD--------LIhhdgvskvsFTGSIPTGKKIMKACADrNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQV 298
Cdd:cd07133 171 AAfsslpfdhLL---------FTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 299 CSNASKVLVHKSVLKEFTKKLVDHTQKMkIGDpLKEDTQVGSHISAEHRNKVEGYISTAIAEGATklcggdRVAVHG--- 375
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPT-LADNPDYTSIINERHYARLQGLLEDARAKGAR------VIELNPage 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 376 -LENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVyv 454
Cdd:cd07133 313 dFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGV-- 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1972260679 455 nTYNDV-----SPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07133 391 -TINDTllhvaQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
35-495 |
1.45e-66 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 222.71 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 35 SDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAywECISN--GKP 112
Cdd:PLN00412 29 SGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA--ECLVKeiAKP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 113 IAEAKADVLSCVDTFYFYSGIASDLLGQHVPL--------DASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACG 184
Cdd:PLN00412 107 AKDAVTEVVRSGDLISYTAEEGVRILGEGKFLvsdsfpgnERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 185 NAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSiPTGKKIMKACAdrnIKPVT 263
Cdd:PLN00412 187 NAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAG---MVPLQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 264 LELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPlKEDTQVGSHIS 343
Cdd:PLN00412 263 MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 344 AEHRNKVEGYISTAIAEGATkLCGGDRvavhglENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAND 423
Cdd:PLN00412 342 ESSANFIEGLVMDAKEKGAT-FCQEWK------REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972260679 424 TDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSP-LVPFGGVGESGFGRENGTAVLEHYTHLKSVFVN 495
Cdd:PLN00412 415 SNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSINMMTKVKSTVIN 487
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-492 |
2.57e-64 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 219.23 E-value: 2.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 24 HFVAGNHVEFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAY 103
Cdd:PLN02419 116 NLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 104 WECISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVP-LDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALA 182
Cdd:PLN02419 196 NITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 183 CGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNiKPV 262
Cdd:PLN02419 276 CGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG-KRI 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 263 TLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVlVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHI 342
Cdd:PLN02419 355 QSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 343 SAEHRNKVEGYISTAIAEGATKLCGGDRVAVHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIAN 422
Cdd:PLN02419 434 SKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIIN 513
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972260679 423 DTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVS-PLVPFGGVGESGFGREN--GTAVLEHYTHLKSV 492
Cdd:PLN02419 514 KNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPlPFFSFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
151-493 |
5.40e-63 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 212.97 E-value: 5.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 151 YTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQGDAETAQDLI 230
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 231 HHDgVSKVSFTGSIPTGKKIMKAcADRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKS 310
Cdd:PTZ00381 183 KEP-FDHIFFTGSPRVGKLVMQA-AAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 311 VLKEFTKKLVDHTQKMkIGDPLKEDTQVGSHISAEHRNKVEGYISTAiaegatklcgGDRVAVHGL--ENGFYLSPCILT 388
Cdd:PTZ00381 261 IKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDH----------GGKVVYGGEvdIENKYVAPTIIV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 389 GITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVntyNDV-----SPL 463
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVI---NDCvfhllNPN 406
|
330 340 350
....*....|....*....|....*....|
gi 1972260679 464 VPFGGVGESGFGRENGTAVLEHYTHLKSVF 493
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
150-493 |
1.43e-61 |
|
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: 207.84 E-value: 1.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 150 AYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQGDAETAQDL 229
Cdd:cd07135 102 PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 230 IHHdGVSKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHK 309
Cdd:cd07135 181 LEQ-KFDKIFYTGSGRVGRIIAEAAA-KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 310 SVLKEFTKKLVDHTQKMKIGDPlKEDTQVGSHISAEHRNKVEGYISTAiaegatklcGGDRVAVHGLENG-FYLSPCILT 388
Cdd:cd07135 259 SVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTT---------KGKVVIGGEMDEAtRFIPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 389 GITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVyvnTYNDV-----SPL 463
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGV---VINDTlihvgVDN 405
|
330 340 350
....*....|....*....|....*....|
gi 1972260679 464 VPFGGVGESGFGRENGTAVLEHYTHLKSVF 493
Cdd:cd07135 406 APFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
150-494 |
3.86e-60 |
|
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: 203.99 E-value: 3.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 150 AYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDgVFNVIQGDAETAQDL 229
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKE-CYPVVLGGVEETTEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 230 IHH--DgvsKVSFTGSIPTGKKIMKAcADRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLV 307
Cdd:cd07132 173 LKQrfD---YIFYTGSTSVGKIVMQA-AAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 308 HKSVLKEFTKKLVDHTQKMkIGDPLKEDTQVGSHISAEHRNKVEGYIStaiaegatklcgGDRVAVHGL--ENGFYLSPC 385
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLS------------GGKVAIGGQtdEKERYIAPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 386 ILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVntyNDV----- 460
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCV---NDTimhyt 392
|
330 340 350
....*....|....*....|....*....|....
gi 1972260679 461 SPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07132 393 LDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLV 426
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
42-497 |
1.84e-59 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 204.30 E-value: 1.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 42 IEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVL 121
Cdd:PLN02315 39 VNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 122 SCVDTFYFYSGIASDLLGQHVPLDASRYAYTRRL-PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTAL 200
Cdd:PLN02315 119 EIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 201 ----ILAEILKSAGLPDGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIKPVtLELGGKSALIVFD 276
Cdd:PLN02315 199 amtkLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCL-LELSGNNAIIVMD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 277 DADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYIST 356
Cdd:PLN02315 278 DADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 357 AIAEGATKLCGGDRVAvhglENGFYLSPCILTgITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKD 436
Cdd:PLN02315 358 IKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972260679 437 LSRSYRVSEQL--NAGNVYVNT-YNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVFVNTG 497
Cdd:PLN02315 433 PETIFKWIGPLgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYG 496
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
15-473 |
1.48e-53 |
|
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: 188.56 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 15 ETKLLELSSH------FVAGNHVeFPSDRKFEVIEPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILK 88
Cdd:cd07123 20 QEALAELKSLtveiplVIGGKEV-RTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 89 KTGDLLKTHCN-DIAYWECISNGKPIAEAKADVlSC--VDTFYFYSGIASDLLGQHvPLDASRYAYTR---RLPVGVVAA 162
Cdd:cd07123 99 KAADLLSGKYRyELNAATMLGQGKNVWQAEIDA-ACelIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRleyRPLEGFVYA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 163 IGAWNYPIQTCSWKTAPALAcGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGDAETAQD-LIHHDGVSKVSFT 241
Cdd:cd07123 177 VSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDtVLASPHLAGLHFT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 242 GSIPTGKKIMKACAD-----RNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFT 316
Cdd:cd07123 256 GSTPTFKSLWKQIGEnldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 317 KKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAE-GATKLCGG---DRVavhglenGFYLSPCILTGITP 392
Cdd:cd07123 336 ERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGkcdDSV-------GYFVEPTVIETTDP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 393 KMTVYREEIFGSVLLIIPFDTED--EAIKIANDT-DMGLAAGLVTKDLSRSYRVSEQLN--AGNVYVntyNDVS--PLV- 464
Cdd:cd07123 409 KHKLMTEEIFGPVLTVYVYPDSDfeETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYI---NDKPtgAVVg 485
|
490
....*....|.
gi 1972260679 465 --PFGGVGESG 473
Cdd:cd07123 486 qqPFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
27-475 |
7.44e-49 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 180.78 E-value: 7.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 27 AGNHVEFPSDRKFEVieprsgkpmATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWEC 106
Cdd:PRK11904 562 EARPVVSPADRRRVV---------GEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCV 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 107 ISNGKPIAEAKADVLSCVDTFYFYSGIASDLLGQHVPL-----DASRYAYTRRlpvGVVAAIGAWNYPI-----QTcswk 176
Cdd:PRK11904 633 REAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLpgptgESNELRLHGR---GVFVCISPWNFPLaiflgQV---- 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 177 tAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGVFNVIQGD-AETAQDLIHHDGVSKVSFTGSIPTGKKIMKACA 255
Cdd:PRK11904 706 -AAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDgATVGAALTADPRIAGVAFTGSTETARIINRTLA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 256 DRNIKPVTL--ELGGKSALI---------VFDDAdIDSAvscammanFYSQGQVCSnASKVL-VHKSVlkeftkklVDHT 323
Cdd:PRK11904 785 ARDGPIVPLiaETGGQNAMIvdstalpeqVVDDV-VTSA--------FRSAGQRCS-ALRVLfVQEDI--------ADRV 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 324 QKM--------KIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEgATKLCGGDRVAvhGLENGFYLSPCI--LTGItpk 393
Cdd:PRK11904 847 IEMlkgamaelKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPA--GTENGHFVAPTAfeIDSI--- 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 394 mTVYREEIFGSVLLIIPFDTED-----EAIkiaNDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTyNDVSPLV---P 465
Cdd:PRK11904 921 -SQLEREVFGPILHVIRYKASDldkviDAI---NATGYGLTLGIHSRIEETADRIADRVRVGNVYVNR-NQIGAVVgvqP 995
|
490
....*....|
gi 1972260679 466 FGGVGESGFG 475
Cdd:PRK11904 996 FGGQGLSGTG 1005
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
52-475 |
3.02e-47 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 176.28 E-value: 3.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 52 TWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTH-------CNDIAywecisnGKPIAEAKADVLSCV 124
Cdd:COG4230 586 TVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHraelmalLVREA-------GKTLPDAIAEVREAV 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 125 DTFYFYSGIASDLLGQHvpldasryayTRRLPVGVVAAIGAWNYPI-----QTcswktAPALACGNAVIYKPSPLSPVTA 199
Cdd:COG4230 659 DFCRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLaiftgQV-----AAALAAGNTVLAKPAEQTPLIA 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 200 LILAEILKSAGLPDGVFNVIQGDAET--AQdLIHHDGVSKVSFTGSIPTGKKIMKACADRNIKPVTL--ELGGKSALIVf 275
Cdd:COG4230 724 ARAVRLLHEAGVPADVLQLLPGDGETvgAA-LVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLiaETGGQNAMIV- 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 276 ddadiDS------AVSCAMMANFYSQGQVCSnASKVL-VHKSVLkeftkklvDHTQKM--------KIGDPLKEDTQVGS 340
Cdd:COG4230 802 -----DSsalpeqVVDDVLASAFDSAGQRCS-ALRVLcVQEDIA--------DRVLEMlkgamaelRVGDPADLSTDVGP 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 341 HISAEHRNKVEGYISTAIAEGatKLCGgdRVAV-HGLENGFYLSPCI--LTGItpkmTVYREEIFGSVLLIIPFDTED-- 415
Cdd:COG4230 868 VIDAEARANLEAHIERMRAEG--RLVH--QLPLpEECANGTFVAPTLieIDSI----SDLEREVFGPVLHVVRYKADEld 939
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972260679 416 ---EAIkiaNDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTyNDVSPLV---PFGGVGESGFG 475
Cdd:COG4230 940 kviDAI---NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR-NIIGAVVgvqPFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
55-475 |
3.78e-47 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 175.82 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 55 YATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVLSCVDTFYFYSGIA 134
Cdd:PRK11905 586 EASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQA 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 135 SDLLGQhvpldasryayTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDG 214
Cdd:PRK11905 666 RRLLNG-----------PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKD 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 215 VFNVIQGDAET--AQdLIHHDGVSKVSFTGSIPTGKKIMKACADRNIKPVTL--ELGGKSALIVfddadiDS------AV 284
Cdd:PRK11905 735 ALQLLPGDGRTvgAA-LVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIV------DSsalpeqVV 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 285 SCAMMANFYSQGQVCSnASKVL-VHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEGAt 363
Cdd:PRK11905 808 ADVIASAFDSAGQRCS-ALRVLcLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGR- 885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 364 klcggdRVAVHGL----ENGFYLSPCILTgiTPKMTVYREEIFGSVLLIIPFDTE--DEAIKIANDTDMGLAAGLVTKDL 437
Cdd:PRK11905 886 ------LVHQLPLpaetEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADelDRVIDDINATGYGLTFGLHSRID 957
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1972260679 438 SRSYRVSEQLNAGNVYVNTyNDVSPLV---PFGGVGESGFG 475
Cdd:PRK11905 958 ETIAHVTSRIRAGNIYVNR-NIIGAVVgvqPFGGEGLSGTG 997
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
156-494 |
1.97e-46 |
|
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: 167.20 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 156 PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILkSAGLPDGVFNVIQGDAETAQDLIHHDGv 235
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEGGVPETTALLEQKW- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 236 SKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYS-QGQVCSNASKVLVHKSVLKE 314
Cdd:cd07137 179 DKIFFTGSPRVGRIIMAAAA-KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESFAPT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 315 FTKKLVDHTQKMkIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEgATKLCGGDRVavhglENGFYLSPCILTGITPKM 394
Cdd:cd07137 258 LIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERD-----EKNLYIEPTILLDPPLDS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 395 TVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVyvnTYNDV-----SPLVPFGGV 469
Cdd:cd07137 331 SIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV---TFNDTvvqyaIDTLPFGGV 407
|
330 340
....*....|....*....|....*
gi 1972260679 470 GESGFGRENGTAVLEHYTHLKSVFV 494
Cdd:cd07137 408 GESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
31-479 |
1.49e-44 |
|
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: 163.54 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 31 VEFPSDRKFEVieprsgkpmATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNG 110
Cdd:TIGR01238 55 VTNPADRRDIV---------GQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 111 KPIAEAKADVLSCVDTFYFYSGIASDLLGQhvplDASRyaytrrlPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYK 190
Cdd:TIGR01238 126 KTIHNAIAEVREAVDFCRYYAKQVRDVLGE----FSVE-------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 191 PSPLSPVTALILAEILKSAGLPDGVFNVIQGDAET-AQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNIKPVTL--ELG 267
Cdd:TIGR01238 195 PAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADvGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 268 GKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHR 347
Cdd:TIGR01238 275 GQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 348 NKVEGYIStAIAEGATKLCGGDRVAVHGLENGFYLSPCILTgiTPKMTVYREEIFGSVLLIIPF--DTEDEAIKIANDTD 425
Cdd:TIGR01238 355 QNLLAHIE-HMSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYkaRELDQIVDQINQTG 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1972260679 426 MGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTyNDVSPLV---PFGGVGESGFGRENG 479
Cdd:TIGR01238 432 YGLTMGVHSRIETTYRWIEKHARVGNCYVNR-NQVGAVVgvqPFGGQGLSGTGPKAG 487
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
156-493 |
1.81e-39 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 149.49 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 156 PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILkSAGLPDGVFNVIQGDAETAQDLIHHDGv 235
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEGGPAVGEQLLQHKW- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 236 SKVSFTGSIPTGKKIMKACAdRNIKPVTLELGGKSALIV--FDDA-DIDSAVSCAMMANFYS-QGQVCSNASKVLVHK-- 309
Cdd:PLN02203 186 DKIFFTGSPRVGRIIMTAAA-KHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYVLVEErf 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 310 -SVLKEFTKKlvdhTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTaiaegatklcggDRVA---VHG---LENGFYL 382
Cdd:PLN02203 265 aPILIELLKS----TIKKFFGENPRESKSMARILNKKHFQRLSNLLKD------------PRVAasiVHGgsiDEKKLFI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 383 SPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVyvnTYND--- 459
Cdd:PLN02203 329 EPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDaii 405
|
330 340 350
....*....|....*....|....*....|....*.
gi 1972260679 460 --VSPLVPFGGVGESGFGRENGTAVLEHYTHLKSVF 493
Cdd:PLN02203 406 qyACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
56-475 |
1.24e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 138.57 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 56 ATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKADVLSCVDTFYFYSGIAS 135
Cdd:PRK11809 679 ATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 136 DLLGQhvplDASRyaytrrlPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLPDGV 215
Cdd:PRK11809 759 DDFDN----DTHR-------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGV 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 216 FNVIQGDAET--AQdLIHHDGVSKVSFTGSIPTGKKIMKACADR---NIKPVTL--ELGGKSALIVFDDADIDSAVSCAM 288
Cdd:PRK11809 828 VQLLPGRGETvgAA-LVADARVRGVMFTGSTEVARLLQRNLAGRldpQGRPIPLiaETGGQNAMIVDSSALTEQVVADVL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 289 MANFYSQGQVCSnASKVLvhksVLKEftkKLVDHTQKM--------KIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAE 360
Cdd:PRK11809 907 ASAFDSAGQRCS-ALRVL----CLQD---DVADRTLKMlrgamaecRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAK 978
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 361 GATkLCGGDRVAVHGLENGFYLSPCI--LTGITPkmtvYREEIFGSVLLIIPFDTE--DEAIKIANDTDMGLAAGLVTKD 436
Cdd:PRK11809 979 GRP-VFQAARENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRNqlDELIEQINASGYGLTLGVHTRI 1053
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1972260679 437 LSRSYRVSEQLNAGNVYVNTyNDVSPLV---PFGGVGESGFG 475
Cdd:PRK11809 1054 DETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1094
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
156-493 |
3.48e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 125.93 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 156 PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAgLPDGVFNVIQGDAETAQDLIHHDGv 235
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQKW- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 236 SKVSFTGSIPTGKKIMKACADRnIKPVTLELGGKSALIVFDDADIDSAVSCAMMANF-YSQGQVCSNASKVLvhksVLKE 314
Cdd:PLN02174 190 DKIFYTGSSKIGRVIMAAAAKH-LTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYIL----TTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 315 FTKKLVD----HTQKMKIGDPLkEDTQVGSHISAEHRNKV-----EGYISTAIAEGATKlcggDRvavhglENgFYLSPC 385
Cdd:PLN02174 265 YAPKVIDamkkELETFYGKNPM-ESKDMSRIVNSTHFDRLsklldEKEVSDKIVYGGEK----DR------EN-LKIAPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 386 ILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLNAGNVYVNTYNDVSPL-- 463
Cdd:PLN02174 333 ILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALht 412
|
330 340 350
....*....|....*....|....*....|
gi 1972260679 464 VPFGGVGESGFGRENGTAVLEHYTHLKSVF 493
Cdd:PLN02174 413 LPFGGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-436 |
1.11e-30 |
|
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: 124.69 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 21 LSShFVAGNHVEfPSDRKFEVIEPRSGKPMATWHYATRDqvdltVKEA-----KKAQKQWAKSSWMERSEILKKTGDLL- 94
Cdd:cd07128 1 LQS-YVAGQWHA-GTGDGRTLHDAVTGEVVARVSSEGLD-----FAAAvayarEKGGPALRALTFHERAAMLKALAKYLm 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 95 --KTHCNDIAYWecisNGKPIAEAKADVLSCVDTFYFYSGIASDLL-GQHVPLDASRYAYTRR---------LPVGVVAA 162
Cdd:cd07128 74 erKEDLYALSAA----TGATRRDSWIDIDGGIGTLFAYASLGRRELpNAHFLVEGDVEPLSKDgtfvgqhilTPRRGVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 163 -IGAWNYPIqtcsW----KTAPALACGNAVIYKP-SPLSPVTALILAEILKSAGLPDGVFNVIQGDAetaQDLIHH-DGV 235
Cdd:cd07128 150 hINAFNFPV----WgmleKFAPALLAGVPVIVKPaTATAYLTEAVVKDIVESGLLPEGALQLICGSV---GDLLDHlGEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 236 SKVSFTGSIPTGKKIMK--ACADRNIkPVTLELGGKSALIVFDDADIDSA--------VSCAMMANfysQGQVCSNASKV 305
Cdd:cd07128 223 DVVAFTGSAATAAKLRAhpNIVARSI-RFNAEADSLNAAILGPDATPGTPefdlfvkeVAREMTVK---AGQKCTAIRRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 306 LVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRVAVHG--LENGFYLS 383
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGadAEKGAFFP 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1972260679 384 PCILTGITPKMT--VYREEIFGSVLLIIPFDTEDEAIKIANdtdMG---LAAGLVTKD 436
Cdd:cd07128 379 PTLLLCDDPDAAtaVHDVEAFGPVATLMPYDSLAEAIELAA---RGrgsLVASVVTND 433
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
68-477 |
7.50e-29 |
|
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: 118.49 E-value: 7.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 68 AKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAkadVLSCVDTFYF-------YSGIASDLLGQ 140
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA---ENICGDQVQLrarafviYSYRIPHEPGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 141 HVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAG-LPDGVFNVI 219
Cdd:cd07084 85 HLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 220 QGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMkacADRNIKPVTLELGGKSALIVFDDADIDSAV--SCAMMANFYSqGQ 297
Cdd:cd07084 165 NGDGKTMQALLLHPNPKMVLFTGSSRVAEKLA---LDAKQARIYLELAGFNWKVLGPDAQAVDYVawQCVQDMTACS-GQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 298 VCSNASKVLVHKSVLKEftkKLVDHTQKMkigdpLKEDTQVGSHISAEHRNKVEGYISTAIAEGATKLCGGDRvAVHGLE 377
Cdd:cd07084 241 KCTAQSMLFVPENWSKT---PLVEKLKAL-----LARRKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFSGK-ELKNHS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 378 NGFYLSPCILTG-------ITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDM--GLAAGLVTKDLSRSYRVSEQL- 447
Cdd:cd07084 312 IPSIYGACVASAlfvpideILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMhgSLTAAIYSNDPIFLQELIGNLw 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1972260679 448 ----------NAGNVYVNTYNDVSPlvPFGGVGESGFGRE 477
Cdd:cd07084 392 vagrtyailrGRTGVAPNQNHGGGP--AADPRGAGIGGPE 429
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
153-422 |
2.20e-23 |
|
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: 102.62 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 153 RRLPVGVVAAIGAWNYP--IQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEI----LKSAGLPDGVFNVIQG-DAET 225
Cdd:cd07129 102 MLVPLGPVAVFGASNFPlaFSVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGVFSLLQGgGREV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 226 AQDLIHHDGVSKVSFTGSIPTGKKIMKACADRNI-KPVTLELGGKSALIVFDDA------DI--DSAVSCAMMAnfysqG 296
Cdd:cd07129 182 GVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFILPGAlaergeAIaqGFVGSLTLGA-----G 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 297 QVCSNASKVLVHKSV-LKEFTKKLVDHTQKMKIGDPLkedtqvgshisaeHRNKVEGYIS--TAIAEGAtklcgGDRVAV 373
Cdd:cd07129 257 QFCTNPGLVLVPAGPaGDAFIAALAEALAAAPAQTML-------------TPGIAEAYRQgvEALAAAP-----GVRVLA 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1972260679 374 HG--LENGFYLSPCIL-----TGITPkmTVYREEIFGSVLLIIPFDTEDEAIKIAN 422
Cdd:cd07129 319 GGaaAEGGNQAAPTLFkvdaaAFLAD--PALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
79-492 |
1.62e-20 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 94.39 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 79 SWMERSEILkktGDLLKT-HCNDIAYWE-CISNGKPIA-EAKADVLSCVDTFYFYSGIASDLLGQHVPLDASRYAYTRR- 154
Cdd:PRK11903 61 TYAQRAALL---AAIVKVlQANRDAYYDiATANSGTTRnDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDp 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 155 --------LPV-GVVAAIGAWNYPiqtcSW----KTAPALACGNAVIYKP-SPLSPVTALILAEILKSAGLPDGVFNVIQ 220
Cdd:PRK11903 138 afqgqhvlVPTrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPaTATAWLTQRMVKDVVAAGILPAGALSVVC 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 221 GdaeTAQDLIHH-DGVSKVSFTGSIPTGKKI--MKACADRNIKpVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQ-- 295
Cdd:PRK11903 214 G---SSAGLLDHlQPFDVVSFTGSAETAAVLrsHPAVVQRSVR-VNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREmt 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 296 ---GQVCSNASKVLVHKSVLKEFTKKLVDHTQKMKIGDPLKEDTQVGSHISAEHRNKVEGYIStAIAEGATKLCGGDRVA 372
Cdd:PRK11903 290 vksGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 373 VHGLEN--GFYLSPCILTGITPK--MTVYREEIFGSVLLIIPFDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLN 448
Cdd:PRK11903 369 LVDADPavAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELA 448
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 449 A--GNVYVNT---------YNDVSPLVPFGGVGESGFGRENGTAVLEHYTHLKSV 492
Cdd:PRK11903 449 DshGRVHVISpdvaalhtgHGNVMPQSLHGGPGRAGGGEELGGLRALAFYHRRSA 503
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
68-322 |
5.35e-17 |
|
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: 82.66 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 68 AKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKAD---VLSCVDTfYFYSGI-------ASDL 137
Cdd:cd07077 3 AKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANwiaMMGCSES-KLYKNIdtergitASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 138 LGQHVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSwKTAPALACGNAVIYKPSPLSPVTALILA----EILKSAGLPD 213
Cdd:cd07077 82 HIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALAllfqAADAAHGPKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 214 GVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKIMKACadrNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFY 293
Cdd:cd07077 161 LVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS---PHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFF 237
|
250 260
....*....|....*....|....*....
gi 1972260679 294 SQgQVCSNASKVLVHKSVLKEFTKKLVDH 322
Cdd:cd07077 238 DQ-NACASEQNLYVVDDVLDPLYEEFKLK 265
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
61-449 |
5.03e-15 |
|
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: 76.92 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 61 VDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKAdVLSCVDTFYFYSGIASDLLGQ 140
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKV-IKNHFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 141 HVPLDASRYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSP-----VTALILAEILKSAGLPDGV 215
Cdd:cd07081 80 VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKkvtqrAATLLLQAAVAAGAPENLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 216 FNVIQGDAETAQDLIHHDGVSKVSFTGsiptGKKIMKAcADRNIKPVTLELGGKSALIVFDDADIDSAVSCAMMANFYSQ 295
Cdd:cd07081 160 GWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 296 GQVCSNASKVLVHKSVLKEFTKKLVDH-------TQKMKIGDPLKEDTQVGSHISAEHRNKVEGYISTAIAEgATKLCGG 368
Cdd:cd07081 235 GVICASEQSVIVVDSVYDEVMRLFEGQgaykltaEELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQ-ETRILIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 369 DRVAVHGLEngfylsPCILTGITPKMTVYREEIFGsvlliipfDTEDEAIKIANDTDMGLAAGLVTKDLSRSYRVSEQLN 448
Cdd:cd07081 314 EVTSLAEHE------PFAHEKLSPVLAMYRAANFA--------DADAKALALKLEGGCGHTSAMYSDNIKAIENMNQFAN 379
|
.
gi 1972260679 449 A 449
Cdd:cd07081 380 A 380
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
156-455 |
8.28e-10 |
|
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: 60.96 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 156 PVGVVAAIGAWNYPiqtcSWKTAPA----LACGNAVIYKPSPLS--PV--TALILAEILKSAGL-PDGVFNVIQG-DAET 225
Cdd:cd07127 193 PRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPHPAAilPLaiTVQVAREVLAEAGFdPNLVTLAADTpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 226 AQDLIHHDGVSKVSFTGSIPTGKKIMKACADrniKPVTLELGGKSALIVfdDADIDSAVSCAMMA---NFYSqGQVCSNA 302
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVNTVVV--DSTDDLKAMLRNLAfslSLYS-GQMCTTP 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 303 SKVLV----------HKSvLKEFTKKLVDHTQKMkIGDPLKEDTQVGSHISAEHRNKVEgyistAIAEGATKLCGGDRVA 372
Cdd:cd07127 343 QNIYVprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIA-----EARQLGEVLLASEAVA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 373 VHGLENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDEAIKIANDTDM---GLAAGLVTKDLSRSYRVSE---- 445
Cdd:cd07127 416 HPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTDPEVVERVQEaald 495
|
330
....*....|....*.
gi 1972260679 446 -----QLN-AGNVYVN 455
Cdd:cd07127 496 agvalSINlTGGVFVN 511
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
156-322 |
1.80e-09 |
|
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: 59.81 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 156 PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSA----GLPDGVFNVIQG-DAETAQDLI 230
Cdd:cd07122 95 PVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEpSIELTQELM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 231 HHDGVSKVSFTGsiptGKKIMKAcADRNIKPVtleLG---GKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLV 307
Cdd:cd07122 175 KHPDVDLILATG----GPGMVKA-AYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIV 246
|
170
....*....|....*
gi 1972260679 308 HKSVLKEFTKKLVDH 322
Cdd:cd07122 247 DDEIYDEVRAELKRR 261
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
61-283 |
2.33e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 53.01 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 61 VDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKadVLSCVDTFYFYSGIaSDLLGQ 140
Cdd:cd07121 6 VDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDK--IAKNHLAAEKTPGT-EDLTTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 141 HVPLDASrYAYTRRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTAL----ILAEILKSAGLPDGVF 216
Cdd:cd07121 83 AWSGDNG-LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAyaveLINKAIAEAGGPDNLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972260679 217 NVIQG-DAETAQDLIHHDGVSKVSFTG-------SIPTGKKIMKACAdrnikpvtlelgGKSALIVFDDADIDSA 283
Cdd:cd07121 162 VTVEEpTIETTNELMAHPDINLLVVTGgpavvkaALSSGKKAIGAGA------------GNPPVVVDETADIEKA 224
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
156-322 |
6.50e-07 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 52.11 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 156 PVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSP----LSPVTALILAEILKSAGLPDGVFNVI-QGDAETAQDLI 230
Cdd:PRK13805 108 PVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPraqkSSIAAAKIVLDAAVAAGAPKDIIQWIeEPSVELTNALM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 231 HHDGVSKVSFTGsiptGKKIMKAcADRNIKPVtleLG---GKSALIVFDDADIDSAVSCAMMANFYSQGQVCSNASKVLV 307
Cdd:PRK13805 188 NHPGIALILATG----GPGMVKA-AYSSGKPA---LGvgaGNVPAYIDKTADIKRAVNDILLSKTFDNGMICASEQAVIV 259
|
170
....*....|....*
gi 1972260679 308 HKSVLKEFTKKLVDH 322
Cdd:PRK13805 260 DDEIYDEVKEEFASH 274
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
43-283 |
2.62e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 43.35 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 43 EPRSGKPMATWHYATRDQVDLTVKEAKKAQKQWAKSSWMERSEILKKTGDLLKTHCNDIAYWECISNGKPIAEAKadvls 122
Cdd:PRK15398 20 SQTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDK----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 123 cvdtfyfysgIASDLL-GQHVP----LDASryAYT--------RRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIY 189
Cdd:PRK15398 95 ----------IAKNVAaAEKTPgvedLTTE--ALTgdngltliEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 190 KPSPLSPVTAL----ILAEILKSAGLPDGVFNVI-QGDAETAQDLIHHDGVSKVSFTG-------SIPTGKKIMKACAdr 257
Cdd:PRK15398 163 SPHPGAKKVSLraieLLNEAIVAAGGPENLVVTVaEPTIETAQRLMKHPGIALLVVTGgpavvkaAMKSGKKAIGAGA-- 240
|
250 260
....*....|....*....|....*.
gi 1972260679 258 nikpvtlelgGKSALIVFDDADIDSA 283
Cdd:PRK15398 241 ----------GNPPVVVDETADIEKA 256
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
133-443 |
4.46e-04 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 42.87 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 133 IASDLLGQHvpldASRYaytrRLPVGVVAAIGAWNYPIQTCSWKTAPALACGNAVIYKPSPLSPVTALILAEILKSAGLP 212
Cdd:cd07126 127 VPGDHQGQQ----SSGY----RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 213 DGVFNVIQGDAETAQDLIHHDGVSKVSFTGSIPTGKKImkaCADRNIKpVTLELGGKSALIVFDD-ADID-SAVSCAMMA 290
Cdd:cd07126 199 ATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERL---ALELHGK-VKLEDAGFDWKILGPDvSDVDyVAWQCDQDA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 291 NFYSqGQVCSNASKVLVHK--------SVLKEFT--KKLVDHTqkmkIGDPLKEDTQVgshiSAEHRNKVEGYISTAIAE 360
Cdd:cd07126 275 YACS-GQKCSAQSILFAHEnwvqagilDKLKALAeqRKLEDLT----IGPVLTWTTER----ILDHVDKLLAIPGAKVLF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972260679 361 GATKLCGGDRVAVHG-LENGFYLSPCILTGITPKMTVYREEIFGSVLLIIPFDTEDE--AIKIANDTDMGLAAGLVTKDL 437
Cdd:cd07126 346 GGKPLTNHSIPSIYGaYEPTAVFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDI 425
|
....*.
gi 1972260679 438 SRSYRV 443
Cdd:cd07126 426 RFLQEV 431
|
|
| |
