|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-485 |
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: 810.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 27 SYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTMD 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 107 IPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVT 186
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 187 AWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 266
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 267 NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAH 346
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 347 AEGAKILCGEGVDQLSlplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSK 426
Cdd:cd07093 320 AEGATILTGGGRPELP---DLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229277487 427 DVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
10-487 |
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: 643.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 10 LENFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEEL 87
Cdd:COG1012 6 YPLFIGGEWVAAASgeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 88 AQAESKDQGKTLTLARtMDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAP 167
Cdd:COG1012 86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 168 AIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHC 247
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 248 KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMG 327
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 328 ALISKAHLEKVRSYVTKAHAEGAKILCGeGVdqlslPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 407
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTG-GR-----RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 408 VIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 1229277487 487 Y 487
Cdd:COG1012 479 L 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
20-483 |
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: 606.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 20 PCNSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTL 99
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 100 TLARTmDIPRSVLNFRFFASSIqHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:pfam00171 84 AEARG-EVDRAIDVLRYYAGLA-RRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 180 SELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVR 339
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 340 SYVTKAHAEGAKILCGeGVDQLSlplrnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGL 419
Cdd:pfam00171 322 KYVEDAKEEGAKLLTG-GEAGLD------NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229277487 420 GATVWSKDVGRIHRVAKRLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTgDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
48-485 |
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: 546.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 48 EVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASSIQHHVSD 127
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 128 CTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVV 207
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 208 FGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEIC 287
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 288 LCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQlslplrN 367
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE------G 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 368 QAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNC 447
Cdd:cd07078 314 GKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 1229277487 448 WLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07078 394 YSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
10-486 |
0e+00 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 544.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 10 LENFIGGKFLPCNSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPA-WSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:TIGR03216 1 IRNFINGAFVESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALKGpWGKMTVAERADLLYAVADEIERRFDDFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHHVSDCTEMSH---LGCMHYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:TIGR03216 81 AAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTECFEMATpdgKGALNYAVRKPLGVVGVISPWNLPLLLMTWKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 166 APAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGP-RVGEALVSHPEVPVISFTGSQPTAERITQLSA 244
Cdd:TIGR03216 161 GPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSAIMKAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 245 PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSA 324
Cdd:TIGR03216 241 DGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 325 NMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQLSLPLRNqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:TIGR03216 321 NMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVPDFGDALAG--GAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 405 EEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVC 478
|
..
gi 1229277487 485 IK 486
Cdd:TIGR03216 479 IK 480
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-485 |
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: 525.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 27 SYDPSTGEVYCKVPNSGKEEIEVAVQAAREAF--PAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTL--TLA 102
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIreTRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 103 RTMDIPRSvlnFRFFAS---SIQHHVSDCTEMSHLGcmhYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:cd07114 81 QVRYLAEW---YRYYAGladKIEGAVIPVDKGDYLN---FTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 180 SELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVR 339
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 340 SYVTKAHAEGAKILCGeGVdQLSLPLRNqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGL 419
Cdd:cd07114 315 RYVARAREEGARVLTG-GE-RPSGADLG-AGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGL 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229277487 420 GATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07114 392 AAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
13-485 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 520.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSR--SPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07091 7 FINNEFVDSVSgkTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA--------SSIQhhvsdcTEMSHLGcmhYTVRTPVGIAGLISPWNLPLYL 160
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAgwadkiqgKTIP------IDGNFLA---YTRREPIGVCGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 161 LTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERIT 240
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 241 QLSA-PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIP 319
Cdd:cd07091 238 EAAAkSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 320 SDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVdqlslplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCV 399
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGER-------HGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 400 VPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTE 479
Cdd:cd07091 391 LKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQ 470
|
....*.
gi 1229277487 480 IKTITI 485
Cdd:cd07091 471 VKAVTI 476
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-485 |
1.29e-178 |
|
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: 508.51 E-value: 1.29e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARtMDI 107
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 108 PRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTA 187
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 188 WMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDAN 267
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 268 LEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHA 347
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 348 EGAKILCGEGVDQLslplrnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKD 427
Cdd:cd07103 321 KGAKVLTGGKRLGL-------GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1229277487 428 VGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
10-485 |
1.53e-176 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 504.73 E-value: 1.53e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 10 LENFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEEL 87
Cdd:TIGR02299 1 IGHFIDGEFVPSESgeTFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 88 AQAESKDQGKTLTLARTMdIPRSVLNFRFFASSIQHHVSDCTEMS--HLgcmHYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQ-VIRAAENFRFFADKCEEAMDGRTYPVdtHL---NYTVRVPVGPVGLITPWNAPFMLSTWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 166 APAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAP 245
Cdd:TIGR02299 157 APALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSAN 325
Cdd:TIGR02299 237 TLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 326 MGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQLSLPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:TIGR02299 317 VGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTFRGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 406 EEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:TIGR02299 397 EEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVAL 476
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-484 |
3.87e-168 |
|
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: 482.39 E-value: 3.87e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 12 NFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQ 89
Cdd:cd07138 1 FYIDGAWVAPAGteTIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 90 AESKDQGKTLTLARTMDIPRSVLNFRFFASSI-----QHHVSDctemSHLgcmhytVRTPVGIAGLISPWNLPLYLLTWK 164
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALkdfefEERRGN----SLV------VREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 165 IAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA 244
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 245 PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSA 324
Cdd:cd07138 231 DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 325 NMGALISKAHLEKVRSYVTKAHAEGAKILCG-----EGVDQlslplrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCV 399
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGgpgrpEGLER---------GYFVKPTVFADVTPDMTIAREEIFGPVLSI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 400 VPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNcWLIRELNLPFGGMKSSGIGREGAKDSYDFFTE 479
Cdd:cd07138 382 IPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLE 460
|
....*
gi 1229277487 480 IKTIT 484
Cdd:cd07138 461 VKSIQ 465
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
29-483 |
8.24e-167 |
|
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: 478.47 E-value: 8.24e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 29 DPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTMDIP 108
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 109 RSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAW 188
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 189 MFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANL 268
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 269 EECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAE 348
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 349 GAKILC-GEGVDqlslplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKD 427
Cdd:cd07115 322 GARLLTgGKRPG--------ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229277487 428 VGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07115 394 LGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-485 |
3.53e-166 |
|
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: 477.09 E-value: 3.53e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 26 DSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPA--WSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLAR 103
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 104 TMDIPRSVLNFRFFASSIQHhVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELT 183
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIDK-VYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 184 SVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA-PHCKKLSLELGGKNPAII 262
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 263 FEDA-NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSY 341
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 342 VTKAHAEGAKILCGEGVDQLslplrNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGA 421
Cdd:cd07112 324 IESGKAEGARLVAGGKRVLT-----ETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 422 TVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-483 |
1.53e-165 |
|
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: 475.26 E-value: 1.53e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARtMDI 107
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 108 PRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTA 187
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPG-GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 188 WMFCKLLDKAGVPPGVINVVFGTGpRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDAN 267
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 268 LEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHA 347
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 348 EGAKILCGEGVDQLSLPLRNqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKD 427
Cdd:cd07090 319 EGAKVLCGGERVVPEDGLEN--GFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229277487 428 VGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-487 |
7.64e-165 |
|
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: 474.52 E-value: 7.64e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 11 ENFIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07559 2 DNFINGEWVAPskGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE-DTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 169 IAAGNTVIAKPSELTSVTAWMFCKLLDKAgVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 249 KLSLELGGKNPAIIFEDANLEEC------IPATVRSSFaNQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDP 322
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAMDADDdfddkaEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 323 SANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQLSlplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPF 402
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLG---GLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 403 DSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 482
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKN 475
|
....*
gi 1229277487 483 ITIKY 487
Cdd:cd07559 476 ILVSY 480
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-485 |
4.27e-163 |
|
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: 470.25 E-value: 4.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAF--PAWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07119 1 YIDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTmDIPRSVLNFRFFASSI------QHHVSDCTEmshlgcmHYTVRTPVGIAGLISPWNLPLYLLT 162
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLAtketgeVYDVPPHVI-------SRTVREPVGVCGLITPWNYPLLQAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 163 WKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQL 242
Cdd:cd07119 153 WKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 243 SAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDP 322
Cdd:cd07119 233 AAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 323 SANMGALISKAHLEKVRSYVTKAHAEGAKILCGEgvdqlSLPLRN--QAGYFMLPTVITDIKDESCCMTEEIFGPVTCVV 400
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGG-----KRPTGDelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 401 PFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEI 480
Cdd:cd07119 388 RFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQET 467
|
....*
gi 1229277487 481 KTITI 485
Cdd:cd07119 468 KHINI 472
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-486 |
1.64e-159 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 460.53 E-value: 1.64e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 8 LMLENFIGGKFLPCN-SYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEE 86
Cdd:PRK13473 1 MQTKLLINGELVAGEgEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 87 LAQAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQH--------HVSDCTEMSHlgcmhytvRTPVGIAGLISPWNLPL 158
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARClegkaageYLEGHTSMIR--------RDPVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 159 YLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAgVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAER 238
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 239 ITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGI 318
Cdd:PRK13473 232 VLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 319 PSDPSANMGALISKAHLEKVRSYVTKAHAEG-AKILCGeGVDQlslplrNQAGYFMLPTVITDIKDESCCMTEEIFGPVT 397
Cdd:PRK13473 312 PDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTG-GEAP------DGKGYYYEPTLLAGARQDDEIVQREVFGPVV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 398 CVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCW--LIRElnLPFGGMKSSGIGREGAKDSYD 475
Cdd:PRK13473 385 SVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHfmLVSE--MPHGGQKQSGYGKDMSLYGLE 462
|
490
....*....|.
gi 1229277487 476 FFTEIKTITIK 486
Cdd:PRK13473 463 DYTVVRHVMVK 473
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-485 |
1.36e-158 |
|
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: 457.56 E-value: 1.36e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTMDI 107
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 108 PRSVLNFRFFASSIQH-HVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVT 186
Cdd:cd07092 82 PGAVDNFRFFAGAARTlEGPAAGEYLP-GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 187 AWMFCKLLdKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 266
Cdd:cd07092 161 TLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 267 NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAh 346
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 347 AEGAKILCGEGVdqlslplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSK 426
Cdd:cd07092 319 PAHARVLTGGRR-------AEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229277487 427 DVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
12-483 |
4.56e-155 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 449.72 E-value: 4.56e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 12 NFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQ 89
Cdd:PRK13252 9 LYIDGAYVEATSgeTFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 90 AESKDQGKTLTLARTMDIPRSVLNFRFFA--------SSIQHHVSDctemshlgcMHYTVRTPVGIAGLISPWNLPLYLL 161
Cdd:PRK13252 89 LETLDTGKPIQETSVVDIVTGADVLEYYAglapalegEQIPLRGGS---------FVYTRREPLGVCAGIGAWNYPIQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 162 TWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGpRVGEALVSHPEVPVISFTGSQPTAERITQ 241
Cdd:PRK13252 160 CWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 242 LSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSD 321
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 322 PSANMGALISKAHLEKVRSYVTKAHAEGAKILC-GEGVDQLSLPlrnqAGYFMLPTVITDIKDEsccMT---EEIFGPVT 397
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCgGERLTEGGFA----NGAFVAPTVFTDCTDD---MTivrEEIFGPVM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 398 CVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFF 477
Cdd:PRK13252 392 SVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHY 471
|
....*.
gi 1229277487 478 TEIKTI 483
Cdd:PRK13252 472 TQIKSV 477
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
13-485 |
5.29e-155 |
|
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: 449.55 E-value: 5.29e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSR-SPQERSLILNRVADVLEQSLEELAQ 89
Cdd:cd07144 11 FINNEFVKSsdGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 90 AESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSP-NKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 170 AAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKK 249
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 250 LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRK-WKVGIPSDPSANMGA 328
Cdd:cd07144 250 VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 329 LISKAHLEKVRSYVTKAHAEGAKILCGegvdQLSLPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGAKLVYG----GEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229277487 409 IARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-485 |
1.76e-154 |
|
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: 446.98 E-value: 1.76e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARtMDI 107
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 108 PRSVLNFRFFAS-SIQHHVSDCTEMSHLgcmhYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVT 186
Cdd:cd07106 81 GGAVAWLRYTASlDLPDEVIEDDDTRRV----ELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 187 AWMFCKLLDKAgVPPGVINVVFGtGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 266
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 267 NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAH 346
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 347 AEGAKILCGEGVDqlslplrNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSK 426
Cdd:cd07106 315 AKGAKVLAGGEPL-------DGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229277487 427 DVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07106 388 DLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-483 |
8.79e-154 |
|
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: 445.93 E-value: 8.79e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 11 ENFIGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQ 89
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 90 AESKDQGKTLTLARTmDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 170 AAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKK 249
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 250 LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGAL 329
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 330 ISKAHLEKVRSYVTKAHAEGAKILC-GEGVDqlslplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYgGERLK------RPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229277487 409 IARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLI-RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTI 483
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-485 |
3.43e-153 |
|
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: 443.98 E-value: 3.43e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 27 SYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSR-SPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTm 105
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 106 DIPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSV 185
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGP-GYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 186 TAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 265
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 266 ANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDpSANMGALISKAHLEKVRSYVTKA 345
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 346 HAEGAKILCGEGVdqlsLPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWS 425
Cdd:cd07109 318 RARGARIVAGGRI----AEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229277487 426 KDVGRIHRVAKRLQSGLVWTNCWLIRE-LNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
29-484 |
2.11e-152 |
|
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: 441.79 E-value: 2.11e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 29 DPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLArTMDIP 108
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 109 RSVLNFRFFAS---SIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSV 185
Cdd:cd07110 82 DVAGCFEYYADlaeQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 186 TAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 265
Cdd:cd07110 162 TELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 266 ANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKA 345
Cdd:cd07110 242 ADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 346 HAEGAKILCGEGVdqlslPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWS 425
Cdd:cd07110 322 KEEGARLLCGGRR-----PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229277487 426 KDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-485 |
7.91e-150 |
|
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: 435.23 E-value: 7.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 30 PSTGEVYCKVPNSGKEEIEVAVQAAREAFPA--WSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTmDI 107
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 108 PRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTA 187
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 188 WMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDAN 267
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 268 LEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHA 347
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 348 EGAKILCGEGVdqlslpLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKD 427
Cdd:cd07118 323 EGATLLLGGER------LASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1229277487 428 VGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-485 |
5.81e-147 |
|
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: 427.93 E-value: 5.81e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 29 DPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLtlaRTMDIP 108
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNAL---RTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 109 --RSVLN-FRFFASsIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSV 185
Cdd:cd07108 80 eaAVLADlFRYFGG-LAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 186 TAWMFCKLLDKAgVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 265
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 266 ANLEECIPATVRSS-FANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTK 344
Cdd:cd07108 238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 345 AHAE-GAKIL-CGEgvdqLSLPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGAT 422
Cdd:cd07108 318 GLSTsGATVLrGGP----LPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 423 VWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSY-DFFTEIKTITI 485
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-487 |
7.46e-147 |
|
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: 428.69 E-value: 7.46e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 12 NFIGGKFLPCNS--YIDSYDPSTG-EVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07131 1 NYIGGEWVDSASgeTFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTmDIPRSVLNFRFFASSIQH---HVSDCtEMSHLGCMhyTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRlfgETVPS-ELPNKDAM--TRRQPIGVVALITPWNFPVAIPSWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 166 APAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAP 245
Cdd:cd07131 157 FPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSAN 325
Cdd:cd07131 237 PNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 326 MGALISKAHLEKVRSYVTKAHAEGAKILCG-EGVDQLSLplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGgERLTGGGY----EKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 405 EEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLI-RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKT 482
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
....*
gi 1229277487 483 ITIKY 487
Cdd:cd07131 473 VYVDY 477
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-485 |
9.99e-147 |
|
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: 423.95 E-value: 9.99e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 52 QAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARtMDIPRSVLNFRFFASSIQHHVSDCTEM 131
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 132 SHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTG 211
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 212 PRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTS 291
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 292 RIFVQRSIYNEFLKRFVeatrkwkvgipsdpsanmgaliskahlekvrsyvtkahaegakilcgegvdqlslplrnqagy 371
Cdd:cd06534 240 RLLVHESIYDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 372 fmlpTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLI- 450
Cdd:cd06534 257 ----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIg 332
|
410 420 430
....*....|....*....|....*....|....*
gi 1229277487 451 RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd06534 333 VGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-483 |
1.51e-146 |
|
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: 427.04 E-value: 1.51e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWS-SRSPQERSLILNRVADVLEQSLEELA---QAESkdqGKTLTLAR 103
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRallVAEV---GAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 104 TMDIPRSVLNFRFFASSI----QHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:cd07089 79 AMQVDGPIGHLRYFADLAdsfpWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 180 SELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVR 339
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 340 SYVTKAHAEGAKILCGEGVdqlslPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGL 419
Cdd:cd07089 319 GYIARGRDEGARLVTGGGR-----PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 420 GATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07089 394 SGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
13-481 |
4.01e-146 |
|
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: 426.53 E-value: 4.01e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQA 90
Cdd:TIGR01804 1 FIDGEYVEDSAgtTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 91 ESKDQGKTLTLARTMDIPRSVLNFRFFASSIQhhvSDCTEMSHLG--CMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAP---ALNGEIIPLGgpSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 169 IAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCK 248
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 249 KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGA 328
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 329 LISKAHLEKVRSYVTKAHAEGAKILCGEGVDQLSlplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:TIGR01804 318 LISAAHRDKVLSYIEKGKAEGATLATGGGRPENV---GLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEV 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229277487 409 IARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 481
Cdd:TIGR01804 395 IARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
13-483 |
6.06e-145 |
|
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: 423.83 E-value: 6.06e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFP--AWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07142 7 FINGQFVDAASgkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQ--HHVSDCTEMSHLGcmhYTVRTPVGIAGLISPWNLPLYLLTWKIA 166
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAGWADkiHGMTLPADGPHHV---YTLHEPIGVVGQIIPWNFPLLMFAWKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 167 PAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA-P 245
Cdd:cd07142 164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSAN 325
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 326 MGALISKAHLEKVRSYVTKAHAEGAKILCGEgvDQLSlplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGG--DRIG-----SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229277487 406 EEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
13-485 |
7.72e-145 |
|
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: 423.14 E-value: 7.72e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAF--PAWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07139 2 FIGGRWVAPSGseTIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 169 IAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGtGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 249 KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGA 328
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 329 LISKAHLEKVRSYVTKAHAEGAKILCGEGVdqlslPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGR-----PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229277487 409 IARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNcWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-485 |
1.35e-144 |
|
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: 422.63 E-value: 1.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQA 90
Cdd:cd07117 4 FINGEWVKGssGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 91 ESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07117 84 ETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE-DTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 171 AGNTVIAKPSELTSVTAWMFCKLLDKAgVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07117 163 AGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 251 SLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALI 330
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 331 SKAHLEKVRSYVTKAHAEGAKILCGeGVDQLSLPLrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIA 410
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTG-GHRLTENGL--DKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229277487 411 RANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-485 |
8.82e-144 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 420.52 E-value: 8.82e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQA 90
Cdd:cd07088 1 YINGEFVPSSSgeTIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 91 ESKDQGKTLTLARtMDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 171 AGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 251 SLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALI 330
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 331 SKAHLEKVRSYVTKAHAEGAKILCGEGVDQLslplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIA 410
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKRPEG------EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229277487 411 RANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-481 |
3.90e-143 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 419.87 E-value: 3.90e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 7 LLMLENFIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSL 84
Cdd:PLN02278 22 LLRTQGLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 85 EELAQAESKDQGKTLTLAR-TMDIPRSVLNFrfFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTW 163
Cdd:PLN02278 102 EDLAQLMTLEQGKPLKEAIgEVAYGASFLEY--FAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 164 KIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLS 243
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 244 APHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPS 323
Cdd:PLN02278 260 AATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 324 ANMGALISKAHLEKVRSYVTKAHAEGAKILCGEgvDQLSLplrnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFD 403
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGG--KRHSL-----GGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFK 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229277487 404 SEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 481
Cdd:PLN02278 413 TEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-486 |
2.15e-142 |
|
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: 417.13 E-value: 2.15e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 12 NFIGGKFLPcnsyidSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAF---PAWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07141 17 DSVSGKTFP------TINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA--------SSIQhhvSDCTEMShlgcmhYTVRTPVGIAGLISPWNLPLYL 160
Cdd:cd07141 91 SLETLDNGKPFSKSYLVDLPGAIKVLRYYAgwadkihgKTIP---MDGDFFT------YTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 161 LTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERIT 240
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 241 QLSA-PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIP 319
Cdd:cd07141 242 QAAGkSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 320 SDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVdqlslplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCV 399
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKR-------HGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 400 VPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTE 479
Cdd:cd07141 395 FKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTE 474
|
....*..
gi 1229277487 480 IKTITIK 486
Cdd:cd07141 475 VKTVTIK 481
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-485 |
3.71e-142 |
|
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: 415.98 E-value: 3.71e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARt 104
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 105 MDIPRSVLNFRFFASSIQHHV-----SDCTEMSHLGcMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRgetipVDAYEYNERR-IAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 180 SELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVR 339
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 340 SYVTKAHAEGAKILCGegvdqlslpLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGL 419
Cdd:cd07145 319 NLVNDAVEKGGKILYG---------GKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229277487 420 GATVWSKDVGRIHRVAKRLQSGLVWTN-CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07145 390 QASVFTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
46-485 |
2.81e-141 |
|
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: 412.69 E-value: 2.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 46 EIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTltlartmdIPRSVLNFRFFASSIQHHV 125
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGST--------RPKAAFEVGAAIAILREAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 126 SDCTEM------SHL-GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVT-AWMFCKLLDKA 197
Cdd:cd07104 73 GLPRRPegeilpSDVpGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 198 GVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVR 277
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 278 SSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEG 357
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 358 VDqlslplrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKR 437
Cdd:cd07104 313 YE----------GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAER 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1229277487 438 LQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07104 383 LETGMVHINDQTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
13-483 |
6.12e-141 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 414.22 E-value: 6.12e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFP--AWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:PLN02766 24 FINGEFVDAASgkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSR-QLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 169 IAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA-PHC 247
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAtSNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 248 KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMG 327
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 328 ALISKAHLEKVRSYVTKAHAEGAKILCGegvdqlSLPLRNQaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 407
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTG------GKPCGDK-GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229277487 408 VIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
13-486 |
6.34e-141 |
|
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: 413.46 E-value: 6.34e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAF--PAWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07143 10 FINGEFVDSvhGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFF---ASSIQHHVSDcTEMSHLGcmhYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYggwADKIHGQVIE-TDIKKLT---YTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 166 APAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA- 244
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 245 PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSA 324
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 325 NMGALISKAHLEKVRSYVTKAHAEGAKILCGEgvdqlslPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGG-------KRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 405 EEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVH 478
|
..
gi 1229277487 485 IK 486
Cdd:cd07143 479 IN 480
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-484 |
8.34e-140 |
|
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: 409.81 E-value: 8.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 27 SYDPSTGEVYCKVPNSGKEEIEVAVQAAREAF--PAWSsRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARt 104
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 105 MDIPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTS 184
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEP-GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 185 VTAWMFCKLLDKA-GVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 263
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 264 EDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVT 343
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 344 KAHAEGAKILC-GEGVDQlslplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGAT 422
Cdd:cd07120 318 RAIAAGAEVVLrGGPVTE-----GLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 423 VWSKDVGRIHRVAKRLQSGLVWTNCW--LIRELNlpFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07120 393 VWTRDLARAMRVARAIRAGTVWINDWnkLFAEAE--EGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-485 |
2.41e-139 |
|
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: 408.26 E-value: 2.41e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 26 DSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLA--R 103
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAwfE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 104 TMDIPRSVLNfrffASSIQHHVSDCTEMSHL-GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEL 182
Cdd:cd07150 82 TTFTPELLRA----AAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 183 TSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 263 FEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYV 342
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 343 TKAHAEGAKILCGEGVDqlslplrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGAT 422
Cdd:cd07150 318 EDAVAKGAKLLTGGKYD----------GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 423 VWSKDVGRIHRVAKRLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
13-487 |
3.11e-139 |
|
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: 409.14 E-value: 3.11e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAF-PAWSSRSPQERSLILNRVADVLEQSLEELAQ 89
Cdd:cd07113 3 FIDGRPVAGQSekRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 90 AESKDQGKTLTLARTMDIPRSVLNFRFFA---SSIQHHVSDCTEMSHLGCMH--YTVRTPVGIAGLISPWNLPLYLLTWK 164
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAgwaTKINGETLAPSIPSMQGERYtaFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 165 IAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGpRVGEALVSHPEVPVISFTGSQPTAERITQLSA 244
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 245 PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSA 324
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 325 NMGALISKAHLEKVRSYVTKAHAEGAKILCG-EGVDqlslplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFD 403
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIVRGgEALA--------GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 404 SEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
....
gi 1229277487 484 TIKY 487
Cdd:cd07113 474 MIRY 477
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-487 |
6.25e-138 |
|
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: 406.07 E-value: 6.25e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 11 ENFIGGKFLP--CNSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07116 2 DNFIGGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDE-NTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 169 IAAGNTVIAKPSELTSVTAWMFCKLLDKAgVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 249 KLSLELGGKNPAIIFE------DANLEECIPATVRSSFaNQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDP 322
Cdd:cd07116 240 PVTLELGGKSPNIFFAdvmdadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 323 SANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQLSlplRNQAGYFMLPTVITDIKDEScCMTEEIFGPVTCVVPF 402
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELG---GLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 403 DSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 482
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 474
|
....*
gi 1229277487 483 ITIKY 487
Cdd:cd07116 475 LLVSY 479
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-485 |
4.93e-136 |
|
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: 400.05 E-value: 4.93e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLART 104
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 105 mDIPRSVLNFRFFASsiqhhvsdctEMSHL--------------GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07149 81 -EVDRAIETLRLSAE----------EAKRLagetipfdaspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 171 AGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAphCKKL 250
Cdd:cd07149 150 AGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 251 SLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALI 330
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 331 SKAHLEKVRSYVTKAHAEGAKILCGEGVDqlslplrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIA 410
Cdd:cd07149 308 SEAEAERIEEWVEEAVEGGARLLTGGKRD----------GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 411 RANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVwtncwLIREL------NLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07149 378 MANDSPYGLQAGVFTNDLQKALKAARELEVGGV-----MINDSstfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
.
gi 1229277487 485 I 485
Cdd:cd07149 453 F 453
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-487 |
3.39e-135 |
|
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: 397.90 E-value: 3.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 29 DPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTmDIP 108
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 109 RSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAW 188
Cdd:cd07107 82 VAAALLDYFAGLVTELKGETIPVGG-RNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 189 MFCKLLDKAgVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANL 268
Cdd:cd07107 161 RLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 269 EECIPATVRS-SFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHA 347
Cdd:cd07107 240 EAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 348 EGAKILCGEGVDQLSLPlrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKD 427
Cdd:cd07107 320 EGARLVTGGGRPEGPAL---EGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 428 VGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITIKY 487
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-487 |
6.64e-135 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 398.41 E-value: 6.64e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPA--WSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:cd07140 9 FINGEFVDAEGgkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA---SSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:cd07140 89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 166 APAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA- 244
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 245 PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSA 324
Cdd:cd07140 249 SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRST 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 325 NMGALISKAHLEKVRSYVTKAHAEGAKILCGEgvDQLSLPlrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:cd07140 329 DHGPQNHKAHLDKLVEYCERGVKEGATLVYGG--KQVDRP-----GFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 405 E--EEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 482
Cdd:cd07140 402 GdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKT 481
|
....*
gi 1229277487 483 ITIKY 487
Cdd:cd07140 482 VTIEY 486
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
13-472 |
3.89e-132 |
|
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: 390.99 E-value: 3.89e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFL--PCNSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQA 90
Cdd:cd07111 25 FINGKWVkpENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 91 ESKDQGKTLTLARTMDIPRSVLNFRFFAssIQHHVSDcTEMSHlgcmhytvRTPVGIAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07111 105 ESLDNGKPIRESRDCDIPLVARHFYHHA--GWAQLLD-TELAG--------WKPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 171 AGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGpRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 251 SLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALI 330
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 331 SKAHLEKVRSYVTKAHAEGAKILcgegvdQLSLPLRNQaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIA 410
Cdd:cd07111 333 DPAQLKRIRELVEEGRAEGADVF------QPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229277487 411 RANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKD 472
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKE 467
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-487 |
4.41e-131 |
|
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: 388.46 E-value: 4.41e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 12 NFIGGKFLP-CNSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQA 90
Cdd:cd07086 1 GVIGGEWVGsGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 91 ESKDQGKTLT------------------LARTmdiprsvLNFRFFASSIQHHVSdctemshlgcmhYTVRTPVGIAGLIS 152
Cdd:cd07086 81 VSLEMGKILPeglgevqemidicdyavgLSRM-------LYGLTIPSERPGHRL------------MEQWNPLGVVGVIT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 153 PWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKA----GVPPGVINVVFGTGPrVGEALVSHPEVPVIS 228
Cdd:cd07086 142 AFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 229 FTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFV 308
Cdd:cd07086 221 FTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 309 EATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVdqlslPLRNQAGYFMLPTVITDIKDESCCM 388
Cdd:cd07086 301 KAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKR-----IDGGEPGNYVEPTIVTGVTDDARIV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 389 TEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRV--AKRLQSGLVWTNCWLI-RELNLPFGGMKSSGI 465
Cdd:cd07086 376 QEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGG 455
|
490 500
....*....|....*....|..
gi 1229277487 466 GREGAKDSYDFFTEIKTITIKY 487
Cdd:cd07086 456 GRESGSDAWKQYMRRSTCTINY 477
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
13-487 |
7.75e-128 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 381.00 E-value: 7.75e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLP--CNSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPA-----WSSRSPQERSLILNRVADVLEQSLE 85
Cdd:PLN02467 11 FIGGEWREpvLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 86 ELAQAESKDQGKTLTLArTMDIPRSVLNFRFFAS-----SIQHHVSDCTEMSHLGCmhYTVRTPVGIAGLISPWNLPLYL 160
Cdd:PLN02467 91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADlaealDAKQKAPVSLPMETFKG--YVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 161 LTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERIT 240
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 241 QLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPS 320
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 321 DPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGeGVDqlslPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVV 400
Cdd:PLN02467 328 EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCG-GKR----PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 401 PFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEI 480
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSV 482
|
....*..
gi 1229277487 481 KTITiKY 487
Cdd:PLN02467 483 KQVT-KY 488
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-485 |
1.99e-124 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 370.40 E-value: 1.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTmDI 107
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 108 PRSVLNFRFFASSI-----QHHVSDCTEMSHLGcmHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEL 182
Cdd:cd07099 80 LLALEAIDWAARNAprvlaPRKVPTGLLMPNKK--ATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 183 TSVTAWMFCKLLDKAGVPPGVINVVFGTGPrVGEALVSHpEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 263 FEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYV 342
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 343 TKAHAEGAKILCGegvdqlsLPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGAT 422
Cdd:cd07099 316 DDAVAKGAKALTG-------GARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229277487 423 VWSKDVGRIHRVAKRLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07099 389 VFSRDLARAEAIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
13-487 |
1.15e-122 |
|
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: 368.09 E-value: 1.15e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAE 91
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 92 SKDQGKTLTLArTMDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRtPVGIAGLISPWNLPLYLLTWKIAPAIAA 171
Cdd:cd07124 116 VLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALVT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 172 GNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA------P 245
Cdd:cd07124 194 GNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgqK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSAN 325
Cdd:cd07124 274 WLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 326 MGALISKAHLEKVRSYVTKAHAEGaKILCGEGVDQLSlplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07124 354 MGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA-----AEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 406 EEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTN-----CWLIRElnlPFGGMKSSGIG-REGAKDSYDFFTE 479
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkitgALVGRQ---PFGGFKMSGTGsKAGGPDYLLQFMQ 504
|
....*...
gi 1229277487 480 IKTITIKY 487
Cdd:cd07124 505 PKTVTENF 512
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-486 |
2.49e-122 |
|
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: 365.47 E-value: 2.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKT-----L 99
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTrikanI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 100 TLARTMDIPRSvlnfrffASSIQHHVSDCTEMSHL-GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAK 178
Cdd:cd07151 92 EWGAAMAITRE-------AATFPLRMEGRILPSDVpGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 179 PSELTSVTA-WMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGK 257
Cdd:cd07151 165 PASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 258 NPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEK 337
Cdd:cd07151 245 NPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 338 VRSYVTKAHAEGAKILCGEGVDqlslplrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKY 417
Cdd:cd07151 325 LLDKIEQAVEEGATLLVGGEAE----------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEY 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 418 GLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:cd07151 395 GLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
10-487 |
3.60e-122 |
|
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: 365.30 E-value: 3.60e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 10 LENFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEEL 87
Cdd:cd07085 1 LKLFINGEWVESKTteWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 88 AQAESKDQGKTLTLARTmDIPRSVLNFRFfASSIQHHVS-DCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIA 166
Cdd:cd07085 81 ARLITLEHGKTLADARG-DVLRGLEVVEF-ACSIPHLLKgEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 167 PAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGtGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPH 246
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 247 CKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANM 326
Cdd:cd07085 238 GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 327 GALISKAHLEKVRSYVTKAHAEGAKILC-GEGVDQLSLPlrnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLdGRGVKVPGYE----NGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 406 EEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVwtncwlirELNLP---------FGGMKSSGIGREGA--KDSY 474
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMV--------GINVPipvplaffsFGGWKGSFFGDLHFygKDGV 465
|
490
....*....|...
gi 1229277487 475 DFFTEIKTITIKY 487
Cdd:cd07085 466 RFYTQTKTVTSRW 478
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
50-485 |
7.93e-122 |
|
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: 363.05 E-value: 7.93e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 50 AVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARtMDIPRSVLNFRFFASSIQHHVSDCT 129
Cdd:cd07105 5 AVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQIIGGSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 130 EMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVF- 208
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTh 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 209 --GTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEI 286
Cdd:cd07105 164 spEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 287 CLCTSRIFVQRSIYNEFLKRFVEATRKwkvgIPSDPSAnMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQlslplr 366
Cdd:cd07105 244 CMSTERIIVHESIADEFVEKLKAAAEK----LFAGPVV-LGSLVSAAAADRVKELVDDALSKGAKLVVGGLADE------ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 367 NQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTN 446
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1229277487 447 CWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07105 393 GMTVHdEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-485 |
2.05e-121 |
|
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: 362.91 E-value: 2.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARt 104
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 105 MDIPRSVLNFRFFASSIQHHV-----SDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRgeeipLDATQGSD-NRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 180 SELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAphCKKLSLELGGKNP 259
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVR 339
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 340 SYVTKAHAEGAKILCGEGVDqlslplrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGL 419
Cdd:cd07094 317 RWVEEAVEAGARLLCGGERD----------GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229277487 420 GATVWSKDVGRIHRVAKRLQSGLVWTN-CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
13-483 |
6.58e-120 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 361.82 E-value: 6.58e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFP--AWSSRSPQERSLILNRVADVLEQSLEELA 88
Cdd:PLN02466 61 LINGQFVDAASgkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA------------SSIQHHVSdctemshlgcmhyTVRTPVGIAGLISPWNL 156
Cdd:PLN02466 141 ALETWDNGKPYEQSAKAELPMFARLFRYYAgwadkihgltvpADGPHHVQ-------------TLHEPIGVAGQIIPWNF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 157 PLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTA 236
Cdd:PLN02466 208 PLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 237 ERITQLSA-PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWK 315
Cdd:PLN02466 288 KIVLELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 316 VGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEgvDQLSlplrnQAGYFMLPTVITDIKDESCCMTEEIFGP 395
Cdd:PLN02466 368 VGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGG--DRFG-----SKGYYIQPTVFSNVQDDMLIAQDEIFGP 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 396 VTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYD 475
Cdd:PLN02466 441 VQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLN 520
|
....*...
gi 1229277487 476 FFTEIKTI 483
Cdd:PLN02466 521 NYLQVKAV 528
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
8-485 |
9.86e-119 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 357.28 E-value: 9.86e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 8 LMLEN--FIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPA--WSSRSPQERSLILNRVADVLE 81
Cdd:PRK09847 16 LAIENrlFINGEYTAAaeNETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 82 QSLEELAQAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHHVSDCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLL 161
Cdd:PRK09847 96 AHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSS-HELAMIVREPVGVIAAIVPWNFPLLLT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 162 TWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQ 241
Cdd:PRK09847 175 CWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 242 LSA-PHCKKLSLELGGKNPAIIFEDA-NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIP 319
Cdd:PRK09847 255 DAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 320 SDPSANMGALISKAHLEKVRSYVTKAHAEGakilcgegvdQLSLPLRNQAGYFML-PTVITDIKDESCCMTEEIFGPVTC 398
Cdd:PRK09847 335 LDPATTMGTLIDCAHADSVHSFIREGESKG----------QLLLDGRNAGLAAAIgPTIFVDVDPNASLSREEIFGPVLV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 399 VVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFT 478
Cdd:PRK09847 405 VTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFT 484
|
....*..
gi 1229277487 479 EIKTITI 485
Cdd:PRK09847 485 ELKTIWI 491
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
25-484 |
2.62e-115 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 349.56 E-value: 2.62e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVAD-VLEQSLE--ELAQAESkdqGKTLTL 101
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDlVLENREEllDLVQLET---GKARRH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 102 A--RTMDIPrsvLNFRFFASSIQHH------------VSDCTEmshlgcmhytVRTPVGIAGLISPWNLPLYLLTWKIAP 167
Cdd:PRK09407 111 AfeEVLDVA---LTARYYARRAPKLlaprrragalpvLTKTTE----------LRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 168 AIAAGNTVIAKPSELTSVTA-WMFcKLLDKAGVPPGVINVVFGTGPRVGEALVSHpeVPVISFTGSQPTAERITQLSAPH 246
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTAlAAV-ELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 247 CKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANM 326
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 327 GALISKAHLEKVRSYVTKAHAEGAKILCGeGVDqlslplRNQAG-YFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAG-GKA------RPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 406 EEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTN-----CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEI 480
Cdd:PRK09407 408 DEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAW--GSVDAPMGGMKDSGLGRRHGAEGLLKYTES 485
|
....
gi 1229277487 481 KTIT 484
Cdd:PRK09407 486 QTIA 489
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
29-484 |
4.07e-115 |
|
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: 346.60 E-value: 4.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 29 DPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELA---QAESkdqGKTLTLA--R 103
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLdliQLET---GKARRHAfeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 104 TMDIprsVLNFRFFASSIQHHVSDCTEMSHLGCMHYTV--RTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSE 181
Cdd:cd07101 79 VLDV---AIVARYYARRAERLLKPRRRRGAIPVLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 182 LTSVTA-WMFcKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVpvISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 260
Cdd:cd07101 156 QTALTAlWAV-ELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 261 IIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRS 340
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 341 YVTKAHAEGAKILCGeGVDqlslplRNQAG-YFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGL 419
Cdd:cd07101 313 HVDDAVAKGATVLAG-GRA------RPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 420 GATVWSKDVGRIHRVAKRLQSGLVWTN-----CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNegyaaAW--ASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
33-485 |
1.49e-111 |
|
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: 336.96 E-value: 1.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 33 GEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLArtmdiprsvl 112
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 113 nfrffASSIQHHVSDCTEMSHL-------------GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:cd07152 71 -----GFEVGAAIGELHEAAGLptqpqgeilpsapGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 180 SELTSVTA-WMFCKLLDKAGVPPGVINVVFGtGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKN 258
Cdd:cd07152 146 DPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 259 PAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKV 338
Cdd:cd07152 225 ALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 339 RSYVTKAHAEGAKILCGEGVDQLslplrnqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYG 418
Cdd:cd07152 305 HAIVDDSVAAGARLEAGGTYDGL----------FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYG 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229277487 419 LGATVWSKDVGRIHRVAKRLQSGLVWTN-CWLIRELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITI 485
Cdd:cd07152 375 LSAGIISRDVGRAMALADRLRTGMLHINdQTVNDEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
47-485 |
8.28e-111 |
|
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: 334.81 E-value: 8.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 47 IEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASSIQHHVS 126
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAENAEAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 127 DcTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINV 206
Cdd:cd07100 80 D-EPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 207 VFGTGPRVgEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEI 286
Cdd:cd07100 159 LLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 287 CLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQlslplr 366
Cdd:cd07100 238 CIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 367 nQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTN 446
Cdd:cd07100 312 -GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 1229277487 447 CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07100 391 GMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
29-485 |
5.21e-109 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 330.86 E-value: 5.21e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 29 DPSTGEVYCKVPNSGKEEIEVAVQAAReAFPAWSSRspQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARtMDIP 108
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALAA-SYRSTLTR--YQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 109 RSVLNFRFFAS---SIQHHVSDCTEMSHLGC-MHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTS 184
Cdd:cd07146 81 RAADVLRFAAAealRDDGESFSCDLTANGKArKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 185 VTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAphCKKLSLELGGKNPAIIFE 264
Cdd:cd07146 161 LSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 265 DANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTK 344
Cdd:cd07146 239 DADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 345 AHAEGAKILCGEGVDqlslplrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVW 424
Cdd:cd07146 319 AIAQGARVLLGNQRQ----------GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVC 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229277487 425 SKDVGRIHRVAKRLQSGLVwtNCWLI---RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITI 485
Cdd:cd07146 389 TNDLDTIKRLVERLDVGTV--NVNEVpgfRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
25-485 |
1.86e-108 |
|
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: 329.59 E-value: 1.86e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLART 104
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 105 mDIPRSVLNFRFFA--SSIQHhvsdcTEMSHL-------GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTV 175
Cdd:cd07147 81 -EVARAIDTFRIAAeeATRIY-----GEVLPLdisargeGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 176 IAKPSELTSVTAWMFCKLLDKAGVPPGVINVVfgtgP---RVGEALVSHPEVPVISFTGSQPTAERITQLsAPHcKKLSL 252
Cdd:cd07147 155 VLKPASRTPLSALILGEVLAETGLPKGAFSVL----PcsrDDADLLVTDERIKLLSFTGSPAVGWDLKAR-AGK-KKVVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 253 ELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISK 332
Cdd:cd07147 229 ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 333 AHLEKVRSYVTKAHAEGAKILCGEGVDqlslplrnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARA 412
Cdd:cd07147 309 SEAERVEGWVNEAVDAGAKLLTGGKRD----------GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229277487 413 NGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTN---CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07147 379 NDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdvpTF--RVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
25-486 |
1.63e-105 |
|
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: 322.60 E-value: 1.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSP-QERSLILNRVADVLEQSLEELAQAESKDQGKTLTLA- 102
Cdd:cd07082 18 IEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 103 ----RTMD-IPRSVLNF-RFFASSIQHHVSDCTemshLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVI 176
Cdd:cd07082 98 kevdRTIDyIRDTIEELkRLDGDSLPGDWFPGT----KGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 177 AKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSapHCKKLSLELGG 256
Cdd:cd07082 174 FKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH--PMKRLVLELGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 257 KNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLE 336
Cdd:cd07082 252 KDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSAD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 337 KVRSYVTKAHAEGAKILCGEGvdqlslplrNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVK 416
Cdd:cd07082 332 FVEGLIDDAVAKGATVLNGGG---------REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSN 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229277487 417 YGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIREL-NLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:cd07082 403 YGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPdHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-483 |
3.18e-101 |
|
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: 310.72 E-value: 3.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGK---------- 97
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRpiaqaggeir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 98 -TLTLARTM-DIPRSVLnfrffASSIQHHVSDCTEmshlgcmhYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTV 175
Cdd:cd07102 81 gMLERARYMiSIAEEAL-----ADIRVPEKDGFER--------YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 176 IAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPrVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELG 255
Cdd:cd07102 148 ILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 256 GKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHL 335
Cdd:cd07102 227 GKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 336 EKVRSYVTKAHAEGAKILCGEGvdqlSLPLRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGV 415
Cdd:cd07102 307 DFVRAQIADAIAKGARALIDGA----LFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDS 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229277487 416 KYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07102 383 EYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
6-485 |
6.39e-101 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 311.07 E-value: 6.39e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 6 ELLMLENFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQS 83
Cdd:PRK11241 7 TLFRQQALINGEWLDANNgeVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 84 LEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTW 163
Cdd:PRK11241 87 QDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 164 KIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLS 243
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 244 APHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPS 323
Cdd:PRK11241 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 324 ANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQLslplrnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFD 403
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL-------GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 404 SEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PRK11241 399 DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYM 478
|
..
gi 1229277487 484 TI 485
Cdd:PRK11241 479 CI 480
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
73-487 |
9.22e-98 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 300.50 E-value: 9.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 73 LNRVADVLEQSLEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLIS 152
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 153 PWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGS 232
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 233 QPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATR 312
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 313 KWKVGIPSDPSA-NMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDqlslplrNQAGYFMLPTVITDIKDESCCMTEE 391
Cdd:PRK10090 240 AVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAV-------EGKGYYYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 392 IFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNcwliRElNLP-----FGGMKSSGIG 466
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN----RE-NFEamqgfHAGWRKSGIG 387
|
410 420
....*....|....*....|.
gi 1229277487 467 REGAKDSYDFFTEIKTITIKY 487
Cdd:PRK10090 388 GADGKHGLHEYLQTQVVYLQS 408
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-484 |
2.84e-97 |
|
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: 301.14 E-value: 2.84e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTMDI 107
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 108 PRSVLNFRFfasSIQH--------HVSDCTEMSHLGCM-HYTvrtPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAK 178
Cdd:cd07098 81 LVTCEKIRW---TLKHgekalrpeSRPGGLLMFYKRARvEYE---PLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 179 PSELTSVTAWMFC----KLLDKAGVPPGVINVVFGTgPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLEL 254
Cdd:cd07098 155 VSEQVAWSSGFFLsiirECLAACGHDPDLVQLVTCL-PETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 255 GGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAH 334
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 335 LEKVRSYVTKAHAEGAKILCGEGVDQlsLPLRNQAGYFmLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANG 414
Cdd:cd07098 314 FDRLEELVADAVEKGARLLAGGKRYP--HPEYPQGHYF-PPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANS 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229277487 415 VKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07098 391 TEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVqqLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
13-484 |
9.39e-97 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 301.40 E-value: 9.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAE 91
Cdd:TIGR01237 36 VINGERVETENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 92 SKDQGKTLTLArTMDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAA 171
Cdd:TIGR01237 116 VKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 172 GNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA------P 245
Cdd:TIGR01237 195 GNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSAN 325
Cdd:TIGR01237 275 HLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 326 MGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQlslplrnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:TIGR01237 355 VGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDS--------KGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 406 EEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGlvwtNCWLIRELN------LPFGGMKSSGIG-REGAKDSYDFFT 478
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVG----NLYFNRNITgaivgyQPFGGFKMSGTDsKAGGPDYLALFM 502
|
....*.
gi 1229277487 479 EIKTIT 484
Cdd:TIGR01237 503 QAKTVT 508
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-487 |
1.13e-96 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 301.08 E-value: 1.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 14 IGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAES 92
Cdd:PRK03137 41 IGGERITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 93 KDQGKTLTLArTMDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAG 172
Cdd:PRK03137 121 KEAGKPWAEA-DADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 173 NTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA---P---H 246
Cdd:PRK03137 200 NTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqPgqiW 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 247 CKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPsANM 326
Cdd:PRK03137 280 LKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 327 GALISKAHLEKVRSYVTKAHAEGAKILCGEGVDqlslplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEE 406
Cdd:PRK03137 359 GPVINQASFDKIMSYIEIGKEEGRLVLGGEGDD--------SKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 407 EVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGlvwtNCWLIRELN------LPFGGMKSSGI-GREGAKDSYDFFTE 479
Cdd:PRK03137 431 HALEIANNTEYGLTGAVISNNREHLEKARREFHVG----NLYFNRGCTgaivgyHPFGGFNMSGTdSKAGGPDYLLLFLQ 506
|
....*...
gi 1229277487 480 IKTITIKY 487
Cdd:PRK03137 507 AKTVSEMF 514
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
13-466 |
4.35e-90 |
|
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: 284.09 E-value: 4.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNSYIDSYDPSTGE-VYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEEL---A 88
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELialA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESkdqGKTLTLArtmdIP--RSVLNF-RFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:cd07125 116 AAEA---GKTLADA----DAevREAIDFcRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 166 APAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAP 245
Cdd:cd07125 189 AAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 246 HCK---KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDP 322
Cdd:cd07125 269 RDGpilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 323 SANMGALISKAHLEKVRSYVTKAHAEgAKILCGEGVDQLSlplrnqaGYFMLPTVITDikDESCCMTEEIFGPVTCVVPF 402
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGN-------GYFVAPGIIEI--VGIFDLTTEVFGPILHVIRF 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229277487 403 DSE--EEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGlvwtNCWLIRE------LNLPFGGMKSSGIG 466
Cdd:cd07125 419 KAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYINRNitgaivGRQPFGGWGLSGTG 486
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
46-470 |
7.43e-79 |
|
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: 252.19 E-value: 7.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 46 EIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLART--------MDIprsvlnfrff 117
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDI---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 118 asSIQHHVSDCTEMS-----HLGCMHYTvrtPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCK 192
Cdd:cd07095 71 --SIKAYHERTGERAtpmaqGRAVLRHR---PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 193 LLDKAGVPPGVINVVFGtGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKK-LSLELGGKNPAIIFEDANLEEC 271
Cdd:cd07095 146 LWEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 272 IPATVRSSFANQGEICLCTSRIFV-QRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGA 350
Cdd:cd07095 225 AYLIVQSAFLTAGQRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 351 KILcgegvdqLSLPLRNQAGYFMLPTVI--TDIKDESccmTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDV 428
Cdd:cd07095 305 EPL-------LAMERLVAGTAFLSPGIIdvTDAADVP---DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDE 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1229277487 429 GRIHRVAKRLQSGLVWTNcwliRELN-----LPFGGMKSSGIGREGA 470
Cdd:cd07095 375 ALFERFLARIRAGIVNWN----RPTTgasstAPFGGVGLSGNHRPSA 417
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-485 |
1.29e-78 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 252.74 E-value: 1.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLART 104
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 105 mDIPRSVLNFRFFASSIQHHVSDCT-EMSHLGCMHYTVR-TPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEL 182
Cdd:PRK09406 83 -EALKCAKGFRYYAEHAEALLADEPaDAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 183 TSVTAWMFCKLLDKAGVPPGVinvvFGT---GPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGC----FQTllvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVR 339
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 340 SYVTKAHAEGAKILCGEgvdqlSLPLRNqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGL 419
Cdd:PRK09406 318 KQVDDAVAAGATILCGG-----KRPDGP--GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229277487 420 GATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
25-487 |
1.31e-78 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 252.90 E-value: 1.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLAR- 103
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 104 ----TMDI-------PRSvLNFRFFASSIQHHVsdCTEMSHlgcmhytvrtPVGIAGLISPWNLPLYLLTWKIAPAIAAG 172
Cdd:cd07130 94 evqeMIDIcdfavglSRQ-LYGLTIPSERPGHR--MMEQWN----------PLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 173 NTVIAKPSELTSVTAW----MFCKLLDKAGVPPGVINVVFGtGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07130 161 NVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 249 KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGA 328
Cdd:cd07130 240 RSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 329 LISKAHLEKVRSYVTKAHAEGAKILCGEGVdqlslplRNQAGYFMLPTVITDIKDEScCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVLFGGKV-------IDGPGNYVEPTIVEGLSDAP-IVKEETFAPILYVLKFDTLEEA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 409 IARANGVKYGLGATVWSKDVGRIHRVAKRLQS--GLVwtNCwlirelNLP---------FGGMKSSGIGREGAKDSYDFF 477
Cdd:cd07130 392 IAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIV--NV------NIGtsgaeiggaFGGEKETGGGRESGSDAWKQY 463
|
490
....*....|
gi 1229277487 478 TEIKTITIKY 487
Cdd:cd07130 464 MRRSTCTINY 473
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
13-484 |
4.91e-76 |
|
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: 247.11 E-value: 4.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEVAVQAAREAFPAWSsRSPQE-RSLILNRVADVLEQSLEELAQA 90
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKTWK-DWPQEdRARLLLKAADLLRRRRRELIAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 91 ESKDQGKTLTLArtMDIPRSVLNF-RFFASSIQHHVSDCTEM-SHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07083 101 LTYEVGKNWVEA--IDDVAEAIDFiRYYARAALRLRYPAVEVvPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 169 IAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHC- 247
Cdd:cd07083 179 VAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 248 -----KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDP 322
Cdd:cd07083 259 gqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 323 SANMGALISKAHLEKVRSYVTKAHAEGAKILcgegvdQLSLPLRNqaGYFMLPTVITDIKDESCCMTEEIFGPVTCV--V 400
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHGKNEGQLVL------GGKRLEGE--GYFVAPTVVEEVPPKARIAQEEIFGPVLSVirY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 401 PFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIREL--NLPFGGMKSSGIG-REGAKDSYDFF 477
Cdd:cd07083 411 KDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSGTNaKTGGPHYLRRF 490
|
....*..
gi 1229277487 478 TEIKTIT 484
Cdd:cd07083 491 LEMKAVA 497
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
13-470 |
7.29e-75 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 243.71 E-value: 7.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNSY-IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAE 91
Cdd:PRK09457 4 WINGDWIAGQGEaFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 92 SKDQGKTLTLARTMdiPRSVLNFrfFASSIQ-HHVSDCTEMSHLGCMHYTVR-TPVGIAGLISPWNLPLYLLTWKIAPAI 169
Cdd:PRK09457 84 ARETGKPLWEAATE--VTAMINK--IAISIQaYHERTGEKRSEMADGAAVLRhRPHGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 170 AAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGtGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKK 249
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 250 -LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIY-NEFLKRFVEATRKWKVGIP-SDPSANM 326
Cdd:PRK09457 239 iLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWdAEPQPFM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 327 GALISKAHLEKVRSYVTKAHAEGAKILcgegvdqLSLPLRNQAGYFMLPTVI--TDIKDESccmTEEIFGPVTCVVPFDS 404
Cdd:PRK09457 319 GAVISEQAAQGLVAAQAQLLALGGKSL-------LEMTQLQAGTGLLTPGIIdvTGVAELP---DEEYFGPLLQVVRYDD 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229277487 405 EEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNcwliRELN-----LPFGGMKSSGIGREGA 470
Cdd:PRK09457 389 FDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN----KPLTgassaAPFGGVGASGNHRPSA 455
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
50-485 |
2.81e-71 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 232.42 E-value: 2.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 50 AVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTMDI--PRSVLNFrffasSIQH---- 123
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIavVLGEIDH-----ALKHlkkw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 124 ----HVSdcTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLtwkIAP---AIAAGNTVIAKPSELTSVTAWMFCKLLDK 196
Cdd:cd07087 78 mkprRVS--VPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 197 AgVPPGVINVVFGtGPRVGEALVSHPeVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEEcipaTV 276
Cdd:cd07087 153 Y-FDPEAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEV----AA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 277 RS----SFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWkvgIPSDP--SANMGALISKAHLEKVRSYVtkahaEGA 350
Cdd:cd07087 226 RRiawgKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF---YGEDPkeSPDYGRIINERHFDRLASLL-----DDG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 351 KILCGEGVDQLSLplrnqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGR 430
Cdd:cd07087 298 KVVIGGQVDKEER--------YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAV 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229277487 431 IHRVAKRLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07087 370 QERVLAETSSGGVCVNDVLLHAAIpnLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-485 |
5.45e-71 |
|
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: 232.69 E-value: 5.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 25 IDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSP-QERSLILNRVADVLEQSLEELAQAESKDQGKTLTLAR 103
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPaHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 104 tMDIPRSVLNFRFFASSIQHHVS-----DCTEMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAK 178
Cdd:cd07148 81 -VEVTRAIDGVELAADELGQLGGreipmGLTPASA-GRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 179 PSELTSVTAWMFCKLLDKAGVPPGVINVVFgTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHcKKLSLELGGKN 258
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 259 PAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKV 338
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 339 RSYVTKAHAEGAKILCGEgvDQLSLPLrnqagyfMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYG 418
Cdd:cd07148 317 EEWVNEAVAAGARLLCGG--KRLSDTT-------YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 419 LGATVWSKDVGRIHRVAKRLQSGLVWTN-------CWlirelnLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07148 388 FQAAVFTKDLDVALKAVRRLDATAVMVNdhtafrvDW------MPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-487 |
5.09e-64 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 218.08 E-value: 5.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 12 NFIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQ 89
Cdd:PLN02419 116 NLIGGSFVESqsSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 90 AESKDQGKTLTLARTmDIPRSVLNFRFFASSIQHHVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAI 169
Cdd:PLN02419 196 NITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 170 AAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVgEALVSHPEVPVISFTGSQPTAERITQLSAPHCKK 249
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 250 LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSR-IFVQRSiyNEFLKRFVEATRKWKVGIPSDPSANMGA 328
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 329 LISKAHLEKVRSYVTKAHAEGAKILCgEGVDqLSLPlRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLL-DGRD-IVVP-GYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 409 IARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLirELNLP---FGGMKSSGIGREG--AKDSYDFFTEIKTI 483
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI--PVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
....
gi 1229277487 484 TIKY 487
Cdd:PLN02419 587 TQKQ 590
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
45-483 |
7.56e-62 |
|
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: 208.23 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 45 EEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHH 124
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 125 VSD-CTEMSHLGCMHYTVRT---PVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAgVP 200
Cdd:cd07135 85 AKDeKVKDGPLAFMFGKPRIrkePLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 201 PGVINVVFGTGPRVGEALVSHPEvpVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSF 280
Cdd:cd07135 164 PDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 281 ANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSaNMGALISKAHLEKVRSYVTKAhaeGAKILCGEGVDQ 360
Cdd:cd07135 242 GNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDTT---KGKVVIGGEMDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 361 LSLplrnqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQS 440
Cdd:cd07135 318 ATR--------FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1229277487 441 G-LVWTNCWL---IRelNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07135 390 GgVVINDTLIhvgVD--NAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
28-466 |
8.04e-62 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 218.27 E-value: 8.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPST--GEVYckvpNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEE---LAQAESkdqGKTLT-- 100
Cdd:COG4230 578 ADHSDvvGTVV----EATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAElmaLLVREA---GKTLPda 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 101 LArtmDIpRSVLNF-RFFASSIQHHvsdctemshlgCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:COG4230 651 IA---EV-REAVDFcRYYAAQARRL-----------FAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKP 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 180 SELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERIT-QLSAPHCKKLSL--ELGG 256
Cdd:COG4230 716 AEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINrTLAARDGPIVPLiaETGG 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 257 KNPAIIfeD--ANLEECIPATVRSSFANQGEIClctS--RI-FVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALIS 331
Cdd:COG4230 796 QNAMIV--DssALPEQVVDDVLASAFDSAGQRC---SalRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVID 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 332 KAHLEKVRSYVTKAHAEGAKIlcgegvDQLSLPLRNQAGYFMLPTV--ITDIKDesccMTEEIFGPVTCVVPFDSEE--E 407
Cdd:COG4230 871 AEARANLEAHIERMRAEGRLV------HQLPLPEECANGTFVAPTLieIDSISD----LEREVFGPVLHVVRYKADEldK 940
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229277487 408 VIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:COG4230 941 VIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYVNR--NIigavvgvqPFGGEGLSGTG 1001
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
38-466 |
1.77e-61 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 216.99 E-value: 1.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 38 KVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEE---LAQAESkdqGKTLTLArtMDIPRSVLNF 114
Cdd:PRK11904 578 EVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAEliaLCVREA---GKTLQDA--IAEVREAVDF 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 115 -RFFASSIQHHVSDCTEM-SHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCK 192
Cdd:PRK11904 653 cRYYAAQARRLFGAPEKLpGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVK 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 193 LLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQ-LSAPHCKKLSL--ELGGKNPAIIFEDANLE 269
Cdd:PRK11904 733 LLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRtLAARDGPIVPLiaETGGQNAMIVDSTALPE 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 270 ECIPATVRSSFANQGEIClctS--RI-FVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALI---SKAHLEkvrsyvt 343
Cdd:PRK11904 813 QVVDDVVTSAFRSAGQRC---SalRVlFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIdaeAKANLD------- 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 344 kAHAE----GAKILCgegvdQLSLPLRNQAGYFMLPTV--ITDIKDesccMTEEIFGPVTCVVPFDSEE--EVIARANGV 415
Cdd:PRK11904 883 -AHIErmkrEARLLA-----QLPLPAGTENGHFVAPTAfeIDSISQ----LEREVFGPILHVIRYKASDldKVIDAINAT 952
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229277487 416 KYGLGATVWSKDVGRIHRVAKRLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:PRK11904 953 GYGLTLGIHSRIEETADRIADRVRVG----NVYVNR--NQigavvgvqPFGGQGLSGTG 1005
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-483 |
2.24e-61 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 207.41 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 27 SYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTmD 106
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 107 IPRSVLNFRFFAssiQHHVSDCTEMSHL-----GCMHYTvrtPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSE 181
Cdd:PRK13968 90 VAKSANLCDWYA---EHGPAMLKAEPTLvenqqAVIEYR---PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 182 LTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEAlVSHPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAI 261
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQM-INDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 262 IFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSY 341
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 342 VTKAHAEGAKILCGEgvDQLSlplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGA 421
Cdd:PRK13968 323 VEATLAEGARLLLGG--EKIA-----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229277487 422 TVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PRK13968 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
32-466 |
2.93e-61 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 217.04 E-value: 2.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 32 TGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLtlARTMDIPRSV 111
Cdd:PRK11905 577 HDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTL--ANAIAEVREA 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 112 LNF-RFFASSIQHHVSDctemshlgcmhyTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMF 190
Cdd:PRK11905 655 VDFlRYYAAQARRLLNG------------PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARA 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 191 CKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHCKK---LSLELGGKNPAIIFEDAN 267
Cdd:PRK11905 723 VRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGQNAMIVDSSAL 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 268 LEECIPATVRSSFANQGEIClctS--RI-FVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTK 344
Cdd:PRK11905 803 PEQVVADVIASAFDSAGQRC---SalRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEA 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 345 AHAEGAKilcgegVDQLSLPLRNQAGYFMLPTVI--TDIKDesccMTEEIFGPVTCVVPFDSEE--EVIARANGVKYGLG 420
Cdd:PRK11905 880 MRAAGRL------VHQLPLPAETEKGTFVAPTLIeiDSISD----LEREVFGPVLHVVRFKADEldRVIDDINATGYGLT 949
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 421 ATVWSKDVGRIHRVAKRLQSGLVWTNcwliRelNL--------PFGGMKSSGIG 466
Cdd:PRK11905 950 FGLHSRIDETIAHVTSRIRAGNIYVN----R--NIigavvgvqPFGGEGLSGTG 997
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
46-466 |
1.55e-60 |
|
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: 206.30 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 46 EIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLArtMDIPRSVLNF-RFFASSIQHh 124
Cdd:TIGR01238 75 HVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA--IAEVREAVDFcRYYAKQVRD- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 125 vsDCTEMSHlgcmhytvrTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVI 204
Cdd:TIGR01238 152 --VLGEFSV---------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 205 NVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQ-----LSAPhcKKLSLELGGKNPAIIFEDANLEECIPATVRSS 279
Cdd:TIGR01238 221 QLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQtlaqrEDAP--VPLIAETGGQNAMIVDSTALPEQVVRDVLRSA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 280 FANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGAKILcgegvd 359
Cdd:TIGR01238 299 FDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIA------ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 360 QLSL--PLRNQAGYFMLPTVIT-DIKDEsccMTEEIFGPVTCVVPFDSEE--EVIARANGVKYGLGATVWSKDVGRIHRV 434
Cdd:TIGR01238 373 QLTLddSRACQHGTFVAPTLFElDDIAE---LSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWI 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 1229277487 435 AKRLQSGlvwtNCWLIREL------NLPFGGMKSSGIG 466
Cdd:TIGR01238 450 EKHARVG----NCYVNRNQvgavvgVQPFGGQGLSGTG 483
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
52-467 |
2.92e-60 |
|
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: 203.61 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 52 QAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTltlARTMDIPR--SVLnfrffaSSIQH---HVS 126
Cdd:cd07134 5 AAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP---AAEVDLTEilPVL------SEINHaikHLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 127 D-------CTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGV 199
Cdd:cd07134 76 KwmkpkrvRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 200 PPGVinVVFGTGPRVGEALVSHPeVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSS 279
Cdd:cd07134 156 EDEV--AVFEGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 280 FANQGEICLCTSRIFVQRSIYNEFLKRFVEATRK-WKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGV 358
Cdd:cd07134 233 FLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 359 DqlslplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRL 438
Cdd:cd07134 313 D--------AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
410 420 430
....*....|....*....|....*....|.
gi 1229277487 439 QSGLVWTNCWLIREL--NLPFGGMKSSGIGR 467
Cdd:cd07134 385 SSGGVVVNDVVLHFLnpNLPFGGVNNSGIGS 415
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
14-464 |
8.39e-60 |
|
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: 204.74 E-value: 8.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 14 IGGKFLPCNSYIDSYDPST-GEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSL-EELAQAE 91
Cdd:cd07123 37 IGGKEVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAAT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 92 SKDQGKTLTLARTMDIPRSVLNFRF---FASSIQHHVSDCTEMSHLGCMHYtvRTPVGIAGLISPWN-------LPLyll 161
Cdd:cd07123 117 MLGQGKNVWQAEIDAACELIDFLRFnvkYAEELYAQQPLSSPAGVWNRLEY--RPLEGFVYAVSPFNftaiggnLAG--- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 162 twkiAPAIAaGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQ 241
Cdd:cd07123 192 ----APALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 242 LSA---------PhckKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATR 312
Cdd:cd07123 267 QIGenldryrtyP---RIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 313 KWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAE-GAKILCGEGVDqlslplrNQAGYFMLPTVI--TDIKDESccMT 389
Cdd:cd07123 344 EIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCD-------DSVGYFVEPTVIetTDPKHKL--MT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 390 EEIFGPVTCV-VPFDSE-EEVIARANGV-KYGLGATVWSKDVGRIHRVAKRLQ--SGLVWTNC----WLIRElnLPFGGM 460
Cdd:cd07123 415 EEIFGPVLTVyVYPDSDfEETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDkptgAVVGQ--QPFGGA 492
|
....
gi 1229277487 461 KSSG 464
Cdd:cd07123 493 RASG 496
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
28-485 |
9.92e-58 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 198.83 E-value: 9.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 28 YDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTmDI 107
Cdd:PLN00412 36 TNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVT-EV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 108 PRS--VLNF------RFFASSiQHHVSDC---TEMSHLgCMhyTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVI 176
Cdd:PLN00412 115 VRSgdLISYtaeegvRILGEG-KFLVSDSfpgNERNKY-CL--TSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 177 AKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQpTAERItqlsaphCKK-----LS 251
Cdd:PLN00412 191 LKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGIAI-------SKKagmvpLQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 252 LELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDpSANMGALIS 331
Cdd:PLN00412 263 MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 332 KAHLEKVRSYVTKAHAEGAKiLCGEgvdqlslplRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIAR 411
Cdd:PLN00412 342 ESSANFIEGLVMDAKEKGAT-FCQE---------WKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHH 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229277487 412 ANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELN-LPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:PLN00412 412 CNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKSTVI 486
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
129-483 |
6.10e-57 |
|
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: 195.42 E-value: 6.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 129 TEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLtwkIAP---AIAAGNTVIAKPSELTSVTAWMFCKLLDKAgVPPGVIN 205
Cdd:cd07136 85 TPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 206 VVFGtGPRVGEALVSHPeVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGE 285
Cdd:cd07136 161 VVEG-GVEENQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 286 ICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDpSANMGALISKAHLEKVRSYVtkahaEGAKILCGEGVDQLSLpl 365
Cdd:cd07136 239 TCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETL-- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 366 rnqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWT 445
Cdd:cd07136 311 ------YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCI 384
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1229277487 446 NCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07136 385 NDTIMHLANpyLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
45-486 |
1.48e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 195.63 E-value: 1.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 45 EEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTMDIPRSVLNFRFFASSIQHH 124
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 125 VS----DCTEMSHLGcMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAgVP 200
Cdd:PTZ00381 87 LKpekvDTVGVFGPG-KSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 201 PGVINVVFGtGPRVGEALVSHPeVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSF 280
Cdd:PTZ00381 165 PSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 281 ANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWkvgIPSDP--SANMGALISKAHLEKVRSYVtKAHaeGAKILCGEGV 358
Cdd:PTZ00381 243 LNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF---FGEDPkkSEDYSRIVNEFHTKRLAELI-KDH--GGKVVYGGEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 359 DqlslplrnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRL 438
Cdd:PTZ00381 317 D--------IENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENT 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1229277487 439 QSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:PTZ00381 389 SSGAVVINDCVFHLLNpnLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
55-483 |
2.30e-56 |
|
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: 193.47 E-value: 2.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 55 REAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKtltlartmdipRSVLNFRF--FASSIQH------HVS 126
Cdd:cd07133 8 KAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGH-----------RSRHETLLaeILPSIAGikharkHLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 127 DC-------TEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLtwkIAP---AIAAGNTVIAKPSELTSVTAWMFCKLLDK 196
Cdd:cd07133 77 KWmkpsrrhVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 197 AGvPPGVINVVFGtGPRVGEALVS----HpevpvISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECI 272
Cdd:cd07133 154 YF-DEDEVAVVTG-GADVAAAFSSlpfdH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 273 PATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPsaNMGALISKAHLEKVRSYVTKAHAEGAKI 352
Cdd:cd07133 227 ERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNP--DYTSIINERHYARLQGLLEDARAKGARV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 353 L-CGEGVDQLSlplrnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRI 431
Cdd:cd07133 305 IeLNPAGEDFA------ATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQ 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 432 HRVAKRLQSGLVWTNCWLIREL--NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07133 379 DRVLRRTHSGGVTINDTLLHVAqdDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
14-464 |
1.37e-55 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 193.85 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 14 IGGK-FLPCNSYIDSYDPST-GEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSL-EELAQA 90
Cdd:TIGR01236 36 IGGEeVYDSNERIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLSGPYrYEILAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 91 ESKDQGKTLTLARTMDIPRSVLNFRFFAssiqHHVSDCTE---MSHLGCMHYTVRTPV-GIAGLISPWNLPLYLLTWKIA 166
Cdd:TIGR01236 116 TMLGQSKTVYQAEIDAVAELIDFFRFNV----KYARELYAqqpISAPGEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 167 PAIAaGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPH 246
Cdd:TIGR01236 192 PALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 247 CKK------LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPS 320
Cdd:TIGR01236 271 LDRyhnfprIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 321 DPSANMGALISKAHLEKVRSYV--TKAHAEGAKILCGEGVDqlslplrNQAGYFMLPTVI--TDIKDESccMTEEIFGPV 396
Cdd:TIGR01236 351 DFRGFMGAVIDEQSFDKIVKYIedAKKDPEALTILYGGKYD-------DSQGYFVEPTVVesKDPDHPL--MSEEIFGPV 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229277487 397 TCVVPFDSEE-----EVIarANGVKYGLGATVWSKDVGRIHRVAKRLQ--SGLVWTN--CWLIRELNLPFGGMKSSG 464
Cdd:TIGR01236 422 LTVYVYPDDKykeilDLV--DSTSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINdkCTGAVVGQQPFGGARMSG 496
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
45-466 |
3.50e-49 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 181.71 E-value: 3.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 45 EEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLArtmdIP--RSVLNF-RFFASSI 121
Cdd:PRK11809 682 AEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNA----IAevREAVDFlRYYAGQV 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 122 QHHVSDCTemshlgcmHytvrTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPP 201
Cdd:PRK11809 758 RDDFDNDT--------H----RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPA 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 202 GVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAeRITQLS-------APHCKKLSLELGGKNPAIIFEDANLEECIPA 274
Cdd:PRK11809 826 GVVQLLPGRGETVGAALVADARVRGVMFTGSTEVA-RLLQRNlagrldpQGRPIPLIAETGGQNAMIVDSSALTEQVVAD 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 275 TVRSSFANQGEIC-----LCtsrifVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALI---SKAHLEKvrsyvtkaH 346
Cdd:PRK11809 905 VLASAFDSAGQRCsalrvLC-----LQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIdaeAKANIER--------H 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 347 AEG--AKilcGEGVDQLSLP--LRNQAGYFMLPTVIT-DIKDEsccMTEEIFGPVTCVVPFDSEE--EVIARANGVKYGL 419
Cdd:PRK11809 972 IQAmrAK---GRPVFQAAREnsEDWQSGTFVPPTLIElDSFDE---LKREVFGPVLHVVRYNRNQldELIEQINASGYGL 1045
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1229277487 420 GATVWSKDVGRIHRVAKRLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:PRK11809 1046 TLGVHTRIDETIAQVTGSAHVG----NLYVNR--NMvgavvgvqPFGGEGLSGTG 1094
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-487 |
8.40e-45 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 164.24 E-value: 8.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 13 FIGGKFLPCNSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAES 92
Cdd:PLN02315 24 YVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 93 KDQGKTLtlARTMDIPRSVLNFRFFASSIQHHVSDCTEMSHL-GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAA 171
Cdd:PLN02315 104 LEMGKIL--AEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 172 GNTVIAKPSELTSVTAWMFCKL----LDKAGVPPGVINVVFGtGPRVGEALVSHPEVPVISFTGSQPTAERITQLSAPHC 247
Cdd:PLN02315 182 GNCVVWKGAPTTPLITIAMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 248 KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDPSANMG 327
Cdd:PLN02315 261 GKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 328 ALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQlslplrnQAGYFMLPTVItDIKDESCCMTEEIFGPVTCVVPFDSEEE 407
Cdd:PLN02315 341 PLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE-------SEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 408 VIARANGVKYGLGATVWSKDVGRIHRVAkrlqsGLVWTNCWLIrELNLP---------FGGMKSSGIGREGAKDSYDFFT 478
Cdd:PLN02315 413 AIEINNSVPQGLSSSIFTRNPETIFKWI-----GPLGSDCGIV-NVNIPtngaeiggaFGGEKATGGGREAGSDSWKQYM 486
|
....*....
gi 1229277487 479 EIKTITIKY 487
Cdd:PLN02315 487 RRSTCTINY 495
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
50-486 |
2.32e-43 |
|
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: 158.92 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 50 AVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLARTMDIpRSVLNfrffasSIQHHVSDCT 129
Cdd:cd07132 3 AVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEI-LLVKN------EIKYAISNLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 130 E----------MSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKL----LD 195
Cdd:cd07132 76 EwmkpepvkknLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELipkyLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 196 KAGVPpgvinVVFGTGPRVGEAL---VSHpevpvISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEeci 272
Cdd:cd07132 156 KECYP-----VVLGGVEETTELLkqrFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDID--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 273 pATVR----SSFANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWkVGIPSDPSANMGALISKAHLEKVRSYVtkahaE 348
Cdd:cd07132 223 -VAARriawGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLL-----S 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 349 GAKILCGEGVDQLSLplrnqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDV 428
Cdd:cd07132 296 GGKVAIGGQTDEKER--------YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNK 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 429 GRIHRVAKRLQSGLVWTNCWLIREL--NLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:cd07132 368 KVINKILSNTSSGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
144-483 |
3.99e-37 |
|
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: 141.39 E-value: 3.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 144 PVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAgVPPGVINVVFGtGPRVGEALVSHpE 223
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 224 VPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSF-ANQGEICLCTSRIFVQRSIYNE 302
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 303 FLKRFVEATRKWkVGIPSDPSANMGALISKAHLEKVrSYVTKAHAEGAKILCGEGVDQLSLplrnqagyFMLPTVITDIK 382
Cdd:cd07137 258 LIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRL-SRLLDDPSVADKIVHGGERDEKNL--------YIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 383 DESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRELN--LPFGGM 460
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIdtLPFGGV 407
|
330 340
....*....|....*....|...
gi 1229277487 461 KSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07137 408 GESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
48-448 |
3.82e-32 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 127.74 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 48 EVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLArtMDIPRSVLNFRFFASSIQ----H 123
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA--ENICGDQVQLRARAFVIYsyriP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 124 HVSDCTEMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAG-VPPG 202
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 203 VINVVFGTGpRVGEALVSHPEVPVISFTGSQPTAERItqLSAPHCKKLSLELGGKNPAIIFEDAN-----LEECipatVR 277
Cdd:cd07084 160 DVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQavdyvAWQC----VQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 278 SSFANQGEICLCTSRIFVQRsiyNEFLKRFVEATrKWKVGIPSDPSANMGALIS---KAHLEKVRSYVTKAHAEGAKILC 354
Cdd:cd07084 233 DMTACSGQKCTAQSMLFVPE---NWSKTPLVEKL-KALLARRKLEDLLLGPVQTfttLAMIAHMENLLGSVLLFSGKELK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 355 GEGVDQLSLPLRNQAGYfmlpTVITDIKDESCCMTEEIFGPVTCVVPF--DSEEEVIARANGVKYGLGATVWSKDVGRIH 432
Cdd:cd07084 309 NHSIPSIYGACVASALF----VPIDEILKTYELVTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFLQ 384
|
410
....*....|....*..
gi 1229277487 433 RVAKRLQS-GLVWTNCW 448
Cdd:cd07084 385 ELIGNLWVaGRTYAILR 401
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
47-439 |
1.99e-31 |
|
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: 125.73 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 47 IEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEEL---AQAESKdqgktLTLAR-TMDIPRSVLNFRFFAS--- 119
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELvarAHAETG-----LPEARlQGELGRTTGQLRLFADlvr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 120 -------SIQHHVSDCTEMSHLGcmHYTVRTPVGIAGLISPWNLPLYLLTW--KIAPAIAAGNTVIAKP-------SELT 183
Cdd:cd07129 76 egswldaRIDPADPDRQPLPRPD--LRRMLVPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAhpahpgtSELV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 184 SVTAwmfCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQLSA--PHCKKLSLELGGKNPAI 261
Cdd:cd07129 154 ARAI---RAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAarPEPIPFYAELGSVNPVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 262 IFEDAnLEECiPATVRSSFA-----NQGEICLCTSRIFVQRSiynEFLKRFVEATRKWKVGIPSDPSANMGalISKAHLE 336
Cdd:cd07129 231 ILPGA-LAER-GEAIAQGFVgsltlGAGQFCTNPGLVLVPAG---PAGDAFIAALAEALAAAPAQTMLTPG--IAEAYRQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 337 KVRSyvTKAHAeGAKILCGEGVDqlslPLRNQAGYFMLPTVITD-IKDESccMTEEIFGPVTCVVPFDSEEEVIARANGV 415
Cdd:cd07129 304 GVEA--LAAAP-GVRVLAGGAAA----EGGNQAAPTLFKVDAAAfLADPA--LQEEVFGPASLVVRYDDAAELLAVAEAL 374
|
410 420
....*....|....*....|....*.
gi 1229277487 416 KYGLGATVWS--KDVGRIHRVAKRLQ 439
Cdd:cd07129 375 EGQLTATIHGeeDDLALARELLPVLE 400
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
144-484 |
2.77e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 125.99 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 144 PVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAgVPPGVINVVFGtGPRVGEALVSHPE 223
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 224 VPVIsFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVR------SSFAnqGEICLCTSRIFVQR 297
Cdd:PLN02203 186 DKIF-FTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTKVAVNRivggkwGSCA--GQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 298 SiYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVtKAHAEGAKILCGEGVDQLSLplrnqagyFMLPTV 377
Cdd:PLN02203 263 R-FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLL-KDPRVAASIVHGGSIDEKKL--------FIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 378 ITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIREL--NL 455
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSL 412
|
330 340
....*....|....*....|....*....
gi 1229277487 456 PFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:PLN02203 413 PFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
10-435 |
3.58e-28 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 117.50 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 10 LENFIGGKFLPCN-SYIDSYDPSTGEVYCKVPNSGKEeIEVAVQAARE-AFPAWSSRSPQERSLILNRVADVLEQSLEEL 87
Cdd:PRK11903 5 LANYVAGRWQAGSgAGTPLFDPVTGEELVRVSATGLD-LAAAFAFAREqGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 88 AQAESKDQGKTLTLArTMDIPRSVLNFRFFAS-----SIQHHVSDcTEMSHLG------CMHYTVRTPvGIAGLISPWNL 156
Cdd:PRK11903 84 YDIATANSGTTRNDS-AVDIDGGIFTLGYYAKlgaalGDARLLRD-GEAVQLGkdpafqGQHVLVPTR-GVALFINAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 157 PLYLLTWKIAPAIAAGNTVIAKPSeltSVTAWM---FCKLLDKAGV-PPGVINVVFGTGPRVGEALvshPEVPVISFTGS 232
Cdd:PRK11903 161 PAWGLWEKAAPALLAGVPVIVKPA---TATAWLtqrMVKDVVAAGIlPAGALSVVCGSSAGLLDHL---QPFDVVSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 233 QPTAERITQLSA--PHCKKLSLELGGKNPAIIFEDAN-----LEECIPATVRSSFANQGEICLCTSRIFVQRSIYNEFLK 305
Cdd:PRK11903 235 AETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 306 RFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVTKAHAEGAKILCGEGVDQLSLPlrNQAGYFMLPT--VITDIKD 383
Cdd:PRK11903 315 ALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVDAD--PAVAACVGPTllGASDPDA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1229277487 384 ESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVA 435
Cdd:PRK11903 393 ATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
10-432 |
3.59e-27 |
|
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: 114.29 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 10 LENFIGGKFL-PCNSYIDSYDPSTGEVYCKVPNSGKEeIEVAVQAARE-AFPAWSSRSPQERSLILNRVADVLEQSLEEL 87
Cdd:cd07128 1 LQSYVAGQWHaGTGDGRTLHDAVTGEVVARVSSEGLD-FAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 88 AQ------AESKD-----QGKTLTLARTMDIPRSVLNFRFFassiqHHVSDCTEMSHLGCM---HytVRTPV-GIAGLIS 152
Cdd:cd07128 80 YAlsaatgATRRDswidiDGGIGTLFAYASLGRRELPNAHF-----LVEGDVEPLSKDGTFvgqH--ILTPRrGVAVHIN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 153 PWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGV-PPGVINVVFGTgprVGEALVSHPEVPVISFTG 231
Cdd:cd07128 153 AFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQDVVAFTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 232 SQPTAER------ITQLSAPhckkLSLELGGKNPAIIFEDANleeciPAT----------VRSSFANQGEICLCTSRIFV 295
Cdd:cd07128 230 SAATAAKlrahpnIVARSIR----FNAEADSLNAAILGPDAT-----PGTpefdlfvkevAREMTVKAGQKCTAIRRAFV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 296 QRSIYNEFLKRFVEATRKWKVGIPSDPSANMGALISKAHLEKVRSYVtKAHAEGAKILCGEGVDQLSLPLRNQAGYFMLP 375
Cdd:cd07128 301 PEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVGADAEKGAFFPP 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229277487 376 TVIT--DIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKD--------------VGRIH 432
Cdd:cd07128 380 TLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafarelvlgaapyHGRLL 452
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
141-483 |
2.01e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 108.98 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 141 VRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAgVPPGVINVVFGTGPRVGEALvs 220
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALL-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 221 HPEVPVISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEecipATVRSSFA-----NQGEICLCTSRIFV 295
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLK----VTVRRIIAgkwgcNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 296 QRsiynEFLKRFVEATRK-WKVGIPSDP--SANMGALISKAHLEKVRSYVTKAHAEGAKILCGEgvdqlslplRNQAGYF 372
Cdd:PLN02174 262 TK----EYAPKVIDAMKKeLETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGE---------KDRENLK 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 373 MLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKYGLGATVWSKDVGRIHRVAKRLQSGLVWTNCWLIRE 452
Cdd:PLN02174 329 IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHL 408
|
330 340 350
....*....|....*....|....*....|...
gi 1229277487 453 L--NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PLN02174 409 AlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
12-434 |
2.42e-17 |
|
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: 84.47 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 12 NFIGGKFLPCNSYIDSYDPSTGEVYCKVPNSGKEEIEVAVQAAReAFPAWSSRSP---QERSLILnrvADVLEQSLEELA 88
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLR-QCPKSGLHNPlknPERYLLY---GDVSHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 89 QAESKDQGKTLTlARTMdiPRS--------------VLNF-----RFFASSIQhhVSDctemSHLGCMHYTVRTPVGIAG 149
Cdd:cd07126 77 KPEVEDFFARLI-QRVA--PKSdaqalgevvvtrkfLENFagdqvRFLARSFN--VPG----DHQGQQSSGYRWPYGPVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 150 LISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMFCKLLDKAGVPPGVINVVFGTGPRVGEaLVSHPEVPVISF 229
Cdd:cd07126 148 IITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK-ILLEANPRMTLF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 230 TGSQPTAERitqlsaphckkLSLELGGKnpaIIFEDANLEECI--PATV----------RSSFANQGEICLCTSRIFVQR 297
Cdd:cd07126 227 TGSSKVAER-----------LALELHGK---VKLEDAGFDWKIlgPDVSdvdyvawqcdQDAYACSGQKCSAQSILFAHE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 298 SIYNE-FLKRFVEATRKWKVgipSD----PSANMGALISKAHLEKVrsyvtkAHAEGAKILCGegvdqlSLPLRNQ---A 369
Cdd:cd07126 293 NWVQAgILDKLKALAEQRKL---EDltigPVLTWTTERILDHVDKL------LAIPGAKVLFG------GKPLTNHsipS 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229277487 370 GY-FMLPTVI------TDIKDESCCMTEEIFGPVTCVVPFDSEEE--VIARANGVKYGLGATVWSKDVGRIHRV 434
Cdd:cd07126 358 IYgAYEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
52-322 |
1.71e-14 |
|
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: 74.95 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 52 QAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTL-----TLARTMDIPRSVLNFRFFAS----SIQ 122
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIrsliaNWIAMMGCSESKLYKNIDTErgitASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 123 HHVSDCTEMSHLGCmhYTVRTPVGIAGLISPWNLPLYLLTwKIAPAIAAGNTVIAKPSELTSVTAWMFCKLL---DKAGV 199
Cdd:cd07077 81 GHIQDVLLPDNGET--YVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFqaaDAAHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 200 PPGVINVVFGTGPRVGEALVSHPEVPVISFTGSqPTAERITQLSAPHckKLSLELGGKNPAIIFEDANLEECIPATVRSS 279
Cdd:cd07077 158 PKILVLYVPHPSDELAEELLSHPKIDLIVATGG-RDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1229277487 280 FANQGEICLCTSRIFVQRSIYNEFLKRFVEATRKWKVGIPSDP 322
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQET 277
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
46-425 |
6.88e-14 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 74.05 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 46 EIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGKTLTLArtmdiprsvlnfrFFASSiqHHV 125
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMA-------------FQAGG--PHA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 126 SDC---------TEMS---HLGCMH--------------YTVrTPVGIAGLISPWNLPlyllTWKIAPA----IAAGNTV 175
Cdd:cd07127 150 QDRgleavayawREMSripPTAEWEkpqgkhdplamektFTV-VPRGVALVIGCSTFP----TWNGYPGlfasLATGNPV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 176 IAKPSELTSVTAWMFCK----LLDKAGVPPGVIN-VVFGTGPRVGEALVSHPEVPVISFTGSQPTAERITQlsapHCKKL 250
Cdd:cd07127 225 IVKPHPAAILPLAITVQvareVLAEAGFDPNLVTlAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEA----NARQA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 251 SL--ELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRS---------IYNEFLKRFVEATRKWkVGIP 319
Cdd:cd07127 301 QVytEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADP 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 320 SDPSANMGALISKAHLEKvrsyVTKAHAEGAKILCGEGVDQLSLP---LRNqagyfmlPTVITDIKDESCCMTEEIFGPV 396
Cdd:cd07127 380 ARAAALLGAIQSPDTLAR----IAEARQLGEVLLASEAVAHPEFPdarVRT-------PLLLKLDASDEAAYAEERFGPI 448
|
410 420
....*....|....*....|....*....
gi 1229277487 397 TCVVPFDSEEEVIARANGVKYGLGATVWS 425
Cdd:cd07127 449 AFVVATDSTDHSIELARESVREHGAMTVG 477
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
50-434 |
2.07e-08 |
|
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: 56.51 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 50 AVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGktltLARTMDiprSVLNFRFFASSIQHHVSD-- 127
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETG----MGRVED---KVIKNHFAAEYIYNVYKDek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 128 ----CTEMSHLGCMhyTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP----SELTSVTAWMFCKLLDKAGV 199
Cdd:cd07081 77 tcgvLTGDENGGTL--IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 200 PPGVINVVFGTGPRVGEALVSHPEVPVISFTGsqptAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSS 279
Cdd:cd07081 155 PENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 280 FANQGEICLCTSRIFVQRSIYNEFLKRFVEatrkwkvgipsdpsaNMGALISKAHLEKVRSYVTKAHAEGAKIlcgegVD 359
Cdd:cd07081 231 TFDNGVICASEQSVIVVDSVYDEVMRLFEG---------------QGAYKLTAEELQQVQPVILKNGDVNRDI-----VG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 360 QLSLPLRNQAGyFMLPT------VITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIARANGVKY--GLGAT--VWSKDVG 429
Cdd:cd07081 291 QDAYKIAAAAG-LKVPQetriliGEVTSLAEHEPFAHEKLSPVLAMYRAANFADADAKALALKLegGCGHTsaMYSDNIK 369
|
....*
gi 1229277487 430 RIHRV 434
Cdd:cd07081 370 AIENM 374
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
144-448 |
4.27e-07 |
|
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: 52.11 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 144 PVG-IAGLI---SPWNLPLYlltwKIAPAIAAGNTVIAKPSELTSVTAWMFCKLL----DKAGVPPGVINVVFGTGPRVG 215
Cdd:cd07122 95 PVGvIAALIpstNPTSTAIF----KALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIEEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 216 EALVSHPEVPVISFTGSQPTAEritqlSAPHCKKLSLELG-GKNPAIIFEDANLEECIPATVRS-SFANqGEICLCTSRI 293
Cdd:cd07122 171 QELMKHPDVDLILATGGPGMVK-----AAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 294 FVQRSIYNEFLKRFveatrkwkvgipsdpSANMGALISKAHLEKVRSYVTKahaeGAKILCGEGVDQLSLPLRNQAGyFM 373
Cdd:cd07122 245 IVDDEIYDEVRAEL---------------KRRGAYFLNEEEKEKLEKALFD----DGGTLNPDIVGKSAQKIAELAG-IE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 374 LP---TVI----TDIKDEScCMTEEIFGPVTCVVPFDSEEEVIARANG-VKY-GLGAT--VWSKDVGRIHRVAKRLQSGL 442
Cdd:cd07122 305 VPedtKVLvaeeTGVGPEE-PLSREKLSPVLAFYRAEDFEEALEKARElLEYgGAGHTavIHSNDEEVIEEFALRMPVSR 383
|
....*.
gi 1229277487 443 VWTNCW 448
Cdd:cd07122 384 ILVNTP 389
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
45-439 |
9.04e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 47.97 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 45 EEIEVAVQAAREAFPAWSSRSPQERSLILNRVADVLEQSLEELAQAESKDQGktltLARTMDiprsvlnfrffasSIQHH 124
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG----MGRVED-------------KIAKN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 125 VSDCTEMSHLGCMHYTVRT-----------PVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVI------AKpseltSVTA 187
Cdd:PRK15398 99 VAAAEKTPGVEDLTTEALTgdngltlieyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVfsphpgAK-----KVSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 188 W---MFCKLLDKAGVPPGVINVVFGTGPRVGEALVSHPEVPVISFTGSQPTAEriTQLSAPhcKKLSLELGGKNPAIIFE 264
Cdd:PRK15398 174 RaieLLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVK--AAMKSG--KKAIGAGAGNPPVVVDE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 265 DANLEECIPATVRS-SFANQgEICLCTSRIFVQRSIYNEFLKRFVEAtrkwkvgipsdpsanmGA-LISKAHLEKVRSYV 342
Cdd:PRK15398 250 TADIEKAARDIVKGaSFDNN-LPCIAEKEVIVVDSVADELMRLMEKN----------------GAvLLTAEQAEKLQKVV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229277487 343 TKAH---------------AEGAKILCGEGVDqlslplrnqagyfmLPTVITDIKDEscCMTEEIFGPVTCVVPFDSEEE 407
Cdd:PRK15398 313 LKNGgtvnkkwvgkdaakiLEAAGINVPKDTR--------------LLIVETDANHP--FVVTELMMPVLPVVRVKDVDE 376
|
410 420 430
....*....|....*....|....*....|....
gi 1229277487 408 VIARANGVKYGL--GATVWSKDVGRIHRVAKRLQ 439
Cdd:PRK15398 377 AIALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| |
