|
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: 783.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 27 SYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMD 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 107 IPRSVLNFRFFASSNLHHVSECTQMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVT 186
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 187 AWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 266
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 267 NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQ 346
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 347 TEGARILCGEGVDQLSlplRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSK 426
Cdd:cd07093 320 AEGATILTGGGRPELP---DLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 30520135 427 DVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 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: 606.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 10 LENFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEEL 87
Cdd:COG1012 6 YPLFIGGEWVAAASgeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 88 AQAESKDQGKTLTLARtMDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAP 167
Cdd:COG1012 86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 168 AIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 247
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 248 KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMG 327
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 328 ALISKAHLEKVRSYVLKAQTEGARILCGeGVdqlslPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEE 407
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTG-GR-----RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 408 VITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 30520135 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: 578.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 20 PCNSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTL 99
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 100 TLARTmDIPRSVLNFRFFASSnLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:pfam00171 84 AEARG-EVDRAIDVLRYYAGL-ARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 180 SEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVR 339
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 340 SYVLKAQTEGARILCGeGVDQLSlplrnqAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGL 419
Cdd:pfam00171 322 KYVEDAKEEGAKLLTG-GEAGLD------NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30520135 420 AATVWSKDVGRIHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTgDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
58-485 |
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: 532.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASSNLHHVSECTQMSHLGCM 137
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEVIPSPDPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 138 HYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEA 217
Cdd:cd07078 90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 218 LVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQR 297
Cdd:cd07078 170 LASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 298 SIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQlslplrNQAGYFMLPTV 377
Cdd:cd07078 250 SIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE------GGKGYFVPPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 378 ITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLI-RELNLP 456
Cdd:cd07078 324 LTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAP 403
|
410 420
....*....|....*....|....*....
gi 30520135 457 FGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07078 404 FGGVKQSGIGREGGPYGLEEYTEPKTVTI 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: 518.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 10 LENFIGGKFLPCNSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPA-WSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:TIGR03216 1 IRNFINGAFVESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALKGpWGKMTVAERADLLYAVADEIERRFDDFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSNLHHVSECTQMSH---LGCMHYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:TIGR03216 81 AAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTECFEMATpdgKGALNYAVRKPLGVVGVISPWNLPLLLMTWKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 166 APAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGP-RVGEALVSHPEVPLISFTGSQPTAERITQLSA 244
Cdd:TIGR03216 161 GPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSAIMKAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 245 PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSA 324
Cdd:TIGR03216 241 DGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 325 NMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQLSLPLRNqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDS 404
Cdd:TIGR03216 321 NMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVPDFGDALAG--GAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 405 EEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVC 478
|
..
gi 30520135 485 IK 486
Cdd:TIGR03216 479 IK 480
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-485 |
4.92e-176 |
|
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: 502.08 E-value: 4.92e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 27 SYDPSTGEVYCKVPNSGKEEIEAAVEAAREAF--PAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTL--TLA 102
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIreTRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 103 RTMDIPRSvlnFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEM 182
Cdd:cd07114 81 QVRYLAEW---YRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 183 TSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 263 FEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYV 342
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 343 LKAQTEGARILCGeGVdQLSLPLRNqAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAAT 422
Cdd:cd07114 318 ARAREEGARVLTG-GE-RPSGADLG-AGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30520135 423 VWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
13-485 |
4.28e-174 |
|
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: 497.89 E-value: 4.28e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSR--SPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07091 7 FINNEFVDSVSgkTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA--SSNLHHVSECTQMSHLGcmhYTVRTPVGIAGLISPWNLPLYLLTWKIA 166
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAgwADKIQGKTIPIDGNFLA---YTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 167 PAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-P 245
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSAN 325
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 326 MGALISKAHLEKVRSYVLKAQTEGARILCGEGVdqlslplRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGER-------HGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 406 EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07091 397 DEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
10-485 |
3.19e-170 |
|
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: 488.55 E-value: 3.19e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 10 LENFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEEL 87
Cdd:TIGR02299 1 IGHFIDGEFVPSESgeTFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 88 AQAESKDQGKTLTLARTMdIPRSVLNFRFFASSNLHHVSECT--QMSHLgcmHYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQ-VIRAAENFRFFADKCEEAMDGRTypVDTHL---NYTVRVPVGPVGLITPWNAPFMLSTWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 166 APAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAP 245
Cdd:TIGR02299 157 APALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSAN 325
Cdd:TIGR02299 237 TLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 326 MGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQLSLPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSE 405
Cdd:TIGR02299 317 VGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTFRGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 406 EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:TIGR02299 397 EEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVAL 476
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-485 |
4.53e-169 |
|
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: 484.24 E-value: 4.53e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 28 YDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARtMDI 107
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 108 PRSVLNFRFFASsnlhhvsECTQM-------SHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPS 180
Cdd:cd07103 81 DYAASFLEWFAE-------EARRIygrtipsPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 181 EMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 260
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 261 IIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRS 340
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 341 YVLKAQTEGARILCGEGVDQLslplrnqAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLA 420
Cdd:cd07103 314 LVEDAVAKGAKVLTGGKRLGL-------GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30520135 421 ATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07103 387 AYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
29-483 |
7.54e-158 |
|
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: 455.75 E-value: 7.54e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 29 DPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMDIP 108
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 109 RSVLNFRFFASSnlhhvseCTQMS------HLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEM 182
Cdd:cd07115 83 RAADTFRYYAGW-------ADKIEgevipvRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 183 TSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07115 156 TPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 263 FEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYV 342
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 343 LKAQTEGARILC-GEGVDqlslplrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAA 421
Cdd:cd07115 316 DVGREEGARLLTgGKRPG--------ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30520135 422 TVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07115 388 GVWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-483 |
9.76e-157 |
|
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: 452.91 E-value: 9.76e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 28 YDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARtMDI 107
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 108 PRSVLNFRFFA--SSNLHhvSECTQMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSV 185
Cdd:cd07090 81 DSSADCLEYYAglAPTLS--GEHVPLPG-GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 186 TAWMFCKLLDKAGVPPGVINIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 265
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 266 ANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKA 345
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 346 QTEGARILCGEGVDQLSLPLRNqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWS 425
Cdd:cd07090 317 KQEGAKVLCGGERVVPEDGLEN--GFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 30520135 426 KDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-484 |
1.15e-156 |
|
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: 453.11 E-value: 1.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 12 NFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQ 89
Cdd:cd07138 1 FYIDGAWVAPAGteTIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 90 AESKDQGKTLTLARTMDIPRSVLNFRFFASSnlhhvsectqmshLGCMHYT--------VRTPVGIAGLISPWNLPLYLL 161
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADA-------------LKDFEFEerrgnslvVREPIGVCGLITPWNWPLNQI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 162 TWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQ 241
Cdd:cd07138 148 VLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 242 LSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSD 321
Cdd:cd07138 228 AAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 322 PSANMGALISKAHLEKVRSYVLKAQTEGARILCG-----EGVDQlslplrnqaGYFMLPTVITDIKDESRCMTEEIFGPV 396
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGgpgrpEGLER---------GYFVKPTVFADVTPDMTIAREEIFGPV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 397 TCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNcWLIRELNLPFGGMKSSGIGREGAKDSYDF 476
Cdd:cd07138 379 LSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEE 457
|
....*...
gi 30520135 477 FTEIKTIT 484
Cdd:cd07138 458 FLEVKSIQ 465
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-485 |
2.67e-155 |
|
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: 450.22 E-value: 2.67e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAF--PAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07119 1 YIDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTmDIPRSVLNFRFFASsnLHHVSECTQMSHLGCMH-YTVRTPVGIAGLISPWNLPLYLLTWKIAP 167
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAG--LATKETGEVYDVPPHVIsRTVREPVGVCGLITPWNYPLLQAAWKLAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 168 AIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 247
Cdd:cd07119 158 ALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 248 KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMG 327
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 328 ALISKAHLEKVRSYVLKAQTEGARILCGEgvdqlSLPLRN--QAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGG-----KRPTGDelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 406 EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-485 |
5.57e-154 |
|
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: 446.28 E-value: 5.57e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 26 DSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPA--WSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLAR 103
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 104 TMDIPRSVLNFRFFASSnLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMT 183
Cdd:cd07112 85 AVDVPSAANTFRWYAEA-IDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 184 SVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-PHCKKLSLELGGKNPAII 262
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 263 FEDA-NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSY 341
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 342 VLKAQTEGARILCGEGVDQLslplrNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAA 421
Cdd:cd07112 324 IESGKAEGARLVAGGKRVLT-----ETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30520135 422 TVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-487 |
9.42e-151 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 438.70 E-value: 9.42e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 11 ENFIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07559 2 DNFINGEWVAPskGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFAS------SNLHHVSECTqmshlgcMHYTVRTPVGIAGLISPWNLPLYLLT 162
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGviraqeGSLSEIDEDT-------LSYHFHEPLGVVGQIIPWNFPLLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 163 WKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQL 242
Cdd:cd07559 155 WKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 243 SAPHCKKLSLELGGKNPAIIFEDANLEEC------IPATVRSSFaNQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKV 316
Cdd:cd07559 234 AAENLIPVTLELGGKSPNIFFDDAMDADDdfddkaEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 317 GVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQLSlplRNQAGYFMLPTVITDIKDESRCMTEEIFGPV 396
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLG---GLDKGYFYEPTLIKGGNNDMRIFQEEIFGPV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 397 TCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDF 476
Cdd:cd07559 390 LAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDH 469
|
490
....*....|.
gi 30520135 477 FTEIKTITIKY 487
Cdd:cd07559 470 YQQTKNILVSY 480
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-486 |
6.19e-149 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 433.57 E-value: 6.19e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 8 LMLENFIGGKFLPCN-SYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEE 86
Cdd:PRK13473 1 MQTKLLINGELVAGEgEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 87 LAQAESKDQGKTLTLARTMDIPRSVLNFRFFA--SSNLH----------HVSectqmshlgcmhYTVRTPVGIAGLISPW 154
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAgaARCLEgkaageylegHTS------------MIRRDPVGVVASIAPW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 155 NLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQP 234
Cdd:PRK13473 149 NYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 235 TAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKW 314
Cdd:PRK13473 228 TGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 315 KVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEG-ARILCGeGVDQlslplrNQAGYFMLPTVITDIKDESRCMTEEIF 393
Cdd:PRK13473 308 KVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTG-GEAP------DGKGYYYEPTLLAGARQDDEIVQREVF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 394 GPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCW--LIRElnLPFGGMKSSGIGREGAK 471
Cdd:PRK13473 381 GPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHfmLVSE--MPHGGQKQSGYGKDMSL 458
|
490
....*....|....*
gi 30520135 472 DSYDFFTEIKTITIK 486
Cdd:PRK13473 459 YGLEDYTVVRHVMVK 473
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-485 |
1.06e-148 |
|
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: 432.14 E-value: 1.06e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 28 YDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMDI 107
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 108 PRSVLNFRFFASSnLHHVSECTQMSHL-GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVT 186
Cdd:cd07092 82 PGAVDNFRFFAGA-ARTLEGPAAGEYLpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 187 AWMFCKLLdKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 266
Cdd:cd07092 161 TLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 267 NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQ 346
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 347 tEGARILCGEGVdqlslplRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSK 426
Cdd:cd07092 320 -AHARVLTGGRR-------AEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 30520135 427 DVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
12-483 |
2.37e-146 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 427.76 E-value: 2.37e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 12 NFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQ 89
Cdd:PRK13252 9 LYIDGAYVEATSgeTFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 90 AESKDQGKTLTLARTMDIPRSVLNFRFFAssNLHHVSECTQMSHLGC-MHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:PRK13252 89 LETLDTGKPIQETSVVDIVTGADVLEYYA--GLAPALEGEQIPLRGGsFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 169 IAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 249 KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGA 328
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 329 LISKAHLEKVRSYVLKAQTEGARILC-GEGVDQLSLPlrnqAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEE 407
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGKAEGARLLCgGERLTEGGFA----NGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30520135 408 VITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
13-485 |
7.34e-146 |
|
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: 426.44 E-value: 7.34e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSR-SPQERSLVLNRLADVLEQSLEELAQ 89
Cdd:cd07144 11 FINNEFVKSsdGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 90 AESKDQGKTLTLARTMDIPRSVLNFRFFASS--NLHHVSECTQMSHLGcmhYTVRTPVGIAGLISPWNLPLYLLTWKIAP 167
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYAGWadKIQGKTIPTSPNKLA---YTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 168 AIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 247
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 248 KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRK-WKVGVPSDPSANM 326
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 327 GALISKAHLEKVRSYVLKAQTEGARILCGegvdQLSLPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEE 406
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYG----GEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30520135 407 EVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-483 |
1.87e-144 |
|
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: 422.43 E-value: 1.87e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 11 ENFIGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQ 89
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 90 AESKDQGKTLTLARTmDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 170 AAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 249
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 250 LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGAL 329
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 330 ISKAHLEKVRSYVLKAQTEGARILC-GEGVDqlslplRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYgGERLK------RPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30520135 409 ITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTI 483
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
58-485 |
7.27e-144 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 416.63 E-value: 7.27e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARtMDIPRSVLNFRFFASsNLHHVSECTQMS-HLGC 136
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAG-LADKLGGPELPSpDPGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 137 MHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGE 216
Cdd:cd06534 85 EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 217 ALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQ 296
Cdd:cd06534 165 ALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 297 RSIYSEFLKRFVeatrkwkvgvpsdpsanmgaliskahlekvrsyvlkaqtegarilcgegvdqlslplrnqagyfmlpT 376
Cdd:cd06534 245 ESIYDEFVEKLV-------------------------------------------------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 377 VITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLI-RELNL 455
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEA 337
|
410 420 430
....*....|....*....|....*....|
gi 30520135 456 PFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd06534 338 PFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-485 |
1.88e-143 |
|
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: 418.86 E-value: 1.88e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 28 YDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARtMDI 107
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 108 PRSVLNFRFFASSNL--HHVSECTQMSHLgcmhyTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSV 185
Cdd:cd07106 81 GGAVAWLRYTASLDLpdEVIEDDDTRRVE-----LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 186 TAWMFCKLLDKAgVPPGVINIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 265
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 266 ANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKA 345
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 346 QTEGARILCGEGVDqlslplrNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWS 425
Cdd:cd07106 314 KAKGAKVLAGGEPL-------DGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 426 KDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-485 |
4.99e-142 |
|
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: 415.48 E-value: 4.99e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 27 SYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSR-SPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTm 105
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 106 DIPRSVLNFRFFASS--NLHHVSECTQMshlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMT 183
Cdd:cd07109 80 DVEAAARYFEYYGGAadKLHGETIPLGP---GYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 184 SVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 263
Cdd:cd07109 157 PLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 264 EDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDpSANMGALISKAHLEKVRSYVL 343
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 344 KAQTEGARILCGEGVdqlsLPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATV 423
Cdd:cd07109 316 RARARGARIVAGGRI----AEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30520135 424 WSKDVGRIHRVAKKLQSGLVWTNCWLIRE-LNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
29-484 |
1.03e-141 |
|
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: 414.83 E-value: 1.03e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 29 DPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLArTMDIP 108
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 109 RSVLNFRFFAS--SNLH-HVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSV 185
Cdd:cd07110 82 DVAGCFEYYADlaEQLDaKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 186 TAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 265
Cdd:cd07110 162 TELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 266 ANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKA 345
Cdd:cd07110 242 ADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 346 QTEGARILCGEGVdqlslPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWS 425
Cdd:cd07110 322 KEEGARLLCGGRR-----PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 30520135 426 KDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
61-485 |
1.20e-141 |
|
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: 414.43 E-value: 1.20e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 61 WSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFAS--SNLHHVSectqMSHLG--C 136
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EIEGAADLWRYAASlaRTLHGDS----YNNLGddM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 137 MHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGE 216
Cdd:cd07118 112 LGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 217 ALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQ 296
Cdd:cd07118 192 AMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVH 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 297 RSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVdqlslpLRNQAGYFMLPT 376
Cdd:cd07118 272 ESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGER------LASAAGLFYQPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 377 VITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLP 456
Cdd:cd07118 346 IFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELP 425
|
410 420
....*....|....*....|....*....
gi 30520135 457 FGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07118 426 FGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
13-481 |
3.15e-139 |
|
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: 408.81 E-value: 3.15e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQA 90
Cdd:TIGR01804 1 FIDGEYVEDSAgtTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 91 ESKDQGKTLTLARTMDIPRSVLNFRFFASsnLHHVSECTQMSHLGC-MHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAI 169
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAG--LAPALNGEIIPLGGPsFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 170 AAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 249
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 250 LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGAL 329
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 330 ISKAHLEKVRSYVLKAQTEGARILCGEGVDQLSlplRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVI 409
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPENV---GLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVI 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30520135 410 TRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 481
Cdd:TIGR01804 396 ARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
13-485 |
1.91e-137 |
|
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: 404.26 E-value: 1.91e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAF--PAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07139 2 FIGGRWVAPSGseTIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 169 IAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 249 KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGA 328
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 329 LISKAHLEKVRSYVLKAQTEGARILCGEGVdqlslPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGR-----PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30520135 409 ITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNcWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
13-483 |
1.94e-137 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 404.57 E-value: 1.94e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFP--AWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07142 7 FINGQFVDAASgkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA--SSNLHHVSECTQMSHLGcmhYTVRTPVGIAGLISPWNLPLYLLTWKIA 166
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAgwADKIHGMTLPADGPHHV---YTLHEPIGVVGQIIPWNFPLLMFAWKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 167 PAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-P 245
Cdd:cd07142 164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSAN 325
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 326 MGALISKAHLEKVRSYVLKAQTEGARILCGEgvDQLSlplrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGG--DRIG-----SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30520135 406 EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-487 |
4.95e-137 |
|
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: 403.65 E-value: 4.95e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 12 NFIGGKFLPCNS--YIDSYDPSTG-EVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07131 1 NYIGGEWVDSASgeTFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTmDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 169 IAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 249 KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGA 328
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 329 LISKAHLEKVRSYVLKAQTEGARILCG-EGVDQLSLplrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEE 407
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGgERLTGGGY----EKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 408 VITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITI 485
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
..
gi 30520135 486 KY 487
Cdd:cd07131 476 DY 477
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-485 |
1.05e-136 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 402.12 E-value: 1.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 29 DPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLtlaRTMDIP 108
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNAL---RTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 109 --RSVLN-FRFFASSnlhhVSEC---TQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEM 182
Cdd:cd07108 80 eaAVLADlFRYFGGL----AGELkgeTLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 183 TSVTAWMFCKLLDKAgVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 263 FEDANLEECIPATVRSS-FANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSY 341
Cdd:cd07108 235 FPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 342 V-LKAQTEGARIL-CGEgvdqLSLPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGL 419
Cdd:cd07108 315 IdLGLSTSGATVLrGGP----LPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30520135 420 AATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSY-DFFTEIKTITI 485
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-485 |
1.35e-136 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 402.03 E-value: 1.35e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQA 90
Cdd:cd07088 1 YINGEFVPSSSgeTIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 91 ESKDQGKTLTLARtMDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 171 AGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 251 SLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALI 330
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 331 SKAHLEKVRSYVLKAQTEGARILCGEGVDQLslplrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVIT 410
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKRPEG------EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30520135 411 RANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-483 |
9.98e-136 |
|
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: 399.31 E-value: 9.98e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 28 YDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWS-SRSPQERSLVLNRLADVLEQSLEELA---QAESkdqGKTLTLAR 103
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRallVAEV---GAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 104 TMDIPRSVLNFRFFA----SSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP 179
Cdd:cd07089 79 AMQVDGPIGHLRYFAdladSFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 180 SEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVR 339
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 340 SYVLKAQTEGARILCGEGVdqlslPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGL 419
Cdd:cd07089 319 GYIARGRDEGARLVTGGGR-----PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30520135 420 AATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07089 394 SGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-485 |
2.19e-135 |
|
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: 397.67 E-value: 2.19e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTltlartmdIPRSVLNFRFFASSNLHHVSECTQM------ 131
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGST--------RPKAAFEVGAAIAILREAAGLPRRPegeilp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 132 SHL-GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVT-AWMFCKLLDKAGVPPGVINIVFG 209
Cdd:cd07104 85 SDVpGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 210 TGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLC 289
Cdd:cd07104 165 GGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 290 TSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDqlslplrnqa 369
Cdd:cd07104 245 AGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 370 GYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWL 449
Cdd:cd07104 315 GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQT 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 30520135 450 IR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07104 395 VNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-485 |
2.46e-134 |
|
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: 395.95 E-value: 2.46e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 25 IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARt 104
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 105 MDIPRSVLNFRFFASSNLHHVSECTQM----SHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPS 180
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 181 EMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 260
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 261 IIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRS 340
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 341 YVLKAQTEGARILCGegvdqlslpLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLA 420
Cdd:cd07145 320 LVNDAVEKGGKILYG---------GKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQ 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30520135 421 ATVWSKDVGRIHRVAKKLQSGLVWTN-CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07145 391 ASVFTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-486 |
2.59e-134 |
|
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: 396.72 E-value: 2.59e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 12 NFIGGKFLPcnsyidSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAF---PAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07141 17 DSVSGKTFP------TINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFASSNLHHVSECTQMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07141 91 SLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 169 IAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-PHC 247
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGkSNL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 248 KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMG 327
Cdd:cd07141 250 KRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 328 ALISKAHLEKVRSYVLKAQTEGARILCGEGVdqlslplRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEE 407
Cdd:cd07141 330 PQIDEEQFKKILELIESGKKEGAKLECGGKR-------HGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30520135 408 VITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:cd07141 403 VIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-485 |
5.21e-134 |
|
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: 395.67 E-value: 5.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQA 90
Cdd:cd07117 4 FINGEWVKGssGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 91 ESKDQGKTLTLARTMDIPRSVLNFRFFASSNLHHVSECTQMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07117 84 ETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE-DTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 171 AGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07117 163 AGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 251 SLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALI 330
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 331 SKAHLEKVRSYVLKAQTEGARILCGeGVDQLSLPLrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVIT 410
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTG-GHRLTENGL--DKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30520135 411 RANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-481 |
1.10e-133 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 395.60 E-value: 1.10e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 7 LLMLENFIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSL 84
Cdd:PLN02278 22 LLRTQGLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 85 EELAQAESKDQGKTLTLAR-TMDIPRSVLNFrfFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTW 163
Cdd:PLN02278 102 EDLAQLMTLEQGKPLKEAIgEVAYGASFLEY--FAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 164 KIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLS 243
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 244 APHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPS 323
Cdd:PLN02278 260 AATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 324 ANMGALISKAHLEKVRSYVLKAQTEGARILCGEgvDQLSLplrnqAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFD 403
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGG--KRHSL-----GGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFK 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30520135 404 SEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 481
Cdd:PLN02278 413 TEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
13-487 |
1.57e-133 |
|
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: 394.50 E-value: 1.57e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAF-PAWSSRSPQERSLVLNRLADVLEQSLEELAQ 89
Cdd:cd07113 3 FIDGRPVAGQSekRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 90 AESKDQGKTLTLARTMDIPRSVLNFRFFASSNLHHVSECTQMShLGCMH------YTVRTPVGIAGLISPWNLPLYLLTW 163
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPS-IPSMQgerytaFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 164 KIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLS 243
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 244 APHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPS 323
Cdd:cd07113 241 ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 324 ANMGALISKAHLEKVRSYVLKAQTEGARILCG-EGVDqlslplrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPF 402
Cdd:cd07113 321 VMFGPLANQPHFDKVCSYLDDARAEGDEIVRGgEALA--------GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 403 DSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 482
Cdd:cd07113 393 EDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKS 472
|
....*
gi 30520135 483 ITIKY 487
Cdd:cd07113 473 VMIRY 477
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
13-486 |
7.36e-133 |
|
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: 393.05 E-value: 7.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAF--PAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07143 10 FINGEFVDSvhGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFF---ASSNLHHVSEcTQMSHLGcmhYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYggwADKIHGQVIE-TDIKKLT---YTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 166 APAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA- 244
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 245 PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSA 324
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 325 NMGALISKAHLEKVRSYVLKAQTEGARILCGEgvdqlslPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDS 404
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGG-------KRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 405 EEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVH 478
|
..
gi 30520135 485 IK 486
Cdd:cd07143 479 IN 480
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
13-483 |
1.35e-132 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 393.03 E-value: 1.35e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFP--AWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:PLN02766 24 FINGEFVDAASgkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA--SSNLHhvSECTQMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIA 166
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAgaADKIH--GETLKMSR-QLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 167 PAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-P 245
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAtS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSAN 325
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 326 MGALISKAHLEKVRSYVLKAQTEGARILCGegvdqlSLPLRNQaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSE 405
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTG------GKPCGDK-GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30520135 406 EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-485 |
1.24e-129 |
|
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: 383.87 E-value: 1.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 25 IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLART 104
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 105 mDIPRSVLNFRFFASSNLHHVSECTQMS----HLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPS 180
Cdd:cd07149 81 -EVDRAIETLRLSAEEAKRLAGETIPFDaspgGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 181 EMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPA 260
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 261 IIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRS 340
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 341 YVLKAQTEGARILCGEGVDqlslplrnqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLA 420
Cdd:cd07149 318 WVEEAVEGGARLLTGGKRD----------GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30520135 421 ATVWSKDVGRIHRVAKKLQSGLVwtncwLIREL------NLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07149 388 AGVFTNDLQKALKAARELEVGGV-----MINDSstfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-485 |
4.25e-129 |
|
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: 382.45 E-value: 4.25e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 26 DSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLA--R 103
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAwfE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 104 TMDIPRSVLNfrffASSNLHHVS-ECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEM 182
Cdd:cd07150 82 TTFTPELLRA----AAGECRRVRgETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 183 TSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 263 FEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYV 342
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 343 LKAQTEGARILCGEGVDqlslplrnqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAAT 422
Cdd:cd07150 318 EDAVAKGAKLLTGGKYD----------GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30520135 423 VWSKDVGRIHRVAKKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-484 |
5.76e-129 |
|
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: 382.08 E-value: 5.76e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 27 SYDPSTGEVYCKVPNSGKEEIEAAVEAAREAF--PAWSsRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARt 104
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 105 MDIPRSVLNFRFFASSNLH---HVSEctqmSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSE 181
Cdd:cd07120 79 FEISGAISELRYYAGLARTeagRMIE----PEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 182 MTSVTAWMFCKLLDKA-GVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 260
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 261 IIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRS 340
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 341 YVLKAQTEGARILC-GEGVDQlslplRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGL 419
Cdd:cd07120 315 MVERAIAAGAEVVLrGGPVTE-----GLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30520135 420 AATVWSKDVGRIHRVAKKLQSGLVWTNCW--LIRELNlpFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07120 390 AASVWTRDLARAMRVARAIRAGTVWINDWnkLFAEAE--EGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-487 |
1.26e-126 |
|
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: 377.18 E-value: 1.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 11 ENFIGGKFLP--CNSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07116 2 DNFIGGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFAS------SNLHHVSECTqmshlgcMHYTVRTPVGIAGLISPWNLPLYLLT 162
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGciraqeGSISEIDENT-------VAYHFHEPLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 163 WKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQL 242
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 243 SAPHCKKLSLELGGKNPAIIFE------DANLEECIPATVRSSFaNQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKV 316
Cdd:cd07116 234 ASENIIPVTLELGGKSPNIFFAdvmdadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 317 GVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQLSlplRNQAGYFMLPTVITDiKDESRCMTEEIFGPV 396
Cdd:cd07116 313 GNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELG---GLLGGGYYVPTTFKG-GNKMRIFQEEIFGPV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 397 TCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDF 476
Cdd:cd07116 389 LAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDH 468
|
490
....*....|.
gi 30520135 477 FTEIKTITIKY 487
Cdd:cd07116 469 YQQTKNLLVSY 479
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-487 |
2.31e-126 |
|
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: 375.56 E-value: 2.31e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 29 DPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTmDIP 108
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 109 RSVLNFRFFASSNLHHVSECTQMSHlGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAW 188
Cdd:cd07107 82 VAAALLDYFAGLVTELKGETIPVGG-RNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 189 MFCKLLDKAgVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANL 268
Cdd:cd07107 161 RLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 269 EECIPATVRS-SFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQT 347
Cdd:cd07107 240 EAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 348 EGARILCGEGVDQLSLPlrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKD 427
Cdd:cd07107 320 EGARLVTGGGRPEGPAL---EGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 428 VGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITIKY 487
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-487 |
5.26e-125 |
|
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: 372.98 E-value: 5.26e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPA--WSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07140 9 FINGEFVDAEGgkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA------SSNLHHVSECTQMSHLGcmhYTVRTPVGIAGLISPWNLPLYLLT 162
Cdd:cd07140 89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcdkiQGKTIPINQARPNRNLT---LTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 163 WKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQL 242
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 243 SA-PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSD 321
Cdd:cd07140 246 CAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 322 PSANMGALISKAHLEKVRSYVLKAQTEGARILCGEgvDQLSLPlrnqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVP 401
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGG--KQVDRP-----GFFFEPTVFTDVEDHMFIAKEESFGPIMIISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 402 FDSE--EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTE 479
Cdd:cd07140 399 FDDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLK 478
|
....*...
gi 30520135 480 IKTITIKY 487
Cdd:cd07140 479 TKTVTIEY 486
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-487 |
1.02e-121 |
|
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: 364.19 E-value: 1.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 12 NFIGGKFLP-CNSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQA 90
Cdd:cd07086 1 GVIGGEWVGsGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 91 ESKDQGKTLTLAR-----TMDIPrsvlnfrFFAssnlhhVSECTQMSHL-------GCMHYTVRTPVGIAGLISPWNLPL 158
Cdd:cd07086 81 VSLEMGKILPEGLgevqeMIDIC-------DYA------VGLSRMLYGLtipserpGHRLMEQWNPLGVVGVITAFNFPV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 159 YLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKA----GVPPGVINIVFGTGPrVGEALVSHPEVPLISFTGSQP 234
Cdd:cd07086 148 AVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 235 TAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKW 314
Cdd:cd07086 227 VGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 315 KVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVdqlslPLRNQAGYFMLPTVITDIKDESRCMTEEIFG 394
Cdd:cd07086 307 RIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKR-----IDGGEPGNYVEPTIVTGVTDDARIVQEETFA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 395 PVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRV--AKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAK 471
Cdd:cd07086 382 PILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGS 461
|
490
....*....|....*.
gi 30520135 472 DSYDFFTEIKTITIKY 487
Cdd:cd07086 462 DAWKQYMRRSTCTINY 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
13-472 |
2.52e-121 |
|
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: 363.25 E-value: 2.52e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLP--CNSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQA 90
Cdd:cd07111 25 FINGKWVKpeNRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 91 ESKDQGKTLTLARTMDIPRSVLNFrffassnLHHVSECTQMSHLGCMHytvrTPVGIAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07111 105 ESLDNGKPIRESRDCDIPLVARHF-------YHHAGWAQLLDTELAGW----KPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 171 AGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 251 SLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALI 330
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 331 SKAHLEKVRSYVLKAQTEGARILcgegvdQLSLPLRNQaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVIT 410
Cdd:cd07111 333 DPAQLKRIRELVEEGRAEGADVF------QPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30520135 411 RANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKD 472
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKE 467
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
13-487 |
3.60e-117 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 353.65 E-value: 3.60e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLP--CNSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPA-----WSSRSPQERSLVLNRLADVLEQSLE 85
Cdd:PLN02467 11 FIGGEWREpvLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 86 ELAQAESKDQGKTLTLArTMDIPRSVLNFRFFASsnLHHVSECTQ-------MSHLGCmhYTVRTPVGIAGLISPWNLPL 158
Cdd:PLN02467 91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYAD--LAEALDAKQkapvslpMETFKG--YVLKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 159 YLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAER 238
Cdd:PLN02467 166 LMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 239 ITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGV 318
Cdd:PLN02467 246 IMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 319 PSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGeGVDqlslPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTC 398
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCG-GKR----PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 399 VVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFT 478
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYL 480
|
....*....
gi 30520135 479 EIKTITiKY 487
Cdd:PLN02467 481 SVKQVT-KY 488
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-485 |
4.34e-117 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 350.72 E-value: 4.34e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARtMDIPRSVLNFRFFASSNLHHVSECTQMSHLGCM 137
Cdd:cd07105 13 FPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQIIGGSIPSDKPGTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 138 HYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVF---GTGPRV 214
Cdd:cd07105 92 AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVThspEDAPEV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 215 GEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIF 294
Cdd:cd07105 172 VEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERII 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 295 VQRSIYSEFLKRFVEATRKWKVGVPSDPSanmgaLISKAHLEKVRSYVLKAQTEGARILCGEGVDQlslplrNQAGYFML 374
Cdd:cd07105 252 VHESIADEFVEKLKAAAEKLFAGPVVLGS-----LVSAAAADRVKELVDDALSKGAKLVVGGLADE------SPSGTSMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 375 PTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIR-EL 453
Cdd:cd07105 321 PTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHdEP 400
|
410 420 430
....*....|....*....|....*....|..
gi 30520135 454 NLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07105 401 TLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-485 |
6.42e-116 |
|
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: 348.65 E-value: 6.42e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 25 IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARt 104
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 105 MDIPRSVLNFRFFASSNLHHVSEC----TQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPS 180
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEipldATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 181 EMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPA 260
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 261 IIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRS 340
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 341 YVLKAQTEGARILCGEGVDqlslplrnqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLA 420
Cdd:cd07094 318 WVEEAVEAGARLLCGGERD----------GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30520135 421 ATVWSKDVGRIHRVAKKLQSGLVWTN-CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-486 |
6.69e-114 |
|
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: 343.90 E-value: 6.69e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 25 IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKT-----L 99
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTrikanI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 100 TLARTMDIPRSvlnfrffASSNLHHVSECTQMSHL-GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAK 178
Cdd:cd07151 92 EWGAAMAITRE-------AATFPLRMEGRILPSDVpGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 179 PSEMTSVTA-WMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGK 257
Cdd:cd07151 165 PASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 258 NPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEK 337
Cdd:cd07151 245 NPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 338 VRSYVLKAQTEGARILCGEGVDqlslplrnqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRY 417
Cdd:cd07151 325 LLDKIEQAVEEGATLLVGGEAE----------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEY 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 418 GLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:cd07151 395 GLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
13-483 |
1.03e-113 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 346.02 E-value: 1.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFP--AWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:PLN02466 61 LINGQFVDAASgkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLARTMDIPRSVLNFRFFA------------SSNLHHVSectqmshlgcmhyTVRTPVGIAGLISPWNL 156
Cdd:PLN02466 141 ALETWDNGKPYEQSAKAELPMFARLFRYYAgwadkihgltvpADGPHHVQ-------------TLHEPIGVAGQIIPWNF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 157 PLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTA 236
Cdd:PLN02466 208 PLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 237 ERITQLSA-PHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWK 315
Cdd:PLN02466 288 KIVLELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 316 VGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEgvDQLSlplrnQAGYFMLPTVITDIKDESRCMTEEIFGP 395
Cdd:PLN02466 368 VGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGG--DRFG-----SKGYYIQPTVFSNVQDDMLIAQDEIFGP 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 396 VTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYD 475
Cdd:PLN02466 441 VQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLN 520
|
....*...
gi 30520135 476 FFTEIKTI 483
Cdd:PLN02466 521 NYLQVKAV 528
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
13-487 |
2.22e-113 |
|
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: 344.21 E-value: 2.22e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAE 91
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 92 SKDQGKTLTLArTMDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRtPVGIAGLISPWNLPLYLLTWKIAPAIAA 171
Cdd:cd07124 116 VLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALVT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 172 GNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA------P 245
Cdd:cd07124 194 GNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgqK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSAN 325
Cdd:cd07124 274 WLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 326 MGALISKAHLEKVRSYVLKAQTEGaRILCGEGVDQLSlplrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07124 354 MGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA-----AEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 406 EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTN-----CWLIRElnlPFGGMKSSGIG-REGAKDSYDFFTE 479
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkitgALVGRQ---PFGGFKMSGTGsKAGGPDYLLQFMQ 504
|
....*...
gi 30520135 480 IKTITIKY 487
Cdd:cd07124 505 PKTVTENF 512
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-485 |
1.09e-112 |
|
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: 340.35 E-value: 1.09e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 28 YDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTmDI 107
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 108 PRSVLNFRFFA----------SSNLHHVsectqMSHLGcmHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIA 177
Cdd:cd07099 80 LLALEAIDWAArnaprvlaprKVPTGLL-----MPNKK--ATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 178 KPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPrVGEALVSHpEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGK 257
Cdd:cd07099 153 KPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 258 NPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEK 337
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 338 VRSYVLKAQTEGARILCGegvdqlsLPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRY 417
Cdd:cd07099 311 VRRHVDDAVAKGAKALTG-------GARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 418 GLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07099 384 GLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
8-485 |
1.36e-109 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 333.79 E-value: 1.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 8 LMLEN--FIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPA--WSSRSPQERSLVLNRLADVLE 81
Cdd:PRK09847 16 LAIENrlFINGEYTAAaeNETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 82 QSLEELAQAESKDQGKTLTLARTMDIPRSVLNFRFFASSnLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLL 161
Cdd:PRK09847 96 AHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEA-IDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 162 TWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQ 241
Cdd:PRK09847 175 CWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 242 LSA-PHCKKLSLELGGKNPAIIFEDA-NLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVP 319
Cdd:PRK09847 255 DAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 320 SDPSANMGALISKAHLEKVRSYVLKAQTEGarilcgegvdQLSLPLRNQAGYFML-PTVITDIKDESRCMTEEIFGPVTC 398
Cdd:PRK09847 335 LDPATTMGTLIDCAHADSVHSFIREGESKG----------QLLLDGRNAGLAAAIgPTIFVDVDPNASLSREEIFGPVLV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 399 VVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFT 478
Cdd:PRK09847 405 VTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFT 484
|
....*..
gi 30520135 479 EIKTITI 485
Cdd:PRK09847 485 ELKTIWI 491
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
10-487 |
1.80e-108 |
|
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: 330.25 E-value: 1.80e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 10 LENFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEEL 87
Cdd:cd07085 1 LKLFINGEWVESKTteWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 88 AQAESKDQGKTLTLARTmDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAP 167
Cdd:cd07085 81 ARLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 168 AIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 247
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 248 KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMG 327
Cdd:cd07085 239 KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 328 ALISKAHLEKVRSYVLKAQTEGARILC-GEGVDQLSLPlrnqAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEE 406
Cdd:cd07085 319 PVISPAAKERIEGLIESGVEEGAKLVLdGRGVKVPGYE----NGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 407 EVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVwtncwlirELNLP---------FGGMKSSGIGREGA--KDSYD 475
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMV--------GINVPipvplaffsFGGWKGSFFGDLHFygKDGVR 466
|
490
....*....|..
gi 30520135 476 FFTEIKTITIKY 487
Cdd:cd07085 467 FYTQTKTVTSRW 478
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
59-485 |
3.03e-107 |
|
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: 326.17 E-value: 3.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 59 PAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARtmdiprsvlnfrFFASSNLHHVSECTQM------- 131
Cdd:cd07152 27 RAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAG------------FEVGAAIGELHEAAGLptqpqge 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 132 ---SHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTA-WMFCKLLDKAGVPPGVINIV 207
Cdd:cd07152 95 ilpSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 208 FGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEIC 287
Cdd:cd07152 175 PG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQIC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 288 LCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQLslplrn 367
Cdd:cd07152 254 MAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYDGL------ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 368 qagyFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTN- 446
Cdd:cd07152 328 ----FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINd 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 30520135 447 CWLIRELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITI 485
Cdd:cd07152 404 QTVNDEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
65-485 |
1.90e-105 |
|
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: 321.62 E-value: 1.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 65 SPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARtMDIPRSVLNFRFFASSNLHHVSEC--TQMSHLGCMH--YT 140
Cdd:cd07146 38 TRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVGRAADVLRFAAAEALRDDGESfsCDLTANGKARkiFT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 141 VRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVS 220
Cdd:cd07146 117 LREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELIT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 221 HPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIY 300
Cdd:cd07146 197 HPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 301 SEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDqlslplrnqaGYFMLPTVITD 380
Cdd:cd07146 275 DEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQRQ----------GALYAPTVLDH 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 381 IKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVwtNCWLI---RELNLPF 457
Cdd:cd07146 345 VPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTV--NVNEVpgfRSELSPF 422
|
410 420
....*....|....*....|....*....
gi 30520135 458 GGMKSSGIG-REGAKDSYDFFTEIKTITI 485
Cdd:cd07146 423 GGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-484 |
1.59e-103 |
|
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: 316.94 E-value: 1.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 60 AWSSRSPQERSLVLNRLADVLEQSLEELA---QAESkdqGKTLTLA--RTMDIprsVLNFRFFASSNLHHVSECTQMSHL 134
Cdd:cd07101 33 AWAARPFAERAAVFLRFHDLVLERRDELLdliQLET---GKARRHAfeEVLDV---AIVARYYARRAERLLKPRRRRGAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 135 GCMHYTV--RTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTA-WMFcKLLDKAGVPPGVINIVFGTG 211
Cdd:cd07101 107 PVLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTAlWAV-ELLIEAGLPRDLWQVVTGPG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 212 PRVGEALVSHPEvpLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTS 291
Cdd:cd07101 186 SEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 292 RIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGeGVDqlslplRNQAG- 370
Cdd:cd07101 264 RIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAG-GRA------RPDLGp 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 371 YFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTN---- 446
Cdd:cd07101 337 YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegya 416
|
410 420 430
....*....|....*....|....*....|....*....
gi 30520135 447 -CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07101 417 aAW--ASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
60-484 |
1.86e-103 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 319.13 E-value: 1.86e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 60 AWSSRSPQERSLVLNRLAD-VLEQSLE--ELAQAESkdqGKTLTLA--RTMDIPrsvLNFRFFASSNLHHVSECTQMSHL 134
Cdd:PRK09407 69 AWAATPVRERAAVLLRFHDlVLENREEllDLVQLET---GKARRHAfeEVLDVA---LTARYYARRAPKLLAPRRRAGAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 135 GCMHYTV--RTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTA-WMFcKLLDKAGVPPGVINIVFGTG 211
Cdd:PRK09407 143 PVLTKTTelRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTAlAAV-ELLYEAGLPRDLWQVVTGPG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 212 PRVGEALVSHpeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTS 291
Cdd:PRK09407 222 PVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 292 RIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGeGVDqlslplRNQAG- 370
Cdd:PRK09407 300 RIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAG-GKA------RPDLGp 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 371 YFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTN---- 446
Cdd:PRK09407 373 LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegya 452
|
410 420 430
....*....|....*....|....*....|....*....
gi 30520135 447 -CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:PRK09407 453 aAW--GSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
58-485 |
2.97e-102 |
|
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: 312.86 E-value: 2.97e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASsNLHHVSECTQMSHLGCM 137
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAE-NAEAFLADEPIETDAGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 138 HYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVgEA 217
Cdd:cd07100 90 AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQV-EA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 218 LVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQR 297
Cdd:cd07100 169 IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 298 SIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQlslplrnQAGYFMLPTV 377
Cdd:cd07100 249 DVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD-------GPGAFYPPTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 378 ITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPF 457
Cdd:cd07100 322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPF 401
|
410 420
....*....|....*....|....*...
gi 30520135 458 GGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07100 402 GGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
25-486 |
6.33e-100 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 308.35 E-value: 6.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 25 IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSP-QERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLA- 102
Cdd:cd07082 18 IEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 103 ----RTMDIprsvLNFRFFASSNLH-HVSECTQMSH-LGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVI 176
Cdd:cd07082 98 kevdRTIDY----IRDTIEELKRLDgDSLPGDWFPGtKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 177 AKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSapHCKKLSLELGG 256
Cdd:cd07082 174 FKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH--PMKRLVLELGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 257 KNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLE 336
Cdd:cd07082 252 KDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSAD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 337 KVRSYVLKAQTEGARILCGEGvdqlslplrNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVR 416
Cdd:cd07082 332 FVEGLIDDAVAKGATVLNGGG---------REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSN 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30520135 417 YGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIREL-NLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:cd07082 403 YGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPdHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
25-485 |
2.80e-98 |
|
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: 303.40 E-value: 2.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 25 IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLART 104
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 105 mDIPRSVLNFRFFA--SSNLHhvsecTQMSHL-------GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTV 175
Cdd:cd07147 81 -EVARAIDTFRIAAeeATRIY-----GEVLPLdisargeGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 176 IAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVfgtgP---RVGEALVSHPEVPLISFTGSQPTAERITQLsAPHcKKLSL 252
Cdd:cd07147 155 VLKPASRTPLSALILGEVLAETGLPKGAFSVL----PcsrDDADLLVTDERIKLLSFTGSPAVGWDLKAR-AGK-KKVVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 253 ELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISK 332
Cdd:cd07147 229 ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 333 AHLEKVRSYVLKAQTEGARILCGEGVDqlslplrnqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRA 412
Cdd:cd07147 309 SEAERVEGWVNEAVDAGAKLLTGGKRD----------GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30520135 413 NSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTN---CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07147 379 NDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdvpTF--RVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
73-487 |
2.77e-97 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 299.34 E-value: 2.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 73 LNRLADVLEQSLEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLIS 152
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 153 PWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGS 232
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 233 QPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATR 312
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 313 KWKVGVPSDPSA-NMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDqlslplrNQAGYFMLPTVITDIKDESRCMTEE 391
Cdd:PRK10090 240 AVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAV-------EGKGYYYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 392 IFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNcwliRElNLP-----FGGMKSSGIG 466
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN----RE-NFEamqgfHAGWRKSGIG 387
|
410 420
....*....|....*....|.
gi 30520135 467 REGAKDSYDFFTEIKTITIKY 487
Cdd:PRK10090 388 GADGKHGLHEYLQTQVVYLQS 408
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
6-485 |
1.21e-93 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 292.20 E-value: 1.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 6 ELLMLENFIGGKFLPCNS--YIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQS 83
Cdd:PRK11241 7 TLFRQQALINGEWLDANNgeVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 84 LEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTW 163
Cdd:PRK11241 87 QDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 164 KIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLS 243
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 244 APHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPS 323
Cdd:PRK11241 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 324 ANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQLslplrnqAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFD 403
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL-------GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 404 SEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PRK11241 399 DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYM 478
|
..
gi 30520135 484 TI 485
Cdd:PRK11241 479 CI 480
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-483 |
5.61e-92 |
|
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: 286.83 E-value: 5.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 28 YDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGK---------- 97
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRpiaqaggeir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 98 -TLTLARTM-DI-PRSVLNFRFFASSNLHHvsectqmshlgcmhYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNT 174
Cdd:cd07102 81 gMLERARYMiSIaEEALADIRVPEKDGFER--------------YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 175 VIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPrVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLEL 254
Cdd:cd07102 147 VILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 255 GGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAH 334
Cdd:cd07102 226 GGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 335 LEKVRSYVLKAQTEGARILCGEGvdqlSLPLRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANS 414
Cdd:cd07102 306 ADFVRAQIADAIAKGARALIDGA----LFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMND 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30520135 415 VRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07102 382 SEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
13-484 |
4.21e-91 |
|
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: 286.76 E-value: 4.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAE 91
Cdd:TIGR01237 36 VINGERVETENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 92 SKDQGKTLTLArTMDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAA 171
Cdd:TIGR01237 116 VKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 172 GNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA------P 245
Cdd:TIGR01237 195 GNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 246 HCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSAN 325
Cdd:TIGR01237 275 HLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 326 MGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQlslplrnqAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSE 405
Cdd:TIGR01237 355 VGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDS--------KGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 406 EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGlvwtNCWLIRELN------LPFGGMKSSGIG-REGAKDSYDFFT 478
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVG----NLYFNRNITgaivgyQPFGGFKMSGTDsKAGGPDYLALFM 502
|
....*.
gi 30520135 479 EIKTIT 484
Cdd:TIGR01237 503 QAKTVT 508
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-484 |
1.86e-90 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 283.42 E-value: 1.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 28 YDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMDI 107
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 108 PRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRT---PVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTS 184
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVeyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 185 VTAWMFC----KLLDKAGVPPGVINIVFGTgPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 260
Cdd:cd07098 161 WSSGFFLsiirECLAACGHDPDLVQLVTCL-PETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 261 IIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRS 340
Cdd:cd07098 240 IVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 341 YVLKAQTEGARILCGEGVDQlsLPLRNQAGYFmLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLA 420
Cdd:cd07098 320 LVADAVEKGARLLAGGKRYP--HPEYPQGHYF-PPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30520135 421 ATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNYYVqqLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-487 |
5.64e-89 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 281.05 E-value: 5.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 14 IGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAES 92
Cdd:PRK03137 41 IGGERITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 93 KDQGKTLTLArTMDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAG 172
Cdd:PRK03137 121 KEAGKPWAEA-DADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 173 NTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA---P---H 246
Cdd:PRK03137 200 NTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqPgqiW 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 247 CKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPsANM 326
Cdd:PRK03137 280 LKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 327 GALISKAHLEKVRSYVLKAQTEGARILCGEGVDqlslplrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEE 406
Cdd:PRK03137 359 GPVINQASFDKIMSYIEIGKEEGRLVLGGEGDD--------SKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 407 EVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGlvwtNCWLIRELN------LPFGGMKSSGI-GREGAKDSYDFFTE 479
Cdd:PRK03137 431 HALEIANNTEYGLTGAVISNNREHLEKARREFHVG----NLYFNRGCTgaivgyHPFGGFNMSGTdSKAGGPDYLLLFLQ 506
|
....*...
gi 30520135 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 |
1.89e-78 |
|
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: 254.04 E-value: 1.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNSYIDSYDPSTGE-VYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEEL---A 88
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELialA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESkdqGKTLTLArtmdIP--RSVLNF-RFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKI 165
Cdd:cd07125 116 AAEA---GKTLADA----DAevREAIDFcRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 166 APAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAP 245
Cdd:cd07125 189 AAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 246 HCK---KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDP 322
Cdd:cd07125 269 RDGpilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 323 SANMGALISKAHLEKVRSYVLKAQTEgARILCGEGVDQLSlplrnqaGYFMLPTVITDikDESRCMTEEIFGPVTCVVPF 402
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGN-------GYFVAPGIIEI--VGIFDLTTEVFGPILHVIRF 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30520135 403 DSE--EEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGlvwtNCWLIRE------LNLPFGGMKSSGIG 466
Cdd:cd07125 419 KAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYINRNitgaivGRQPFGGWGLSGTG 486
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
13-484 |
7.37e-74 |
|
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: 241.33 E-value: 7.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNSYIDSYDPS-TGEVYCKVPNSGKEEIEAAVEAAREAFPAWSsRSPQE-RSLVLNRLADVLEQSLEELAQA 90
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKTWK-DWPQEdRARLLLKAADLLRRRRRELIAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 91 ESKDQGKTLTLArtMDIPRSVLNF-RFFASSNLHHVSECTQM-SHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07083 101 LTYEVGKNWVEA--IDDVAEAIDFiRYYARAALRLRYPAVEVvPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 169 IAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC- 247
Cdd:cd07083 179 VAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 248 -----KKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDP 322
Cdd:cd07083 259 gqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 323 SANMGALISKAHLEKVRSYVLKAQTEGARILcgegvdQLSLPLRNqaGYFMLPTVITDIKDESRCMTEEIFGPVTCV--V 400
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHGKNEGQLVL------GGKRLEGE--GYFVAPTVVEEVPPKARIAQEEIFGPVLSVirY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 401 PFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIREL--NLPFGGMKSSGIG-REGAKDSYDFF 477
Cdd:cd07083 411 KDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSGTNaKTGGPHYLRRF 490
|
....*..
gi 30520135 478 TEIKTIT 484
Cdd:cd07083 491 LEMKAVA 497
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-470 |
1.35e-72 |
|
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: 236.01 E-value: 1.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLART--------MDIprsvlnfrffaSSNLHHV---S 126
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDI-----------SIKAYHErtgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 127 ECTQMS-HLGCMHYTvrtPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVIN 205
Cdd:cd07095 82 RATPMAqGRAVLRHR---PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 206 IVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK-LSLELGGKNPAIIFEDANLEECIPATVRSSFANQG 284
Cdd:cd07095 159 LVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 285 EICLCTSRIFV-QRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKvrsYVLKAQT---EGARILcgegvdq 360
Cdd:cd07095 238 QRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAAR---YLLAQQDllaLGGEPL------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 361 LSLPLRNQAGYFMLPTVI--TDIKDESrcmTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKL 438
Cdd:cd07095 308 LAMERLVAGTAFLSPGIIdvTDAADVP---DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARI 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 30520135 439 QSGLVWTNcwliRELN-----LPFGGMKSSGIGREGA 470
Cdd:cd07095 385 RAGIVNWN----RPTTgasstAPFGGVGLSGNHRPSA 417
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
63-485 |
3.90e-70 |
|
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: 229.33 E-value: 3.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 63 SRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMDI--PRSVLNFrffASSNLHHVSEcTQMSHLGCMH-- 138
Cdd:cd07087 16 TRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIavVLGEIDH---ALKHLKKWMK-PRRVSVPLLLqp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 139 ---YTVRTPVGIAGLISPWNLPLYLLtwkIAP---AIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGtGP 212
Cdd:cd07087 92 akaYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 213 RVGEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEEcipaTVRS----SFANQGEICL 288
Cdd:cd07087 167 EVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEV----AARRiawgKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 289 CTSRIFVQRSIYSEFLKRFVEATRKWkvgVPSDP--SANMGALISKAHLEKVRSYVlkaqtEGARILCGEGVDQLSLplr 366
Cdd:cd07087 242 APDYVLVHESIKDELIEELKKAIKEF---YGEDPkeSPDYGRIINERHFDRLASLL-----DDGKVVIGGQVDKEER--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 367 nqagyFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTN 446
Cdd:cd07087 311 -----YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN 385
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 30520135 447 CWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07087 386 DVLLHAAIpnLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
25-487 |
2.60e-69 |
|
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: 228.63 E-value: 2.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 25 IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLAR- 103
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 104 ----TMDI-------PRSvLNFRFFASSNLHHVsectqmshlgcMhYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAG 172
Cdd:cd07130 94 evqeMIDIcdfavglSRQ-LYGLTIPSERPGHR-----------M-MEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 173 NTVIAKPSEMTSVTAW----MFCKLLDKAGVPPGVINIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07130 161 NVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 249 KLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGA 328
Cdd:cd07130 240 RSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 329 LISKAHLEKVRSYVLKAQTEGARILCGEGVdqlslplRNQAGYFMLPTVITdIKDESRCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVLFGGKV-------IDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 409 ITRANSVRYGLAATVWSKDVGRIHRVAKKLQS--GLVwtNCwlirelNLP---------FGGMKSSGIGREGAKDSYDFF 477
Cdd:cd07130 392 IAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIV--NV------NIGtsgaeiggaFGGEKETGGGRESGSDAWKQY 463
|
490
....*....|
gi 30520135 478 TEIKTITIKY 487
Cdd:cd07130 464 MRRSTCTINY 473
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-485 |
5.46e-69 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 227.31 E-value: 5.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 25 IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLART 104
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 105 mDIPRSVLNFRFFASSNLHHVS-ECTQMSHLGCMHYTVR-TPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEM 182
Cdd:PRK09406 83 -EALKCAKGFRYYAEHAEALLAdEPADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 183 TSVTAWMFCKLLDKAGVPPGVinivFGT---GPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGC----FQTllvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 260 AIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVR 339
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 340 SYVLKAQTEGARILCGEgvdqlSLPLRNqaGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGL 419
Cdd:PRK09406 318 KQVDDAVAAGATILCGG-----KRPDGP--GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30520135 420 AATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
66-485 |
5.35e-67 |
|
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: 222.29 E-value: 5.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 66 PQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARtMDIPRSVLNFRFFASSNLHHVSECTQMSHL----GCMHYTV 141
Cdd:cd07148 43 AHERIAILERLADLMEERADELALLIAREGGKPLVDAK-VEVTRAIDGVELAADELGQLGGREIPMGLTpasaGRIAFTT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 142 RTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFgTGPRVGEALVSH 221
Cdd:cd07148 122 REPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 222 PEVPLISFTGSQPTAERITQLSAPHcKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYS 301
Cdd:cd07148 201 PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIAD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 302 EFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEgvDQLSLPLrnqagyfMLPTVITDI 381
Cdd:cd07148 280 DFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGG--KRLSDTT-------YAPTVLLDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 382 KDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTN-------CWlireln 454
Cdd:cd07148 351 PRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNdhtafrvDW------ 424
|
410 420 430
....*....|....*....|....*....|.
gi 30520135 455 LPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:cd07148 425 MPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
13-470 |
1.45e-63 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 214.05 E-value: 1.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 13 FIGGKFLPCNSY-IDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAE 91
Cdd:PRK09457 4 WINGDWIAGQGEaFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 92 SKDQGKTLTLART--------MDIprsvlnfrffaSSNLHHVSECTQMSHLGCMHYTVR-TPVGIAGLISPWNLPLYLLT 162
Cdd:PRK09457 84 ARETGKPLWEAATevtaminkIAI-----------SIQAYHERTGEKRSEMADGAAVLRhRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 163 WKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQL 242
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 243 SAPHCKK-LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSE-FLKRFVEATRKWKVGVP- 319
Cdd:PRK09457 232 FAGQPEKiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWd 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 320 SDPSANMGALISkahlEKVRSYVLKAQTE----GARILcgegvdqLSLPLRNQAGYFMLPTVItDIKDESRCMTEEIFGP 395
Cdd:PRK09457 312 AEPQPFMGAVIS----EQAAQGLVAAQAQllalGGKSL-------LEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 396 VTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNcwliRELN-----LPFGGMKSSGIGREGA 470
Cdd:PRK09457 380 LLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN----KPLTgassaAPFGGVGASGNHRPSA 455
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
58-467 |
1.72e-62 |
|
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: 209.78 E-value: 1.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMDIPRSVLNFRFfASSNLH------HVSecTQM 131
Cdd:cd07134 11 ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINH-AIKHLKkwmkpkRVR--TPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 132 SHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVinIVFGTG 211
Cdd:cd07134 88 LLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFEGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 212 PRVGEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTS 291
Cdd:cd07134 166 AEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 292 RIFVQRSIYSEFLKRFVEATRK-WKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDqlslplrnQAG 370
Cdd:cd07134 245 YVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD--------AAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 371 YFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLI 450
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVL 396
|
410
....*....|....*....
gi 30520135 451 REL--NLPFGGMKSSGIGR 467
Cdd:cd07134 397 HFLnpNLPFGGVNNSGIGS 415
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
64-483 |
3.70e-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: 209.00 E-value: 3.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 64 RSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMDIpRSVLNFRFFASSNLHHVS--ECTQMSHLGCMHYTV 141
Cdd:cd07135 24 KDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEV-SGVKNDILHMLKNLKKWAkdEKVKDGPLAFMFGKP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 142 RT---PVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGTGPRVGEAL 218
Cdd:cd07135 103 RIrkePLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 219 VSHPEvpLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFVQRS 298
Cdd:cd07135 182 EQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 299 IYSEFLKRFVEATRKWKVGVPSDPSaNMGALISKAHLEKVRSYVlkAQTEGARILCGEgvdqlslplRNQAGYFMLPTVI 378
Cdd:cd07135 260 VYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLL--DTTKGKVVIGGE---------MDEATRFIPPTIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 379 TDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSG-LVWTNCWL---IRelN 454
Cdd:cd07135 328 SDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGgVVINDTLIhvgVD--N 405
|
410 420
....*....|....*....|....*....
gi 30520135 455 LPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07135 406 APFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
65-483 |
1.87e-58 |
|
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: 198.86 E-value: 1.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 65 SPQERSLVLNRLADVLEQSLEELAQAESKDQG---KTLTLarTMDIPRSVLNFRFfASSNL--------HHVSectqMSH 133
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGhrsRHETL--LAEILPSIAGIKH-ARKHLkkwmkpsrRHVG----LLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 134 LGCMHYTVRTPVGIAGLISPWNLPLYLLtwkIAP---AIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGvPPGVINIVFGt 210
Cdd:cd07133 91 LPAKAEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYF-DEDEVAVVTG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 211 GPRVGEALVSHPEVPLIsFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCT 290
Cdd:cd07133 166 GADVAAAFSSLPFDHLL-FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 291 SRIFVQRsiysEFLKRFVEATRKWKVGVPSDPSAN--MGALISKAHLEKVRSYVLKAQTEGARIL-CGEGVDQLSlplrn 367
Cdd:cd07133 245 DYVLVPE----DKLEEFVAAAKAAVAKMYPTLADNpdYTSIINERHYARLQGLLEDARAKGARVIeLNPAGEDFA----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 368 qAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNC 447
Cdd:cd07133 316 -ATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIND 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 30520135 448 WLIREL--NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07133 395 TLLHVAqdDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
63-486 |
1.48e-57 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 198.33 E-value: 1.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 63 SRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMDIPRSVLNFRFFassnLHHVSECTQ--------MSHL 134
Cdd:PTZ00381 25 TRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHL----LKHLDEYLKpekvdtvgVFGP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 135 GcMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGtGPRV 214
Cdd:PTZ00381 101 G-KSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 215 GEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIF 294
Cdd:PTZ00381 178 TTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 295 VQRSIYSEFLKRFVEAtRKWKVGVPSDPSANMGALISKAHLEKVRSyvLKAQTEGARILCGEGvdqlslplrNQAGYFML 374
Cdd:PTZ00381 257 VHRSIKDKFIEALKEA-IKEFFGEDPKKSEDYSRIVNEFHTKRLAE--LIKDHGGKVVYGGEV---------DIENKYVA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 375 PTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELN 454
Cdd:PTZ00381 325 PTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLN 404
|
410 420 430
....*....|....*....|....*....|....
gi 30520135 455 --LPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:PTZ00381 405 pnLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-487 |
1.49e-57 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 200.74 E-value: 1.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 12 NFIGGKFLPC--NSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQ 89
Cdd:PLN02419 116 NLIGGSFVESqsSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 90 AESKDQGKTLTLARTmDIPRSVLNFRFFASSNLHHVSECTQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAI 169
Cdd:PLN02419 196 NITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 170 AAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVgEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 249
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 250 LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSR-IFVQRSIYSEflKRFVEATRKWKVGVPSDPSANMGA 328
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDAKSWE--DKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 329 LISKAHLEKVRSYVLKAQTEGARILCgEGVDqLSLPlRNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLL-DGRD-IVVP-GYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 409 ITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLirELNLP---FGGMKSSGIGREG--AKDSYDFFTEIKTI 483
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI--PVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
....
gi 30520135 484 TIKY 487
Cdd:PLN02419 587 TQKQ 590
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
58-466 |
6.23e-57 |
|
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: 196.67 E-value: 6.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLArtMDIPRSVLNF-RFFASSNLHHVSEctqmshlgc 136
Cdd:TIGR01238 87 FPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA--IAEVREAVDFcRYYAKQVRDVLGE--------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 137 mhYTVRtPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGE 216
Cdd:TIGR01238 156 --FSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 217 ALVSHPEVPLISFTGSQPTAERITQ-----LSAPhcKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTS 291
Cdd:TIGR01238 233 ALTSDPRIAGVAFTGSTEVAQLINQtlaqrEDAP--VPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 292 RIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILcgegvdQLSL--PLRNQA 369
Cdd:TIGR01238 311 VLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIA------QLTLddSRACQH 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 370 GYFMLPTVITdiKDESRCMTEEIFGPVTCVVPFDSEE--EVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGlvwtNC 447
Cdd:TIGR01238 385 GTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVG----NC 458
|
410 420
....*....|....*....|....*
gi 30520135 448 WLIREL------NLPFGGMKSSGIG 466
Cdd:TIGR01238 459 YVNRNQvgavvgVQPFGGQGLSGTG 483
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
129-483 |
9.75e-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: 195.03 E-value: 9.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 129 TQMSHLGCMHYTVRTPVGIAGLISPWNLPLYLLtwkIAP---AIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVIN 205
Cdd:cd07136 85 TPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 206 IVFGtGPRVGEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGE 285
Cdd:cd07136 161 VVEG-GVEENQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 286 ICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDpSANMGALISKAHLEKVRSYVlkaqtEGARILCGEGVDQLSLpl 365
Cdd:cd07136 239 TCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETL-- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 366 rnqagyFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWT 445
Cdd:cd07136 311 ------YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCI 384
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 30520135 446 NCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07136 385 NDTIMHLANpyLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
58-466 |
1.31e-54 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 197.34 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEE---LAQAESkdqGKTLTLArtMDIPRSVLNF-RFFASSNLHHVSECTQM-S 132
Cdd:PRK11904 598 FPAWSRTPVEERAAILERAADLLEANRAEliaLCVREA---GKTLQDA--IAEVREAVDFcRYYAAQARRLFGAPEKLpG 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 133 HLGCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGP 212
Cdd:PRK11904 673 PTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 213 RVGEALVSHPEVPLISFTGSQPTAERITQ-LSAPHCKKLSL--ELGGKNPAIIFEDANLEECIPATVRSSFANQGEIClc 289
Cdd:PRK11904 753 TVGAALTADPRIAGVAFTGSTETARIINRtLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRC-- 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 290 tS--RI-FVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVlKAQTEGARILCgegvdQLSLPLR 366
Cdd:PRK11904 831 -SalRVlFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHI-ERMKREARLLA-----QLPLPAG 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 367 NQAGYFMLPTV--ITDIKDesrcMTEEIFGPVTCVVPFDSEE--EVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGl 442
Cdd:PRK11904 904 TENGHFVAPTAfeIDSISQ----LEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVG- 978
|
410 420 430
....*....|....*....|....*....|..
gi 30520135 443 vwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:PRK11904 979 ---NVYVNR--NQigavvgvqPFGGQGLSGTG 1005
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-483 |
6.17e-54 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 187.76 E-value: 6.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 27 SYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTmD 106
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 107 IPRSVLNFRFFASSNLHHV-SECTQM-SHLGCMHYTvrtPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTS 184
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLkAEPTLVeNQQAVIEYR---PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 185 VTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEAlVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFE 264
Cdd:PRK13968 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQM-INDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 265 DANLEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLK 344
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 345 AQTEGARILCGEgvDQLSlplrnQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVW 424
Cdd:PRK13968 326 TLAEGARLLLGG--EKIA-----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 30520135 425 SKDVGRIHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
58-466 |
1.92e-53 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 194.00 E-value: 1.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEE---LAQAESkdqGKTLT--LArtmDIpRSVLNF-RFFASSNLHHvsectqm 131
Cdd:COG4230 606 FPAWSATPVEERAAILERAADLLEAHRAElmaLLVREA---GKTLPdaIA---EV-REAVDFcRYYAAQARRL------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 132 shlgCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTG 211
Cdd:COG4230 672 ----FAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDG 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 212 PRVGEALVSHPEVPLISFTGSQPTAERIT-QLSAPHCKKLSL--ELGGKNPAIIfeD--ANLEECIPATVRSSFANQGEI 286
Cdd:COG4230 748 ETVGAALVADPRIAGVAFTGSTETARLINrTLAARDGPIVPLiaETGGQNAMIV--DssALPEQVVDDVLASAFDSAGQR 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 287 ClctS--RI-FVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARIlcgegvDQLSL 363
Cdd:COG4230 826 C---SalRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV------HQLPL 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 364 PLRNQAGYFMLPTV--ITDIKDesrcMTEEIFGPVTCVVPFDSEE--EVITRANSVRYGLAATVWSKDVGRIHRVAKKLQ 439
Cdd:COG4230 897 PEECANGTFVAPTLieIDSISD----LEREVFGPVLHVVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARAR 972
|
410 420 430
....*....|....*....|....*....|....*
gi 30520135 440 SGlvwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:COG4230 973 VG----NVYVNR--NIigavvgvqPFGGEGLSGTG 1001
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
60-485 |
2.21e-53 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 187.27 E-value: 2.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 60 AWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTmDIPRSVLNFRFFASSNLHHVSE---CTQMSHLG- 135
Cdd:PLN00412 68 AWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVT-EVVRSGDLISYTAEEGVRILGEgkfLVSDSFPGn 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 136 -----CMhyTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGT 210
Cdd:PLN00412 147 ernkyCL--TSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 211 GPRVGEALVSHPEVPLISFTGSQpTAERItqlsaphCKK-----LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGE 285
Cdd:PLN00412 225 GSEIGDFLTMHPGVNCISFTGGD-TGIAI-------SKKagmvpLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 286 ICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDpSANMGALISKAHLEKVRSYVLKAQTEGARiLCGEgvdqlslpl 365
Cdd:PLN00412 297 RCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGAT-FCQE--------- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 366 RNQAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWT 445
Cdd:PLN00412 366 WKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQI 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 30520135 446 NCWLIRELN-LPFGGMKSSGIGREGAKDSYDFFTEIKTITI 485
Cdd:PLN00412 446 NSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKSTVI 486
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
58-466 |
4.43e-53 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 193.16 E-value: 4.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLtlARTMDIPRSVLNF-RFFASsnlhhvsectQMSHLGC 136
Cdd:PRK11905 603 FPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTL--ANAIAEVREAVDFlRYYAA----------QARRLLN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 137 MhyTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGE 216
Cdd:PRK11905 671 G--PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGA 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 217 ALVSHPEVPLISFTGSQPTAERITQLSAPHCKK---LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEIClctS-- 291
Cdd:PRK11905 749 ALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRC---Sal 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 292 RI-FVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARilcgegVDQLSLPLRNQAG 370
Cdd:PRK11905 826 RVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRL------VHQLPLPAETEKG 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 371 YFMLPTVI--TDIKDesrcMTEEIFGPVTCVVPFDSEE--EVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTN 446
Cdd:PRK11905 900 TFVAPTLIeiDSISD----LEREVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
410 420
....*....|....*....|....*...
gi 30520135 447 cwliRelNL--------PFGGMKSSGIG 466
Cdd:PRK11905 976 ----R--NIigavvgvqPFGGEGLSGTG 997
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
59-464 |
1.60e-52 |
|
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: 185.48 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 59 PAWSSRSPQERSLVLNRLADVLEQSL-EELAQAESKDQGKTLTLARTMDIPRSVLNFRFfassNLHHVSECTQM----SH 133
Cdd:cd07123 83 KEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNVWQAEIDAACELIDFLRF----NVKYAEELYAQqplsSP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 134 LGC---MHYtvRTPVGIAGLISPWN-------LPLylltwkiAPAIAaGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGV 203
Cdd:cd07123 159 AGVwnrLEY--RPLEGFVYAVSPFNftaiggnLAG-------APALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 204 INIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA---------PhckKLSLELGGKNPAIIFEDANLEECIPA 274
Cdd:cd07123 229 INFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryrtyP---RIVGETGGKNFHLVHPSADVDSLVTA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 275 TVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTE-GARIL 353
Cdd:cd07123 306 TVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEII 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 354 CGEGVDqlslplrNQAGYFMLPTVI--TDIKDESrcMTEEIFGPVTCV-VPFDSE-EEVITRANSV-RYGLAATVWSKDV 428
Cdd:cd07123 386 AGGKCD-------DSVGYFVEPTVIetTDPKHKL--MTEEIFGPVLTVyVYPDSDfEETLELVDTTsPYALTGAIFAQDR 456
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 30520135 429 GRIHRVAKKLQ--SGLVWTNC----WLIRElnLPFGGMKSSG 464
Cdd:cd07123 457 KAIREATDALRnaAGNFYINDkptgAVVGQ--QPFGGARASG 496
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
61-464 |
2.07e-47 |
|
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: 171.89 E-value: 2.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 61 WSSRSPQERSLVLNRLADVLEQSL-EELAQAESKDQGKTLTLARTMDIPRSVLNFRFfassNLHHVSECTQ---MSHLGC 136
Cdd:TIGR01236 85 WSNLPFYDRAAIFLKAADLLSGPYrYEILAATMLGQSKTVYQAEIDAVAELIDFFRF----NVKYARELYAqqpISAPGE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 137 MHYTVRTPV-GIAGLISPWNLPLYLLTWKIAPAIAaGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVG 215
Cdd:TIGR01236 161 WNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 216 EALVSHPEVPLISFTGSQPTAERITQLSAPHCKK------LSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLC 289
Cdd:TIGR01236 240 DQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRyhnfprIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 290 TSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYV--LKAQTEGARILCGEGVDqlslplrN 367
Cdd:TIGR01236 320 ASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIedAKKDPEALTILYGGKYD-------D 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 368 QAGYFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEE-----EVITraNSVRYGLAATVWSKDVGRIHRVAKKLQ--S 440
Cdd:TIGR01236 393 SQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKykeilDLVD--STSQYGLTGAVFAKDRKAILEADKKLRfaA 470
|
410 420
....*....|....*....|....*.
gi 30520135 441 GLVWTN--CWLIRELNLPFGGMKSSG 464
Cdd:TIGR01236 471 GNFYINdkCTGAVVGQQPFGGARMSG 496
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
59-466 |
7.05e-43 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 162.84 E-value: 7.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 59 PAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLArtmdIP--RSVLNF-RFFASSNLHHVSECTQMshlg 135
Cdd:PRK11809 696 PIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNA----IAevREAVDFlRYYAGQVRDDFDNDTHR---- 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 136 cmhytvrtPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVG 215
Cdd:PRK11809 768 --------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVG 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 216 EALVSHPEVPLISFTGSQPTAeRITQLS-------APHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEIC- 287
Cdd:PRK11809 840 AALVADARVRGVMFTGSTEVA-RLLQRNlagrldpQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCs 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 288 ----LCtsrifVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARilcgegVDQLSL 363
Cdd:PRK11809 919 alrvLC-----LQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRP------VFQAAR 987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 364 P--LRNQAGYFMLPTVIT-DIKDEsrcMTEEIFGPVTCVVPFDSEE--EVITRANSVRYGLAATVWSKDVGRIHRVAKKL 438
Cdd:PRK11809 988 EnsEDWQSGTFVPPTLIElDSFDE---LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSA 1064
|
410 420 430
....*....|....*....|....*....|....*.
gi 30520135 439 QSGlvwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:PRK11809 1065 HVG----NLYVNR--NMvgavvgvqPFGGEGLSGTG 1094
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
60-486 |
1.94e-42 |
|
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: 156.23 E-value: 1.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 60 AWSS---RSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLARTMDIpRSVLNFRFFASSNLHHVSE--------C 128
Cdd:cd07132 10 AFSSgktRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEI-LLVKNEIKYAISNLPEWMKpepvkknlA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 129 TQMSHLgcmhYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKL----LDKAGVPpgvi 204
Cdd:cd07132 89 TLLDDV----YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELipkyLDKECYP---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 205 niVFGTGPRVGEALVSHpEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEecipATVR----SSF 280
Cdd:cd07132 161 --VVLGGVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDID----VAARriawGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 281 ANQGEICLCTSRIFVQRSIYSEFLKRFVEATRKWkvgVPSDP--SANMGALISKAHLEKvrsyvLKAQTEGARILCGEGV 358
Cdd:cd07132 234 INAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF---YGEDPkeSPDYGRIINDRHFQR-----LKKLLSGGKVAIGGQT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 359 DQLSLplrnqagyFMLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKL 438
Cdd:cd07132 306 DEKER--------YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNT 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 30520135 439 QSGLVWTNCWLIREL--NLPFGGMKSSGIGREGAKDSYDFFTEIKTITIK 486
Cdd:cd07132 378 SSGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
137-487 |
4.67e-40 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 151.14 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 137 MHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKL----LDKAGVPPGVINIVFGtGP 212
Cdd:PLN02315 147 MMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLvaevLEKNNLPGAIFTSFCG-GA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 213 RVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSR 292
Cdd:PLN02315 226 EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRR 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 293 IFVQRSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVLKAQTEGARILCGEGVDQlslplrnQAGYF 372
Cdd:PLN02315 306 LLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE-------SEGNF 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 373 MLPTVItDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSglvwtNCWLIrE 452
Cdd:PLN02315 379 VQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGS-----DCGIV-N 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 30520135 453 LNLP---------FGGMKSSGIGREGAKDSYDFFTEIKTITIKY 487
Cdd:PLN02315 452 VNIPtngaeiggaFGGEKATGGGREAGSDSWKQYMRRSTCTINY 495
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
144-483 |
1.21e-38 |
|
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: 145.63 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 144 PVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGtGPRVGEALVSHpE 223
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 224 VPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSF-ANQGEICLCTSRIFVQRSIYSE 302
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 303 FLKRFVEATRKWkVGVPSDPSANMGALISKAHLEKVrSYVLKAQTEGARILCGEGVDQLSLplrnqagyFMLPTVITDIK 382
Cdd:cd07137 258 LIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRL-SRLLDDPSVADKIVHGGERDEKNL--------YIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 383 DESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRELN--LPFGGM 460
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIdtLPFGGV 407
|
330 340
....*....|....*....|...
gi 30520135 461 KSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07137 408 GESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
144-484 |
3.29e-32 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 128.69 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 144 PVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGtGPRVGEALVSHPe 223
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHK- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 224 VPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVR------SSFAnqGEICLCTSRIFVQR 297
Cdd:PLN02203 185 WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTKVAVNRivggkwGSCA--GQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 298 SiYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYvLKAQTEGARILCGEGVDQLSLplrnqagyFMLPTV 377
Cdd:PLN02203 263 R-FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNL-LKDPRVAASIVHGGSIDEKKL--------FIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 378 ITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIREL--NL 455
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSL 412
|
330 340
....*....|....*....|....*....
gi 30520135 456 PFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:PLN02203 413 PFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
59-448 |
8.82e-31 |
|
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: 123.89 E-value: 8.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 59 PAWSSRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTLTLArtMDIPRSVLNFRFFA----SSNLHHVSECTQMSHL 134
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA--ENICGDQVQLRARAfviySYRIPHEPGNHLGQGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 135 GCMHYTVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAG-VPPGVINIVFGTGpR 213
Cdd:cd07084 91 KQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDG-K 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 214 VGEALVSHPEVPLISFTGSQPTAERItqLSAPHCKKLSLELGGKNPAIIFEDAN-----LEECipatVRSSFANQGEICL 288
Cdd:cd07084 170 TMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQavdyvAWQC----VQDMTACSGQKCT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 289 CTSRIFVQRSIYSE-FLKRFVEATRKWKVGvpsdpsanmGALISKAHLEKVRSYVLKAQTEGARILCgegVDQLSLPLRN 367
Cdd:cd07084 244 AQSMLFVPENWSKTpLVEKLKALLARRKLE---------DLLLGPVQTFTTLAMIAHMENLLGSVLL---FSGKELKNHS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 368 QAGYF------MLPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRY--GLAATVWSKDVGRIHRVAKKLQ 439
Cdd:cd07084 312 IPSIYgacvasALFVPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMhgSLTAAIYSNDPIFLQELIGNLW 391
|
410
....*....|
gi 30520135 440 S-GLVWTNCW 448
Cdd:cd07084 392 VaGRTYAILR 401
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
10-432 |
7.75e-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: 113.13 E-value: 7.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 10 LENFIGGKFL-PCNSYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:cd07128 1 LQSYVAGQWHaGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 Q------AESKD-----QGKTLTLARTMDIPRSVLNfrffaSSNLHHVSECTQMSHLGCM---HytVRTPV-GIAGLISP 153
Cdd:cd07128 81 AlsaatgATRRDswidiDGGIGTLFAYASLGRRELP-----NAHFLVEGDVEPLSKDGTFvgqH--ILTPRrGVAVHINA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 154 WNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGV-PPGVINIVFGTgprVGEALVSHPEVPLISFTGS 232
Cdd:cd07128 154 FNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQDVVAFTGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 233 QPTAER------ITQLSAPhckkLSLELGGKNPAIIFEDANleeciPAT----------VRSSFANQGEICLCTSRIFVQ 296
Cdd:cd07128 231 AATAAKlrahpnIVARSIR----FNAEADSLNAAILGPDAT-----PGTpefdlfvkevAREMTVKAGQKCTAIRRAFVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 297 RSIYSEFLKRFVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYVlKAQTEGARILCGEGVDQLSLPLRNQAGYFMLPT 376
Cdd:cd07128 302 EARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVGADAEKGAFFPPT 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30520135 377 VIT-DIKDESRCMTE-EIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKD--------------VGRIH 432
Cdd:cd07128 381 LLLcDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafarelvlgaapyHGRLL 452
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
141-483 |
4.20e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.91 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 141 VRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAgVPPGVINIVFGTGPRVGEALvs 220
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALL-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 221 HPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEecipATVRSSFA-----NQGEICLCTSRIFV 295
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLK----VTVRRIIAgkwgcNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 296 QRsiysEFLKRFVEATRKWK---VGVPSDPSANMGALISKAHLEKVrSYVLKAQTEGARILCGEGVDQLSLPLRnqagyf 372
Cdd:PLN02174 262 TK----EYAPKVIDAMKKELetfYGKNPMESKDMSRIVNSTHFDRL-SKLLDEKEVSDKIVYGGEKDRENLKIA------ 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 373 mlPTVITDIKDESRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKLQSGLVWTNCWLIRE 452
Cdd:PLN02174 331 --PTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHL 408
|
330 340 350
....*....|....*....|....*....|...
gi 30520135 453 L--NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PLN02174 409 AlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
10-438 |
1.84e-25 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 109.41 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 10 LENFIGGKFLPCN-SYIDSYDPSTGEVYCKVPNSGKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELA 88
Cdd:PRK11903 5 LANYVAGRWQAGSgAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 89 QAESKDQGKTLTLArTMDIPRSVLNFRFFAS-----SNLHHVSECTQMShLG------CMHYTVRTPvGIAGLISPWNLP 157
Cdd:PRK11903 85 DIATANSGTTRNDS-AVDIDGGIFTLGYYAKlgaalGDARLLRDGEAVQ-LGkdpafqGQHVLVPTR-GVALFINAFNFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 158 LYLLTWKIAPAIAAGNTVIAKPSemtSVTAWM---FCKLLDKAGV-PPGVINIVFGTGPRVGEALvshPEVPLISFTGSQ 233
Cdd:PRK11903 162 AWGLWEKAAPALLAGVPVIVKPA---TATAWLtqrMVKDVVAAGIlPAGALSVVCGSSAGLLDHL---QPFDVVSFTGSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 234 PTAERITQLSA--PHCKKLSLELGGKNPAIIFEDAN-----LEECIPATVRSSFANQGEICLCTSRIFVQRSIYSEFLKR 306
Cdd:PRK11903 236 ETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 307 FVEATRKWKVGVPSDPSANMGALISKAHLEKVRSYvLKAQTEGARILCGEGVDQLsLPLRNQAGYFMLPT--VITDIKDE 384
Cdd:PRK11903 316 LAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAG-LAALRAQAEVLFDGGGFAL-VDADPAVAACVGPTllGASDPDAA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 30520135 385 SRCMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAATVWSKDVGRIHRVAKKL 438
Cdd:PRK11903 394 TAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
58-427 |
2.25e-25 |
|
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: 108.40 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 58 FPAWSSRSPQERSLVLNRLADVLEQSLEEL---AQAESKdqgktLTLAR-TMDIPRSVLNFRFFASsnlhhvsECTQMSH 133
Cdd:cd07129 12 FESYRALSPARRAAFLEAIADEIEALGDELvarAHAETG-----LPEARlQGELGRTTGQLRLFAD-------LVREGSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 134 LGCMHYT---------------VRTPVGIAGLISPWNLPLYLLTW--KIAPAIAAGNTVIAKP-------SEMTSVTAwm 189
Cdd:cd07129 80 LDARIDPadpdrqplprpdlrrMLVPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAhpahpgtSELVARAI-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 190 fCKLLDKAGVPPGVINIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA--PHCKKLSLELGGKNPAIIFEDAn 267
Cdd:cd07129 158 -RAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAarPEPIPFYAELGSVNPVFILPGA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 268 LEECiPATVRSSFA-----NQGEICLCTSRIFVQRsiySEFLKRFVEATRKWKVGVPSDPSANMGalISKAHLEKVRSyv 342
Cdd:cd07129 236 LAER-GEAIAQGFVgsltlGAGQFCTNPGLVLVPA---GPAGDAFIAALAEALAAAPAQTMLTPG--IAEAYRQGVEA-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 343 LKAQTeGARILCGEGVDqlslPLRNQAGYFMLPTVITD-IKDESrcMTEEIFGPVTCVVPFDSEEEVITRANSVRYGLAA 421
Cdd:cd07129 308 LAAAP-GVRVLAGGAAA----EGGNQAAPTLFKVDAAAfLADPA--LQEEVFGPASLVVRYDDAAELLAVAEALEGQLTA 380
|
....*.
gi 30520135 422 TVWSKD 427
Cdd:cd07129 381 TIHGEE 386
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
12-434 |
1.57e-14 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 75.61 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 12 NFIGGKFLPCNSYIDSYDPSTGEVYCKVPNSgKEEIEAAVEAAREAFPAWSSRSPQERSLVLNRLADVLEQSLEELAQAE 91
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKFISVPDT-DEDEINEFVDSLRQCPKSGLHNPLKNPERYLLYGDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 92 SKDQGKTLTlARTMdiPRS--------VLNFRF---FASSNLHHVSECTQMS--HLGCMHYTVRTPVGIAGLISPWNLPL 158
Cdd:cd07126 80 VEDFFARLI-QRVA--PKSdaqalgevVVTRKFlenFAGDQVRFLARSFNVPgdHQGQQSSGYRWPYGPVAIITPFNFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 159 YLLTWKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVGEaLVSHPEVPLISFTGSQPTAER 238
Cdd:cd07126 157 EIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK-ILLEANPRMTLFTGSSKVAER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 239 itqlsaphckkLSLELGGKnpaIIFEDANLEECI--PATV----------RSSFANQGEICLCTSRIFVQRS-IYSEFLK 305
Cdd:cd07126 236 -----------LALELHGK---VKLEDAGFDWKIlgPDVSdvdyvawqcdQDAYACSGQKCSAQSILFAHENwVQAGILD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 306 RFVEATRKWKVgvpSD----PSANMGALISKAHLEKVrsyvlkAQTEGARILCGegvdqlSLPLRNQ---AGY-FMLPTV 377
Cdd:cd07126 302 KLKALAEQRKL---EDltigPVLTWTTERILDHVDKL------LAIPGAKVLFG------GKPLTNHsipSIYgAYEPTA 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30520135 378 I------TDIKDESRCMTEEIFGPVTCVVPFDSEEE--VITRANSVRYGLAATVWSKDVGRIHRV 434
Cdd:cd07126 367 VfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
63-322 |
2.47e-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: 74.57 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 63 SRSPQERSLVLNRLADVLEQSLEELAQAESKDQGKTL-----TLARTMDIPRSVLNFRFFAS----SNLHHVSECTQMSH 133
Cdd:cd07077 12 VNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIrsliaNWIAMMGCSESKLYKNIDTErgitASVGHIQDVLLPDN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 134 LGCmhYTVRTPVGIAGLISPWNLPLYLLTwKIAPAIAAGNTVIAKPSEMTSVTAWMFcKLLDKAGVPPGVINIVFGTGP- 212
Cdd:cd07077 92 GET--YVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAL-ALLFQAADAAHGPKILVLYVPh 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 213 ---RVGEALVSHPEVPLISFTGSqPTAERITQLSAPHckKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLC 289
Cdd:cd07077 168 psdELAEELLSHPKIDLIVATGG-RDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACAS 244
|
250 260 270
....*....|....*....|....*....|...
gi 30520135 290 TSRIFVQRSIYSEFLKRFVEATRKWKVGVPSDP 322
Cdd:cd07077 245 EQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQET 277
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
138-434 |
8.80e-11 |
|
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: 64.04 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 138 HYTVrTPVGIAGLISPWNLPlyllTWKIAPA----IAAGNTVIAKPSEMTSVTAWMFCK----LLDKAGVPPGVINIV-F 208
Cdd:cd07127 188 TFTV-VPRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPHPAAILPLAITVQvareVLAEAGFDPNLVTLAaD 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 209 GTGPRVGEALVSHPEVPLISFTGSQPTAERITQlsapHCKKLSL--ELGGKNPAIIFEDANLEECIPATVRSSFANQGEI 286
Cdd:cd07127 263 TPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEA----NARQAQVytEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQM 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 287 CLCTSRIFVQRS---------IYSEFLKRFVEATRKWkVGVPSDPSANMGALISKAHLEKVRsyvlKAQTEGARILCGEG 357
Cdd:cd07127 339 CTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIA----EARQLGEVLLASEA 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 358 VDQLSLPlrnQAGYFMLPTVITDIKDESRcMTEEIFGPVTCVVPFDSEEEVITRA-NSVRY--GLAATVWSKDVGRIHRV 434
Cdd:cd07127 414 VAHPEFP---DARVRTPLLLKLDASDEAA-YAEERFGPIAFVVATDSTDHSIELArESVREhgAMTVGVYSTDPEVVERV 489
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
144-448 |
2.23e-08 |
|
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: 56.35 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 144 PVG-IAGLI---SPWNLPLYlltwKIAPAIAAGNTVIAKPSEMTSVTAWMFCKLL----DKAGVPPGVINIVFGTGPRVG 215
Cdd:cd07122 95 PVGvIAALIpstNPTSTAIF----KALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIEEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 216 EALVSHPEVPLISFTGSQPTAEritqlSAPHCKKLSLELG-GKNPAIIFEDANLEECIPATVRS-SFANqGEICLCTSRI 293
Cdd:cd07122 171 QELMKHPDVDLILATGGPGMVK-----AAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 294 FVQRSIYSEFLKRFveatrkwkvgvpsdpSANMGALISKAHLEKVRSYVLKaqteGARILCGEGVDQLSLPLRNQAGyFM 373
Cdd:cd07122 245 IVDDEIYDEVRAEL---------------KRRGAYFLNEEEKEKLEKALFD----DGGTLNPDIVGKSAQKIAELAG-IE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 374 LP---TVI----TDIKDESRcMTEEIFGPVTCVVPFDSEEEVITRANS-VRYGLA---ATVWSKDVGRIHRVAKKLQSGL 442
Cdd:cd07122 305 VPedtKVLvaeeTGVGPEEP-LSREKLSPVLAFYRAEDFEEALEKARElLEYGGAghtAVIHSNDEEVIEEFALRMPVSR 383
|
....*.
gi 30520135 443 VWTNCW 448
Cdd:cd07122 384 ILVNTP 389
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
140-344 |
1.55e-07 |
|
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: 53.42 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 140 TVRTPVGIAGLISPWNLPLYLLTWKIAPAIAAGNTVIAKP----SEMTSVTAWMFCKLLDKAGVPPGVINIVFGTGPRVG 215
Cdd:cd07081 91 IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520135 216 EALVSHPEVPLISFTGsqptAERITQLSAPHCKKLSLELGGKNPAIIFEDANLEECIPATVRSSFANQGEICLCTSRIFV 295
Cdd:cd07081 171 QRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30520135 296 QRSIYSEFLKRFVEatrkwkvgvpsdpsaNMGALISKAHLEKVRSYVLK 344
Cdd:cd07081 247 VDSVYDEVMRLFEG---------------QGAYKLTAEELQQVQPVILK 280
|
|
| |
