|
Name |
Accession |
Description |
Interval |
E-value |
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
24-507 |
0e+00 |
|
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: 918.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 24 IKLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:TIGR02299 1 IGHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK-RWAELKAAERKRYLHKIADLIEQHADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQTRKQVSRSANNFRFYADTVKSQMYGEVYQVDdEFINYTVRSAVGVAGLITPWNAPFMLETWKIAP 183
Cdd:TIGR02299 80 IAVLECLDCGQPLRQTRQQVIRAAENFRFFADKCEEAMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 184 ALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADAL 263
Cdd:TIGR02299 159 ALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 264 KRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIG 343
Cdd:TIGR02299 239 KRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETEVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 344 PLIKTEHYNNVKKYLKIAEEEGCEIISG------VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETE 417
Cdd:TIGR02299 319 PLIHPEHLAKVLGYVEAAEKEGATILVGgeraptFRGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 418 VIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHVAI 497
Cdd:TIGR02299 399 AIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVALAL 478
|
490
....*....|
gi 22778556 498 GDHHIPQFGK 507
Cdd:TIGR02299 479 GPHHIPKFGK 488
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
43-495 |
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 22778556 43 NISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRK- 121
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG-WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 122 QVSRSANNFRFYADTVKsQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPL 201
Cdd:cd07093 80 DIPRAAANFRFFADYIL-QLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 202 TANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFED 281
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 282 ADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIA 361
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 362 EEEGCEIISGVIPKELNR---GNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDM 438
Cdd:cd07093 319 RAEGATILTGGGRPELPDlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 22778556 439 KRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
22-495 |
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: 657.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 22 DDIKLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFkGEWGNLKQVERLEYVYKIGDLIEQHT 101
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF-PAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 102 DEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKsQMYGEVYQVDDE-FINYTVRSAVGVAGLITPWNAPFMLETWK 180
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEAR-RLYGETIPSDAPgTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 181 IAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGA 260
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 261 DALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNT 340
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 341 QIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIE 420
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 421 KANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQN-VRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTtGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
32-493 |
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: 623.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 32 FMDAEDRgTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLD 111
Cdd:pfam00171 1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP-AWRKTPAAERAAILRKAADLLEERKDELAELETLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 112 TGLPISQTRKQVSRSANNFRFYADtVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTV 191
Cdd:pfam00171 79 NGKPLAEARGEVDRAIDVLRYYAG-LARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 192 ILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELG 271
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 272 GKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHY 351
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 352 NNVKKYLKIAEEEGCEIISGVIPKELNrGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAG 431
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAGLDN-GYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22778556 432 YVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRT-PFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
44-491 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 564.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFK-GEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQ 122
Cdd:cd07114 2 INPATGEPWARVPEASAADVDRAVAAARAAFEgGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VSRSANNFRFYA---DTVKsqmyGEVYQVD-DEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEW 198
Cdd:cd07114 82 VRYLAEWYRYYAglaDKIE----GAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 199 SPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIV 278
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 279 FEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYL 358
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 359 KIAEEEGCEIISGVIP---KELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWT 435
Cdd:cd07114 318 ARAREEGARVLTGGERpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 436 NDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
64-495 |
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: 558.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 64 DKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKSQMYG 143
Cdd:cd07078 1 DAAVAAARAAFKA-WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 144 EVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIV 223
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 224 HGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERC 303
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 304 TANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELNRGNYV 383
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 384 APTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNV-RD 462
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAE 399
|
410 420 430
....*....|....*....|....*....|...
gi 22778556 463 LRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07078 400 PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
25-495 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 557.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFK-GEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFEtGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQTRK-QVSRSANNFRFYA---DtvksQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETW 179
Cdd:cd07091 85 LAALESLDNGKPLEESAKgDVALSIKCLRYYAgwaD----KIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 180 KIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNG 259
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 260 ADA-LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLEN 338
Cdd:cd07091 241 AKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 339 NTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGViPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEV 418
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGG-ERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22778556 419 IEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
43-497 |
0e+00 |
|
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: 545.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 43 NISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQ 122
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA-WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 -VSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPL 201
Cdd:cd07115 80 dVPRAADTFRYYAGWA-DKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 202 TANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFED 281
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 282 ADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIA 361
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 362 EEEGCEIISGViPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRG 441
Cdd:cd07115 319 REEGARLLTGG-KRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 442 HRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHVAI 497
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
27-495 |
0e+00 |
|
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: 534.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 27 YINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAF-KGEWGNLKQVERLEYVYKIGDLIEQHTDEIA 105
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 106 ILESLDTGLPISQTRKQVSRSANNFRFYADTVKSqMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPAL 185
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATK-ETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 186 ATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKR 265
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 266 FSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPL 345
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 346 IKTEHYNNVKKYLKIAEEEGCEIISG---VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKA 422
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGgkrPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22778556 423 NDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
40-493 |
0e+00 |
|
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: 524.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 40 TFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFK-GEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQ 118
Cdd:cd07112 3 TFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 119 TRK-QVSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAE 197
Cdd:cd07112 83 ALAvDVPSAANTFRWYAEAI-DKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 198 WSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA-LKRFSMELGGKSPI 276
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 277 IVFEDA-DLERALDAATWGIFsFN-GERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNV 354
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIF-WNqGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 355 KKYLKIAEEEGCEIISG-VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYV 433
Cdd:cd07112 321 LGYIESGKAEGARLVAGgKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 434 WTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
24-495 |
5.33e-179 |
|
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: 511.19 E-value: 5.33e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 24 IKLYINGEFMdAEDRgTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:TIGR03216 1 IRNFINGAFV-ESGK-TFANINPVDGRVIARVHEAGAAEVDAAVAAARAALKGPWGKMTVAERADLLYAVADEIERRFDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQTRK-QVSRSANNFRFYADTVKsQMYGEVYQVD----DEFINYTVRSAVGVAGLITPWNAPFMLET 178
Cdd:TIGR03216 79 FLAAEVADTGKPRSLASHlDIPRGAANFRVFADVVK-NAPTECFEMAtpdgKGALNYAVRKPLGVVGVISPWNLPLLLMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 179 WKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFG-ETAGDALVKHPDVQLISFTGETTTGSTIMR 257
Cdd:TIGR03216 158 WKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGpDSAGEFLTRHPGVDAITFTGETRTGSAIMK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 258 NGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLE 337
Cdd:TIGR03216 238 AAADGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 338 NNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISG----VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFN 413
Cdd:TIGR03216 318 PATNMGPLISAEHRDKVLSYYALAVEEGATVVTGggvpDFGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 414 DETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:TIGR03216 398 SEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNV 477
|
..
gi 22778556 494 HV 495
Cdd:TIGR03216 478 CI 479
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
24-495 |
9.73e-176 |
|
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: 503.09 E-value: 9.73e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 24 IKLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQT-RKQVSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIA 182
Cdd:cd07144 88 LAAIEALDSGKPYHSNaLGDLDEIIAVIRYYAGWA-DKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 183 PALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA 262
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRV-WNIRVGDPLENNTQ 341
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 342 IGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPK--ELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVI 419
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKApeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 420 EKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
26-494 |
5.54e-175 |
|
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: 500.49 E-value: 5.54e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 26 LYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIA 105
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA-WSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 106 ILESLDTGLPISQTRK-QVSRSANNFRFYADTVKSqmYGEVYQVDDEFInytVRSAVGVAGLITPWNAPFMLETWKIAPA 184
Cdd:cd07138 80 QAITLEMGAPITLARAaQVGLGIGHLRAAADALKD--FEFEERRGNSLV---VREPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 185 LATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALK 264
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 265 RFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGP 344
Cdd:cd07138 235 RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 345 LIKTEHYNNVKKYLKIAEEEGCEIISG--VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKA 422
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGARLVAGgpGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22778556 423 NDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSqNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIH 494
Cdd:cd07138 395 NDTPYGLAGYVWSADPERARAVARRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
44-495 |
1.11e-173 |
|
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: 496.57 E-value: 1.11e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK-TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYADTVKsQMYGEVyqVDDEFIN---YTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSP 200
Cdd:cd07103 81 DYAASFLEWFAEEAR-RIYGRT--IPSPAPGkriLVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 201 LTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFE 280
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 281 DADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKI 360
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 361 AEEEGCEIISGVIPKElNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKR 440
Cdd:cd07103 318 AVAKGAKVLTGGKRLG-LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 441 GHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
43-498 |
1.57e-170 |
|
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: 488.74 E-value: 1.57e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 43 NISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQ 122
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK-EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VSRSANNFRFYADTVKSqMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLT 202
Cdd:cd07090 80 IDSSADCLEYYAGLAPT-LSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 203 ANRMAEIIDQAGLPDGVFNIVHGFGETaGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDA 282
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 283 DLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAE 362
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 363 EEGCEIISG----VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDM 438
Cdd:cd07090 318 QEGAKVLCGgervVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 439 KRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHVAIG 498
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
25-499 |
9.49e-168 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 482.84 E-value: 9.49e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEI 104
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK-IWAAMTAMERSRILRRAVDILRERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 105 AILESLDTGLPISQTRK-QVSRSANNFRFYADTVKSqMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAP 183
Cdd:PRK13252 87 AALETLDTGKPIQETSVvDIVTGADVLEYYAGLAPA-LEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 184 ALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETaGDALVKHPDVQLISFTGETTTGSTIMRNGADAL 263
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 264 KRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIG 343
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 344 PLIKTEHYNNVKKYLKIAEEEGCEIISG---VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIE 420
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGARLLCGgerLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIA 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22778556 421 KANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHVAIGD 499
Cdd:PRK13252 405 RANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
25-495 |
1.01e-165 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 477.61 E-value: 1.01e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEI 104
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT-WGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 105 AILESLDTGLPISQTRK-QVSRSANNFRFYADTVKSQMyGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAP 183
Cdd:cd07559 81 AVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQE-GSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 184 ALATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADAL 263
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 264 KRFSMELGGKSPIIVFEDA-----DLERALDAATWGiFSFN-GERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLE 337
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLG-FAFNqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 338 NNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELN---RGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFND 414
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 415 ETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIH 494
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
.
gi 22778556 495 V 495
Cdd:cd07559 478 V 478
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
27-491 |
2.33e-165 |
|
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: 476.22 E-value: 2.33e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 27 YINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFkGEWGNLKQVERLEYVYKIGDLIEQHTDEIAI 106
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ-GEWAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 107 LESLDTGLPISQTRK-QVSRSANNFRFYADtVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPAL 185
Cdd:TIGR01804 80 LETLDTGKTLQETIVaDMDSGADVFEFFAG-LAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 186 ATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKR 265
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 266 FSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPL 345
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 346 IKTEHYNNVKKYLKIAEEEGCEIIS-GVIPK--ELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKA 422
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATgGGRPEnvGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22778556 423 NDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
25-495 |
1.04e-162 |
|
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: 469.91 E-value: 1.04e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFK--GEWGNLKQVERLEYVYKIGDLIEQHTD 102
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgSPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 103 EIAILESLDTGLPIS-QTRKQVSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKI 181
Cdd:cd07141 88 YLASLETLDNGKPFSkSYLVDLPGAIKVLRYYAGWA-DKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 182 APALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRN-GA 260
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAaGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 261 DALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNT 340
Cdd:cd07141 247 SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 341 QIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKElNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIE 420
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHG-DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIE 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 421 KANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07141 406 RANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
44-493 |
3.41e-162 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 467.48 E-value: 3.41e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKGEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTA 203
Cdd:cd07109 82 EAAARYFEYYGGAA-DKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 204 NRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDAD 283
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 284 LERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLEnNTQIGPLIKTEHYNNVKKYLKIAEE 363
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 364 EGCEIISG--VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRG 441
Cdd:cd07109 320 RGARIVAGgrIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 22778556 442 HRVAHAIDSGMLWVNSQ-NVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07109 400 LRVARRLRAGQVFVNNYgAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
27-495 |
2.74e-161 |
|
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: 465.96 E-value: 2.74e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 27 YINGEFMDAEDrgTFDNISPFS-NEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIA 105
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPA-WRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 106 ILESLDTGLPISQTRKQVSRSANNFRFYADTVkSQMYGEVYQ-VDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPA 184
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEA-LRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 185 LATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALK 264
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 265 RFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGP 344
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 345 LIKTEHYNNVKKYLKIAEEEGCEIISGVIP-KELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKAN 423
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22778556 424 DVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVR-DLRTPFGGSKDSGIG-REGGHYAFEFYTEQKIIHV 495
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
26-495 |
4.24e-160 |
|
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: 462.81 E-value: 4.24e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 26 LYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAF-KGEWGNLKQVERLEYVYKIGDLIEQHTDEI 104
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 105 AILESLDTGLPISQTRK-QVSRSANNFRFYADTVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAP 183
Cdd:cd07139 81 ARLWTAENGMPISWSRRaQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 184 ALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGfGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADAL 263
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 264 KRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIG 343
Cdd:cd07139 240 ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 344 PLIKTEHYNNVKKYLKIAEEEGCEIIS-GVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKA 422
Cdd:cd07139 320 PLASARQRERVEGYIAKGRAEGARLVTgGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22778556 423 NDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVrDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07139 400 NDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL-DFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
44-495 |
7.85e-158 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 456.40 E-value: 7.85e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRK-Q 122
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS-WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VSRSANNFRFYAD---TVKSQMYGEvYQVDdeFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWS 199
Cdd:cd07092 81 LPGAVDNFRFFAGaarTLEGPAAGE-YLPG--HTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 200 PLTANRMAEIIdQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVF 279
Cdd:cd07092 158 PLTTLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 280 EDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLK 359
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 360 IAEEEGCEIISGVIPKElnRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMK 439
Cdd:cd07092 317 RAPAHARVLTGGRRAEG--PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 440 RGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKiiHV 495
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIK--HV 448
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
44-493 |
4.74e-157 |
|
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: 454.50 E-value: 4.74e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPR-WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYAD---TVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSP 200
Cdd:cd07110 81 DDVAGCFEYYADlaeQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 201 LTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFE 280
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 281 DADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKI 360
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 361 AEEEGCEII-SGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMK 439
Cdd:cd07110 321 GKEEGARLLcGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 22778556 440 RGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
26-495 |
9.33e-157 |
|
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: 454.68 E-value: 9.33e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 26 LYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGEWG-NLKQVERLEYVYKIGDLIEQHTDEI 104
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGlKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 105 AILESLDTGLPISQTRK-QVSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAP 183
Cdd:cd07143 89 ASIEALDNGKTFGTAKRvDVQASADTFRYYGGWA-DKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 184 ALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA- 262
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSn 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQI 342
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 343 GPLIKTEHYNNVKKYLKIAEEEGCEIISGViPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKA 422
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGG-KRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22778556 423 NDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
27-495 |
1.04e-156 |
|
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: 454.50 E-value: 1.04e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 27 YINGEFMDAEDRGTFDNISP-FSNEKINSVASGQAADIDKAVQSAKKAFkGEWGNLKQVERLEYVYKIGDLIEQHTDEIA 105
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAF-PEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 106 ILESLDTGLPISQTRKQVsRSANNFRFYADTVKSQMYGEVyqVDDEFIN---YTVRSAVGVAGLITPWNAPFMLETWKIA 182
Cdd:cd07131 81 RLVTREMGKPLAEGRGDV-QEAIDMAQYAAGEGRRLFGET--VPSELPNkdaMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 183 PALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA 262
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQI 342
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 343 GPLIKTEHYNNVKKYLKIAEEEGCEI-ISGVIPKE--LNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVI 419
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLlLGGERLTGggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22778556 420 EKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNV-RDLRTPFGGSKDSGIG-REGGHYAFEFYTEQKIIHV 495
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
25-491 |
2.41e-156 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 454.58 E-value: 2.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFK----GEWGNLKQVERLEYVYKIGDLIEQH 100
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 101 TDEIAILESLDTGLPISQTRKQVSRSANNFRFYAD---TVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLE 177
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADlaeALDAKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 178 TWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMR 257
Cdd:PLN02467 169 TWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 258 NGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLE 337
Cdd:PLN02467 249 AAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 338 NNTQIGPLIKTEHYNNVKKYLKIAEEEGCEII-SGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDET 416
Cdd:PLN02467 329 EGCRLGPVVSEGQYEKVLKFISTAKSEGATILcGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTED 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 417 EVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:PLN02467 409 EAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
27-495 |
1.44e-155 |
|
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: 451.33 E-value: 1.44e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 27 YINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAI 106
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK-AWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 107 LESLDTGLPISQTRKQVSRSANNFRFYADTVKSqMYGEVYQVD--DEFInYTVRSAVGVAGLITPWNAPFMLETWKIAPA 184
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWARR-IEGEIIPSDrpNENI-FIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 185 LATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALK 264
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 265 RFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGP 344
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 345 LIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKAND 424
Cdd:cd07088 318 LVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22778556 425 VRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
25-491 |
1.68e-155 |
|
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: 451.18 E-value: 1.68e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAF-KGEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFdEGPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQTR-KQVSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIA 182
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWA-DKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 183 PALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA 262
Cdd:cd07142 164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 -LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQ 341
Cdd:cd07142 244 nLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 342 IGPLIKTEHYNNVKKYLKIAEEEGCEIISGviPKEL-NRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIE 420
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITG--GDRIgSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22778556 421 KANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
68-495 |
1.25e-154 |
|
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: 445.14 E-value: 1.25e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 68 QSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKSQMYGEVYQ 147
Cdd:cd06534 1 AAARAAFK-AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 148 VDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFG 227
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 228 ETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANS 307
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 308 RLYLHESIADEFIEKLKqrvwnirvgdplenntqigpliktehynnvkkylkiaeeegceiisgvipkelnrgnyvapTI 387
Cdd:cd06534 240 RLLVHESIYDEFVEKLV-------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 388 LLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNV-RDLRTP 466
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAP 338
|
410 420
....*....|....*....|....*....
gi 22778556 467 FGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
44-495 |
2.12e-154 |
|
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: 447.55 E-value: 2.12e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAF-KGEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQ 122
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VSRSANNFRfYADTVKSQMYGEVYQ-VDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPL 201
Cdd:cd07118 82 IEGAADLWR-YAASLARTLHGDSYNnLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 202 TANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFED 281
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 282 ADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIA 361
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 362 EEEGCEIISGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRG 441
Cdd:cd07118 321 RAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 22778556 442 HRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
44-495 |
6.07e-154 |
|
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: 446.81 E-value: 6.07e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPI-SQTRKQ 122
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFP-EWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VSRSANNFRFYADtVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLT 202
Cdd:cd07108 81 AAVLADLFRYFGG-LAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 203 ANRMAEIIDQAgLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDA 282
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 283 DLERALDAATWGI-FSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIA 361
Cdd:cd07108 239 DLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 362 -EEEGCEIISGVIPKE---LNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTND 437
Cdd:cd07108 319 lSTSGATVLRGGPLPGegpLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22778556 438 MKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREgghYAFE----FYTEQKIIHV 495
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGRE---ASLEgmleHFTQKKTVNI 457
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
44-495 |
6.13e-154 |
|
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: 446.44 E-value: 6.13e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFP-EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTA 203
Cdd:cd07107 81 MVAAALLDYFAGLV-TELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 204 NRMAEIIDQAgLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDAD 283
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 284 LERALDAATWGI-FSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAE 362
Cdd:cd07107 239 PEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 363 EEGCEIISG-VIPK--ELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMK 439
Cdd:cd07107 319 REGARLVTGgGRPEgpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 440 RGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
21-480 |
7.01e-152 |
|
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: 442.22 E-value: 7.01e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 21 LDDIK----LYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDL 96
Cdd:cd07111 15 LDAHDrsfgHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES-WSALPGHVRARHLYRIARH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 97 IEQHTDEIAILESLDTGLPISQTRK-QVSRSANNFRFYAdtvksqmyGEVYQVDDEFINYtvrSAVGVAGLITPWNAPFM 175
Cdd:cd07111 94 IQKHQRLFAVLESLDNGKPIRESRDcDIPLVARHFYHHA--------GWAQLLDTELAGW---KPVGVVGQIVPWNFPLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 176 LETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETaGDALVKHPDVQLISFTGETTTGSTI 255
Cdd:cd07111 163 MLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 256 MRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDP 335
Cdd:cd07111 242 RRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 336 LENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEII--SGVIPKElnrGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFN 413
Cdd:cd07111 322 LDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFqpGADLPSK---GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFR 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22778556 414 DETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGG 480
Cdd:cd07111 399 TAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGG 465
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
43-495 |
9.42e-152 |
|
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: 441.30 E-value: 9.42e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 43 NISPFSNEKINSVASGQAADIDKAVQSAKKAF-KGEWGnLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTR- 120
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFdTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 121 KQVSRSANNFRFYADTVKSQMYGEVYQVDDEFINYT----VRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPA 196
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 197 EWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPI 276
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 277 IVFEDADLERALDAATwGIFSFN-GERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVK 355
Cdd:cd07089 240 IVLDDADLAAAAPAAV-GVCMHNaGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 356 KYLKIAEEEGCEIISGV-IPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVW 434
Cdd:cd07089 319 GYIARGRDEGARLVTGGgRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22778556 435 TNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
23-497 |
3.29e-151 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 440.50 E-value: 3.29e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 23 DIKLYINGEFMDAEDRgTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFkGEWGNLKQVERLEYVYKIGDLIEQHTD 102
Cdd:PRK13473 2 QTKLLINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF-PEWSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 103 EIAILESLDTGLPISQTRK-QVSRSANNFRFYADTVKS---QMYGEvYQVDdeFINYTVRSAVGVAGLITPWNAPFMLET 178
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARClegKAAGE-YLEG--HTSMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 179 WKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRN 258
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 259 GADALKRFSMELGGKSPIIVFEDADLERALD-AATWGIFSfNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLE 337
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEgIRTFGYYN-AGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 338 NNTQIGPLIKTEHYNNVKKYLKIAEEEGC-EIISGVIPKELNrGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDET 416
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVERAKALGHiRVVTGGEAPDGK-GYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 417 EVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKiiHVA 496
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR--HVM 471
|
.
gi 22778556 497 I 497
Cdd:PRK13473 472 V 472
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
25-495 |
1.49e-150 |
|
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: 438.81 E-value: 1.49e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEI 104
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK-TWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 105 AILESLDTGLPISQTRK-QVSRSANNFRFYADTVKSQMyGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAP 183
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEE-GSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 184 ALATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADAL 263
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 264 KRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIG 343
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 344 PLIKTEHYNNVKKYLKIAEEEGCEIISG---VIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIE 420
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTGghrLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 421 KANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
25-497 |
1.48e-147 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 431.63 E-value: 1.48e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAF-KGEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFeRGDWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQT-RKQVSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIA 182
Cdd:PRK09847 101 LALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAI-DKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 183 PALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA 262
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 -LKRFSMELGGKSPIIVFEDA-DLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNT 340
Cdd:PRK09847 260 nMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 341 QIGPLIKTEHYNNVKKYLKIAEEEGCEIISGvipKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIE 420
Cdd:PRK09847 340 TMGTLIDCAHADSVHSFIREGESKGQLLLDG---RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22778556 421 KANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHVAI 497
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
26-491 |
4.88e-146 |
|
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: 427.24 E-value: 4.88e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 26 LYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGEWGNLKQVERLEYVYKIGDLIEQHTDEIA 105
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 106 ILESLDTGLPISQTRK-QVSRSANNFRFYA--------DTVKSQ---MYGEVYQVddefinYTVRSAVGVAGLITPWNAP 173
Cdd:cd07113 82 QLETLCSGKSIHLSRAfEVGQSANFLRYFAgwatkingETLAPSipsMQGERYTA------FTRREPVGVVAGIVPWNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 174 FMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETaGDALVKHPDVQLISFTGETTTGS 253
Cdd:cd07113 156 VMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 254 TIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVG 333
Cdd:cd07113 235 KIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 334 DPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISG--VIPKElnrGNYVAPTILLNASNEMRVVQEEIFGPVIAVMT 411
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGgeALAGE---GYFVQPTLVLARSADSRLMREETFGPVVSFVP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 412 FNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:cd07113 392 YEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELK 471
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
62-495 |
7.27e-146 |
|
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: 425.02 E-value: 7.27e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 62 DIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRfYADTVKSQM 141
Cdd:cd07104 1 DVDRAYAAAAAAQK-AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILR-EAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 142 YGEVYQVDDE-FINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRM-AEIIDQAGLPDGV 219
Cdd:cd07104 79 EGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 220 FNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFN 299
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 300 GERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGvipkELNR 379
Cdd:cd07104 239 GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTG----GTYE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 380 GNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQN 459
Cdd:cd07104 315 GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQT 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 22778556 460 VRDLRT-PFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07104 395 VNDEPHvPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
44-495 |
4.12e-145 |
|
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: 423.86 E-value: 4.12e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG-WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYADTVKSQmygEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTA 203
Cdd:cd07106 81 GGAVAWLRYTASLDLPD---EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 204 NRMAEIIDQAgLPDGVFNIVHGFGEtAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDAD 283
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 284 LERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEE 363
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 364 EGCEIISGVIPKELNrGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHR 443
Cdd:cd07106 316 KGAKVLAGGEPLDGP-GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 22778556 444 VAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07106 395 VARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
25-499 |
9.06e-145 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 425.00 E-value: 9.06e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFK-GEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTG-LPISQTRKQVSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIA 182
Cdd:PLN02766 102 LAALDTIDAGkLFALGKAVDIPAAAGLLRYYAGAA-DKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 183 PALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA 262
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 -LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQ 341
Cdd:PLN02766 261 nLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 342 IGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKElNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEK 421
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCG-DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKK 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22778556 422 ANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHVAIGD 499
Cdd:PLN02766 420 ANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPLYN 497
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
25-493 |
5.90e-144 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 424.22 E-value: 5.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAF-KGEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdEGPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQTRK-QVSRSANNFRFYADTVkSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIA 182
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKaELPMFARLFRYYAGWA-DKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 183 PALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA 262
Cdd:PLN02466 218 PALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 -LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQ 341
Cdd:PLN02466 298 nLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 342 IGPLIKTEHYNNVKKYLKIAEEEGCEIISGViPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEK 421
Cdd:PLN02466 378 QGPQIDSEQFEKILRYIKSGVESGATLECGG-DRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRR 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22778556 422 ANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:PLN02466 457 ANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
44-493 |
1.95e-143 |
|
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: 419.69 E-value: 1.95e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAK-EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYADTVKsQMYGEVYQVD-----DEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEW 198
Cdd:cd07149 83 DRAIETLRLSAEEAK-RLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 199 SPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRngADALKRFSMELGGKSPIIV 278
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIAR--KAGLKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 279 FEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYL 358
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 359 KIAEEEGCEIISGvipkELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDM 438
Cdd:cd07149 320 EEAVEGGARLLTG----GKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 439 KRGHRVAHAIDSGMLWVN-SQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07149 396 QKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
27-491 |
8.44e-139 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 408.88 E-value: 8.44e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 27 YINGEFmDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAI 106
Cdd:cd07086 2 VIGGEW-VGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK-EWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 107 LESLDTGLPISQTRKQV-------------SRsannfRFYADTVKSQMYGEVyqvddefiNYTVRSAVGVAGLITPWNAP 173
Cdd:cd07086 80 LVSLEMGKILPEGLGEVqemidicdyavglSR-----MLYGLTIPSERPGHR--------LMEQWNPLGVVGVITAFNFP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 174 FMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQA----GLPDGVFNIVHGFGEtAGDALVKHPDVQLISFTGET 249
Cdd:cd07086 147 VAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGST 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 250 TTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWN 329
Cdd:cd07086 226 EVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 330 IRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGviPKELNR---GNYVAPTILLNASNEMRVVQEEIFGPV 406
Cdd:cd07086 306 VRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTG--GKRIDGgepGNYVEPTIVTGVTDDARIVQEETFAPI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 407 IAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRV--AHAIDSGMLWVN-SQNVRDLRTPFGGSKDSGIGREGGHYA 483
Cdd:cd07086 384 LYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNiPTSGAEIGGAFGGEKETGGGRESGSDA 463
|
....*...
gi 22778556 484 FEFYTEQK 491
Cdd:cd07086 464 WKQYMRRS 471
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
41-495 |
1.45e-138 |
|
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: 407.10 E-value: 1.45e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 41 FDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTR 120
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPA-WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 121 KQVSRSANNFRFYADTVKsQMYGEVYQVDDE-FINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWS 199
Cdd:cd07150 80 FETTFTPELLRAAAGECR-RVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 200 PLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVF 279
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 280 EDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLK 359
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 360 IAEEEGCEIISGvipkELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMK 439
Cdd:cd07150 319 DAVAKGAKLLTG----GKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 22778556 440 RGHRVAHAIDSGMLWVNSQNVRDLRT-PFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07150 395 RAFKLAERLESGMVHINDPTILDEAHvPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
44-495 |
4.49e-138 |
|
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: 405.96 E-value: 4.49e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKG-EWGNLKQVeRLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQ 122
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VSRSANNFRFYADTVKSqMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLT 202
Cdd:cd07120 81 ISGAISELRYYAGLART-EAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 203 ANRMAEIIDQA-GLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFED 281
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 282 ADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIA 361
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 362 EEEGCEII--SGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMK 439
Cdd:cd07120 320 IAAGAEVVlrGGPVTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 440 RGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
41-493 |
1.05e-136 |
|
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: 402.50 E-value: 1.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 41 FDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTR 120
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD-VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 121 KQVSRSANNFRFYADTVKsQMYGEVYQVDD-----EFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKP 195
Cdd:cd07145 80 VEVERTIRLFKLAAEEAK-VLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 196 AEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSP 275
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 276 IIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVK 355
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 356 KYLKIAEEEGCEIISGVipkELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWT 435
Cdd:cd07145 319 NLVNDAVEKGGKILYGG---KRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 22778556 436 NDMKRGHRVAHAIDSGMLWVN-SQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07145 396 NDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
11-499 |
2.03e-136 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 403.30 E-value: 2.03e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 11 SGKHEELANKLDDIKLY-----INGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVE 85
Cdd:PLN02278 7 SMDAQSALVKLRNAGLLrtqglIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP-SWSKLTASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 86 RLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKsQMYGEVyqVDDEFIN---YTVRSAVG 162
Cdd:PLN02278 86 RSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAK-RVYGDI--IPSPFPDrrlLVLKQPVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 163 VAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQL 242
Cdd:PLN02278 163 VVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 243 ISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEK 322
Cdd:PLN02278 243 ITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 323 LKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELNrGNYVAPTILLNASNEMRVVQEEI 402
Cdd:PLN02278 323 FSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLG-GTFYEPTVLGDVTEDMLIFREEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 403 FGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHY 482
Cdd:PLN02278 402 FGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKY 481
|
490
....*....|....*..
gi 22778556 483 AFEFYTEQKiiHVAIGD 499
Cdd:PLN02278 482 GIDEYLEIK--YVCLGN 496
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
25-495 |
4.18e-134 |
|
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: 397.25 E-value: 4.18e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFK-GEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFEnGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQTRK-QVSRSANNFRFYADTVkSQMYGEVYQVDDEFIN----YTVRSAVGVAGLITPWNAPFMLET 178
Cdd:cd07140 87 LATIESLDSGAVYTLALKtHVGMSIQTFRYFAGWC-DKIQGKTIPINQARPNrnltLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 179 WKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRN 258
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 259 GADA-LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLE 337
Cdd:cd07140 246 CAVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 338 NNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGviPKELNR-GNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDE- 415
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYG--GKQVDRpGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGd 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 416 -TEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIH 494
Cdd:cd07140 404 vDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVT 483
|
.
gi 22778556 495 V 495
Cdd:cd07140 484 I 484
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
27-496 |
2.21e-132 |
|
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: 392.59 E-value: 2.21e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 27 YINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAI 106
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA-WGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 107 LESLDTGLPISQT-RKQVSRSANNFRFYADTVKSQMyGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPAL 185
Cdd:cd07116 83 AETWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQE-GSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 186 ATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKR 265
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 266 FSMELGGKSPIIVFE------DADLERALDAATwgIFSFN-GERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLEN 338
Cdd:cd07116 241 VTLELGGKSPNIFFAdvmdadDAFFDKALEGFV--MFALNqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 339 NTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISG----VIPKELNRGNYVAPTILlnASNEMRVVQEEIFGPVIAVMTFND 414
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGgernELGGLLGGGYYVPTTFK--GGNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 415 ETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIH 494
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
..
gi 22778556 495 VA 496
Cdd:cd07116 477 VS 478
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
30-495 |
2.22e-131 |
|
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: 389.36 E-value: 2.22e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 30 GEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILES 109
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQK-EWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 110 LDTGLPISQTRKQVSRSANNFRfYADTVKSQMYGEVYQVDDEFI-NYTVRSAVGVAGLITPWNAPFMLETWKIAPALATG 188
Cdd:cd07151 80 RESGSTRIKANIEWGAAMAITR-EAATFPLRMEGRILPSDVPGKeNRVYREPLGVVGVISPWNFPLHLSMRSVAPALALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 189 NTVILKPAEWSPLTANRM-AEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFS 267
Cdd:cd07151 159 NAVVLKPASDTPITGGLLlAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 268 MELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIK 347
Cdd:cd07151 239 LELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLIN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 348 TEHYNNVKKYLKIAEEEGCEIISGVIPKelnrGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRY 427
Cdd:cd07151 319 ESQVDGLLDKIEQAVEEGATLLVGGEAE----GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22778556 428 GLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDL-RTPFGGSKDSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07151 395 GLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
25-493 |
1.29e-123 |
|
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: 369.59 E-value: 1.29e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 25 KLYINGEFMDAEDRgTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGEWGNLKQVERLEYVYKIGDLIEQHTDEI 104
Cdd:cd07082 3 KYLINGEWKESSGK-TIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 105 AILESLDTGLPISQTRKQVSRSANNFRFYADTVKSqMYGEVYQVD-----DEFINYTVRSAVGVAGLITPWNAPFMLETW 179
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKR-LDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 180 KIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNG 259
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 260 AdaLKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENN 339
Cdd:cd07082 241 P--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 340 TQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGvipKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVI 419
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATVLNG---GGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAI 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 420 EKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRT-PFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07082 396 ELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
42-493 |
2.97e-120 |
|
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: 360.59 E-value: 2.97e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 42 DNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRK 121
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN-RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 122 QVSRSANNFRFYADTVKsQMYGEVYQVDDEFIN-----YTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPA 196
Cdd:cd07094 81 EVDRAIDTLRLAAEEAE-RIRGEEIPLDATQGSdnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 197 EWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGadALKRFSMELGGKSPI 276
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA--GGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 277 IVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKK 356
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 357 YLKIAEEEGCEIISGVIPKelnrGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTN 436
Cdd:cd07094 318 WVEEAVEAGARLLCGGERD----GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 22778556 437 DMKRGHRVAHAIDSGMLWVN-SQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
26-493 |
1.85e-118 |
|
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: 358.07 E-value: 1.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 26 LYINGEFMDAEDrgTFDNISPF-SNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEI 104
Cdd:cd07124 35 LVIGGKEVRTEE--KIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP-TWRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 105 AILESLDTGLPISQTRKQVSRSANNFRFYADTVKSQMYGEVYQVDDEfINYTVRSAVGVAGLITPWNAPFMLETWKIAPA 184
Cdd:cd07124 112 AAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGE-DNRYVYRPLGVGAVISPWNFPLAILAGMTTAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 185 LATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMR------N 258
Cdd:cd07124 191 LVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYEraakvqP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 259 GADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLEN 338
Cdd:cd07124 271 GQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 339 NTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEV 418
Cdd:cd07124 351 EVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEA 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22778556 419 IEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDL--RTPFGGSKDSGIG-REGGHYAFEFYTEQKII 493
Cdd:cd07124 431 LEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALvgRQPFGGFKMSGTGsKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
62-493 |
1.28e-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: 353.04 E-value: 1.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 62 DIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVkSQM 141
Cdd:cd07105 1 DADQAVEAAAAAFP-AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLI-TQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 142 YGEVYQVDDE-FINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVF 220
Cdd:cd07105 79 IGGSIPSDKPgTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 221 NIVHGFGETAG---DALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFS 297
Cdd:cd07105 159 NVVTHSPEDAPevvEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 298 FNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDplennTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKEL 377
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 378 NRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNS 457
Cdd:cd07105 314 PSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING 393
|
410 420 430
....*....|....*....|....*....|....*..
gi 22778556 458 QNVRDLRT-PFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07105 394 MTVHDEPTlPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
63-486 |
8.37e-117 |
|
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: 350.61 E-value: 8.37e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 63 IDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKSQMY 142
Cdd:cd07100 1 IEAALDRAHAAFL-AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 143 GEVYQVDDEfINYTVRSAVGVAGLITPWNAPFmletWKI----APALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDG 218
Cdd:cd07100 80 DEPIETDAG-KAYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 219 VFNIVHGFGETAgDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSF 298
Cdd:cd07100 155 VFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 299 NGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELN 378
Cdd:cd07100 234 AGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 379 rGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQ 458
Cdd:cd07100 314 -GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM 392
|
410 420
....*....|....*....|....*....
gi 22778556 459 NVRDLRTPFGGSKDSGIGREGGHYAF-EF 486
Cdd:cd07100 393 VKSDPRLPFGGVKRSGYGRELGRFGIrEF 421
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
24-493 |
1.64e-116 |
|
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: 351.82 E-value: 1.64e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 24 IKLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP-AWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQTRKQVSRSANNFRFyADTVKSQMYGE-VYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIA 182
Cdd:cd07085 80 LARLITLEHGKTLADARGDVLRGLEVVEF-ACSIPHLLKGEyLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 183 PALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGfGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA 262
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQI 342
Cdd:cd07085 238 GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 343 GPLIKTEHYNNVKKYLKIAEEEGCEII---SGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVI 419
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVldgRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 420 EKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNsqnvrdLRTP-------FGGSKDSGIGrEGGHY---AFEFYTE 489
Cdd:cd07085 398 AIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN------VPIPvplaffsFGGWKGSFFG-DLHFYgkdGVRFYTQ 470
|
....
gi 22778556 490 QKII 493
Cdd:cd07085 471 TKTV 474
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
20-497 |
1.86e-114 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 346.51 E-value: 1.86e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 20 KLDDIKL-----YINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIG 94
Cdd:PRK11241 2 QLNDSTLfrqqaLINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA-WRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 95 DLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKsQMYGEV---YQVDDEFInyTVRSAVGVAGLITPWN 171
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGK-RIYGDTipgHQADKRLI--VIKQPIGVTAAITPWN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 172 APFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTT 251
Cdd:PRK11241 158 FPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 252 GSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIR 331
Cdd:PRK11241 238 GRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 332 VGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELNrGNYVAPTILLNASNEMRVVQEEIFGPVIAVMT 411
Cdd:PRK11241 318 IGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG-GNFFQPTILVDVPANAKVAKEETFGPLAPLFR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 412 FNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:PRK11241 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
....*.
gi 22778556 492 IIHVAI 497
Cdd:PRK11241 477 YMCIGL 482
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
46-493 |
1.75e-112 |
|
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: 340.49 E-value: 1.75e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 46 PFSNEKINSVASGQAADIDKAVQSAKkafkGEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSR 125
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAA----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 126 SANNFRFYADTVKsQMYGEVYQVDD-----EFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSP 200
Cdd:cd07146 82 AADVLRFAAAEAL-RDDGESFSCDLtangkARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 201 LTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMrnGADALKRFSMELGGKSPIIVFE 280
Cdd:cd07146 161 LSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIA--ATAGYKRQLLELGGNDPLIVMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 281 DADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKI 360
Cdd:cd07146 239 DADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 361 AEEEGCEIISGvipkELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKR 440
Cdd:cd07146 319 AIAQGARVLLG----NQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 441 GHRVAHAIDSGMLWVNSQ-NVRDLRTPFGGSKDSGIG-REGGHYAFEFYTEQKII 493
Cdd:cd07146 395 IKRLVERLDVGTVNVNEVpGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
44-493 |
1.75e-111 |
|
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: 338.04 E-value: 1.75e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR-AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYADTVksqmyGEVyqVDDEFINY-----TVRSAV-----GVAGLITPWNAPFMLETWKIAPALATGNTVIL 193
Cdd:cd07099 80 LLALEAIDWAARNA-----PRV--LAPRKVPTgllmpNKKATVeyrpyGVVGVISPWNYPLLTPMGDIIPALAAGNAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 194 KPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETaGDALVKHPdVQLISFTGETTTGSTIMRNGADALKRFSMELGGK 273
Cdd:cd07099 153 KPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 274 SPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNN 353
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 354 VKKYLKIAEEEGCEIISGViPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYV 433
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGG-ARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22778556 434 WTNDMKRGHRVAHAIDSGMLWVNS--QNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07099 390 FSRDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
50-489 |
6.07e-109 |
|
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: 331.18 E-value: 6.07e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 50 EKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANN 129
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQR-AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 130 FrFYADTVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRM-AE 208
Cdd:cd07152 81 L-HEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVViAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 209 IIDQAGLPDGVFNIVHGFGEtAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERAL 288
Cdd:cd07152 160 LFEEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 289 DAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEI 368
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 369 ISGVIPKELnrgnYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAI 448
Cdd:cd07152 319 EAGGTYDGL----FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 22778556 449 DSGMLWVNSQNVRD-LRTPFGGSKDSGIG-REGGHYAFEFYTE 489
Cdd:cd07152 395 RTGMLHINDQTVNDePHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
44-494 |
9.57e-106 |
|
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: 323.04 E-value: 9.57e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG-WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYADTVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTA 203
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 204 NRMAEIIDQAGLPDGVFNIVHGFGETaGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDAD 283
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 284 LERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEE 363
Cdd:cd07102 239 LDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 364 EGCEIISGviPKELNR----GNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMK 439
Cdd:cd07102 319 KGARALID--GALFPEdkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 440 RGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQKIIH 494
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYH 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
41-491 |
9.07e-102 |
|
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: 313.03 E-value: 9.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 41 FDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTR 120
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR-PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 121 KQVSRSANNFRFYADTVkSQMYGEVYQVD-----DEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKP 195
Cdd:cd07147 80 GEVARAIDTFRIAAEEA-TRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 196 AEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAgDALVKHPDVQLISFTGETTTGSTIM-RNGAdalKRFSMELGGKS 274
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKaRAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 275 PIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNV 354
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 355 KKYLKIAEEEGCEIISGvipkELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVW 434
Cdd:cd07147 315 EGWVNEAVDAGAKLLTG----GKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 435 TNDMKRGHRVAHAIDSGMLWVNsqNVRDLRT---PFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVIN--DVPTFRVdhmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
44-489 |
7.44e-101 |
|
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: 310.78 E-value: 7.44e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQV 123
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQR-AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 124 SRSANNFRFYADTVKSQMYGEVYQVDDEFINYTV--RSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPL 201
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRGAIPVLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 202 TANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDvqLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFED 281
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 282 ADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIA 361
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 362 EEEGCEIISGVIPKElNRGNYV-APTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKR 440
Cdd:cd07101 318 VAKGATVLAGGRARP-DLGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 22778556 441 GHRVAHAIDSGMLWVNSQNVR---DLRTPFGGSKDSGIGREGGHYAFEFYTE 489
Cdd:cd07101 397 GRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTE 448
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
34-489 |
3.32e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 308.73 E-value: 3.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 34 DAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAfKGEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTG 113
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 114 lpisQTRK----QVSRSANNFRFYA----DTVKSQMYGEVYQVddefINYTV--RSAVGVAGLITPWNAPFMLETWKIAP 183
Cdd:PRK09407 106 ----KARRhafeEVLDVALTARYYArrapKLLAPRRRAGALPV----LTKTTelRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 184 ALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDvqLISFTGETTTGSTIMRNGADAL 263
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNAD--YLMFTGSTATGRVLAEQAGRRL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 264 KRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIG 343
Cdd:PRK09407 256 IGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 344 PLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKElNRGNYV-APTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKA 422
Cdd:PRK09407 336 SLISEAQLETVSAHVDDAVAKGATVLAGGKARP-DLGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 423 NDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLwvnsqNVRD--------LRTPFGGSKDSGIGREGGHYAFEFYTE 489
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTV-----NVNEgyaaawgsVDAPMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
26-480 |
1.43e-98 |
|
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: 306.79 E-value: 1.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 26 LYINGEFMDAEdrGTFDNISPFSNEK-INSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEI 104
Cdd:TIGR01237 35 LVINGERVETE--NKIVSINPCDKSEvVGTVSKASQEHAEHALQAAAKAFE-AWKKTDPEERAAILFKAAAIVRRRRHEF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 105 AILESLDTGLPISQTRKQVSRSANNFRFYADT-VKSQMYGEVYQVDDEfINYTVRSAVGVAGLITPWNAPFMLETWKIAP 183
Cdd:TIGR01237 112 SALLVKEVGKPWNEADAEVAEAIDFMEYYARQmIELAKGKPVNSREGE-TNQYVYTPTGVTVVISPWNFPFAIMVGMTVA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 184 ALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTI------MR 257
Cdd:TIGR01237 191 PIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIferaakVQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 258 NGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLE 337
Cdd:TIGR01237 271 PGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 338 NNTQIGPLIKTEHYNNVKKYLKIAEEEgCEIISGVIPKElNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETE 417
Cdd:TIGR01237 351 ADVYVGPVIDQKSFNKIMEYIEIGKAE-GRLVSGGCGDD-SKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDE 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 418 VIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDL--RTPFGGSKDSGIGREGG 480
Cdd:TIGR01237 429 ALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIvgYQPFGGFKMSGTDSKAG 493
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
23-474 |
2.87e-96 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 300.70 E-value: 2.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 23 DIKLYINGEFMDAEDrgTFDNISPfSN--EKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQH 100
Cdd:PRK03137 36 DYPLIIGGERITTED--KIVSINP-ANksEVVGRVSKATKELAEKAMQAALEAFE-TWKKWSPEDRARILLRAAAIIRRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 101 TDEIAILESLDTGLPISQTRKQVSRSANNFRFYA-DTVKSQMYGEVYQVDDEFiNYTVRSAVGVAGLITPWNAPFMLETW 179
Cdd:PRK03137 112 KHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYArQMLKLADGKPVESRPGEH-NRYFYIPLGVGVVISPWNFPFAIMAG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 180 KIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNG 259
Cdd:PRK03137 191 MTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 260 ADA------LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVG 333
Cdd:PRK03137 271 AKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 334 DPlENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVipKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFN 413
Cdd:PRK03137 351 NP-EDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGE--GDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 414 DETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNsqnvrdlRT---------PFGGSKDSG 474
Cdd:PRK03137 428 DFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN-------RGctgaivgyhPFGGFNMSG 490
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
92-495 |
2.42e-95 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 295.11 E-value: 2.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 92 KIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKsQMYGEVYQVDDEFIN-YTVRSAVGVAGLITPW 170
Cdd:PRK10090 3 KIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR-RYEGEIIQSDRPGENiLLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 171 NAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETT 250
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 251 TGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNI 330
Cdd:PRK10090 162 AGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 331 RVGDPLENNT-QIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKElNRGNYVAPTILLNASNEMRVVQEEIFGPVIAV 409
Cdd:PRK10090 242 QFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE-GKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 410 MTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAFEFYTE 489
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQ 400
|
....*.
gi 22778556 490 QKIIHV 495
Cdd:PRK10090 401 TQVVYL 406
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
46-480 |
1.82e-84 |
|
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: 268.78 E-value: 1.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 46 PFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGlpisqtrkqvsr 125
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQR-EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTG------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 126 sannfrfyaDTVKSQMYGEVYqVDDEFINYTV---------------------RSAV-----GVAGLITPWNAPFMLETW 179
Cdd:cd07098 70 ---------KTMVDASLGEIL-VTCEKIRWTLkhgekalrpesrpggllmfykRARVeyeplGVVGAIVSWNYPFHNLLG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 180 KIAPALATGNTVILKPAEWSPLTANRMAEIIDQA----GLPDGVFNIVHGFGETaGDALVKHPDVQLISFTGETTTGSTI 255
Cdd:cd07098 140 PIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 256 MRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDP 335
Cdd:cd07098 219 MAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 336 LENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPK---ELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTF 412
Cdd:cd07098 299 LDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22778556 413 NDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVN----SQNVRDLrtPFGGSKDSGIGREGG 480
Cdd:cd07098 379 SDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvNYYVQQL--PFGGVKGSGFGRFAG 448
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
39-487 |
2.69e-84 |
|
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: 268.31 E-value: 2.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 39 GTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQ 118
Cdd:cd07130 12 GVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK-EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 119 TRKQV-------------SRSannfrFYADTVKSQ-----MYgEVYQvddefinytvrsAVGVAGLITPWNAPFMLETWK 180
Cdd:cd07130 91 GLGEVqemidicdfavglSRQ-----LYGLTIPSErpghrMM-EQWN------------PLGVVGVITAFNFPVAVWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 181 IAPALATGNTVILKPAEWSPLTA----NRMAEIIDQAGLPDGVFNIVHGfGETAGDALVKHPDVQLISFTGETTTGSTIM 256
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLTAiavtKIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 257 RNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPL 336
Cdd:cd07130 232 QAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 337 ENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGviPKELNR-GNYVAPTIlLNASNEMRVVQEEIFGPVIAVMTFNDE 415
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFG--GKVIDGpGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22778556 416 TEVIEKANDVRYGLAGYVWTNDMKRGHRV--AHAIDSGMLWVN-SQNVRDLRTPFGGSKDSGIGREGGHYAFEFY 487
Cdd:cd07130 389 EEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNiGTSGAEIGGAFGGEKETGGGRESGSDAWKQY 463
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
24-492 |
2.84e-82 |
|
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: 264.06 E-value: 2.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 24 IKLYINGEFMDAEDRGTfdNISPFS-NEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTD 102
Cdd:cd07083 19 YPLVIGGEWVDTKERMV--SVSPFApSEVVGTTAKADKAEAEAALEAAWAAFK-TWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 103 EIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKSQMYG--EVYQVDDEfINYTVRSAVGVAGLITPWNAPFMLETWK 180
Cdd:cd07083 96 ELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPavEVVPYPGE-DNESFYVGLGAGVVISPWNFPVAIFTGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 181 IAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGA 260
Cdd:cd07083 175 IVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 261 D------ALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGD 334
Cdd:cd07083 255 RlapgqtWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 335 PLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKelNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFND 414
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLE--GEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 415 E--TEVIEKANDVRYGLAGYVWTNdmKRGH--RVAHAIDSGMLWVNSQNVRDL--RTPFGGSKDSGIGREGG--HYAFEF 486
Cdd:cd07083 413 DdfAEALEVANSTPYGLTGGVYSR--KREHleEARREFHVGNLYINRKITGALvgVQPFGGFKLSGTNAKTGgpHYLRRF 490
|
....*.
gi 22778556 487 YTEQKI 492
Cdd:cd07083 491 LEMKAV 496
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
24-493 |
3.01e-82 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 263.28 E-value: 3.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 24 IKLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDE 103
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLT-WGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 104 IAILESLDTGLPISQTRKQVSRSANNFRfYADTVKSQMYGE-VYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIA 182
Cdd:TIGR01722 80 IAELITAEHGKTHSDALGDVARGLEVVE-HACGVNSLLKGEtSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 183 PALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGfGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADA 262
Cdd:TIGR01722 159 IAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 263 LKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESiADEFIEKLKQRVWNIRVGDPLENNTQI 342
Cdd:TIGR01722 238 GKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 343 GPLIKTEHYNNVKKYLKIAEEEGCEII---SGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVI 419
Cdd:TIGR01722 317 GPLITPQAKDRVASLIAGGAAEGAEVLldgRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 420 EKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQnvrdLRTP-----FGGSKDSGIGREG--GHYAFEFYTEQKI 492
Cdd:TIGR01722 397 ALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP----IPVPlpyfsFTGWKDSFFGDHHiyGKQGTHFYTRGKT 472
|
.
gi 22778556 493 I 493
Cdd:TIGR01722 473 V 473
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
28-489 |
2.29e-79 |
|
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: 257.12 E-value: 2.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 28 INGEFMDAEDRGTFdnISPFSNEK-INSVASGQAADIDKAVQSAKKAFkGEWGNLKQVERLEYVYKIGDLIEQHTDE-IA 105
Cdd:cd07125 37 INGEETETGEGAPV--IDPADHERtIGEVSLADAEDVDAALAIAAAAF-AGWSATPVEERAEILEKAADLLEANRGElIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 106 ILeSLDTGLPISQTRKQVsRSANNF-RFYADTVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPA 184
Cdd:cd07125 114 LA-AAEAGKTLADADAEV-REAIDFcRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 185 LATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTI-----MRNG 259
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLInralaERDG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 260 ADAlkRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENN 339
Cdd:cd07125 272 PIL--PLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 340 TQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKelNRGNYVAPTILLNASNEmrVVQEEIFGPVIAVMTFNDET--E 417
Cdd:cd07125 350 TDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDD--GNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEDldE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 418 VIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNsqnvRD------LRTPFGGSKDSGIGREGG--HYAFEFYTE 489
Cdd:cd07125 426 AIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN----RNitgaivGRQPFGGWGLSGTGPKAGgpNYLLRFGNE 501
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
62-486 |
3.64e-78 |
|
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: 251.04 E-value: 3.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 62 DIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFyadTVKSQ- 140
Cdd:cd07095 1 QVDAAVAAARAAFPG-WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDI---SIKAYh 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 141 -MYGEVyQVDDEFINYTVR-SAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDG 218
Cdd:cd07095 77 eRTGER-ATPMAQGRAVLRhRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 219 VFNIVHGFGETaGDALVKHPDVQLISFTGETTTGSTIMRNGADAL-KRFSMELGGKSPIIVFEDADLERALDAATWGIFS 297
Cdd:cd07095 156 VLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 298 FNGERCTANSRLYLHES-IADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKE 376
Cdd:cd07095 235 TAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 377 LnRGNYVAPTILLnaSNEMRVVQ-EEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWV 455
Cdd:cd07095 315 A-GTAFLSPGIID--VTDAADVPdEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNW 391
|
410 420 430
....*....|....*....|....*....|..
gi 22778556 456 NSQ-NVRDLRTPFGGSKDSGIGREGGHYAFEF 486
Cdd:cd07095 392 NRPtTGASSTAPFGGVGLSGNHRPSAYYAADY 423
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
44-486 |
1.89e-75 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 245.03 E-value: 1.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFKgewgNLKQV---ERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTR 120
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFR----DYRTTtfaQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 121 KQVSRSANNFRFYADTVKSQMYGEVYQVDD-----EFINYtvrSAVGVAGLITPWNAPFmletWKI----APALATGNTV 191
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADEPADAAAvgasrAYVRY---QPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 192 ILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHgFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELG 271
Cdd:PRK09406 155 LLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 272 GKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHY 351
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 352 NNVKKYLKIAEEEGCEIISGVIPKElNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAG 431
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGKRPD-GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 432 YVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGRE-GGHYAFEF 486
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRElSAHGIREF 448
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
43-492 |
3.48e-74 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 241.69 E-value: 3.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 43 NISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQ 122
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR-DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VSRSANNFRFYADTVKSQMYGEVYQVDDE--FINYtvrSAVGVAGLITPWNAPFmletWKI----APALATGNTVILKPA 196
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQqaVIEY---RPLGTILAIMPWNFPL----WQVmrgaVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 197 EWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAgDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPI 276
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 277 IVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPL----IKTEHYN 352
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMarfdLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 353 NVKKYLKiaeeEGCEIISGViPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGY 432
Cdd:PRK13968 322 QVEATLA----EGARLLLGG-EKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22778556 433 VWTNDMKRGHRVAHAIDSGMLWVNSQNVRDLRTPFGGSKDSGIGREGGHYAF-EFYTEQKI 492
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLhEFCNIQTV 457
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
22-479 |
4.49e-74 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 242.35 E-value: 4.49e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 22 DDIKLYINGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHT 101
Cdd:PLN00412 14 DVYKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA-WAKTPLWKRAELLHKAAAILKEHK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 102 DEIAILESLDTGLPISQTRKQVSRSANNFRFYADT-VKSQMYGEvYQVDDEF-----INYTVRSAV--GVAGLITPWNAP 173
Cdd:PLN00412 93 APIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEgVRILGEGK-FLVSDSFpgnerNKYCLTSKIplGVVLAIPPFNYP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 174 FMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGeTTTGS 253
Cdd:PLN00412 172 VNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG-GDTGI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 254 TIMRN-GADALKrfsMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRV 332
Cdd:PLN00412 251 AISKKaGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 333 GDPlENNTQIGPLIKTEHYNNVKKYLKIAEEEGceiisGVIPKELNR-GNYVAPTILLNASNEMRVVQEEIFGPVIAVMT 411
Cdd:PLN00412 328 GPP-EDDCDITPVVSESSANFIEGLVMDAKEKG-----ATFCQEWKReGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 412 FNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVR--DlRTPFGGSKDSGIGREG 479
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARgpD-HFPFQGLKDSGIGSQG 470
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
44-493 |
1.51e-71 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 234.62 E-value: 1.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEKINSVASGQAADIDKAVQSAKKAFK--GEWgnLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRK 121
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 122 QVSRSANNFRFYADTVkSQMYGE-----VYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPA 196
Cdd:cd07148 82 EVTRAIDGVELAADEL-GQLGGReipmgLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 197 EWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAgDALVKHPDVQLISFTGETTTGsTIMRNGADALKRFSMELGGKSPI 276
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVA-EKLVTDPRVAFFSFIGSARVG-WMLRSKLAPGTRCALEHGGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 277 IVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKK 356
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 357 YLKIAEEEGCEIISGviPKELNRGNYvAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTN 436
Cdd:cd07148 319 WVNEAVAAGARLLCG--GKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTK 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 437 DMKRGHRVAHAIDSGMLWVNSQNVrdLRT---PFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07148 396 DLDVALKAVRRLDATAVMVNDHTA--FRVdwmPFAGRRQSGYGTGGIPYTMHDMTQEKMA 453
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
162-491 |
9.52e-70 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 229.42 E-value: 9.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 162 GVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFnIVHGFGETAgDALVKHPdVQ 241
Cdd:cd07134 102 GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEGDAEVA-QALLELP-FD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 242 LISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIE 321
Cdd:cd07134 179 HIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 322 KLKQRVwnIRV---GDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKElnRGNYVAPTILLNASNEMRVV 398
Cdd:cd07134 259 HLKAEI--EKFygkDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDA--AQRYIAPTVLTNVTPDMKIM 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 399 QEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNS--QNVRDLRTPFGGSKDSGIG 476
Cdd:cd07134 335 QEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDvvLHFLNPNLPFGGVNNSGIG 414
|
330
....*....|....*
gi 22778556 477 REGGHYAFEFYTEQK 491
Cdd:cd07134 415 SYHGVYGFKAFSHER 429
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
162-495 |
1.27e-68 |
|
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: 226.25 E-value: 1.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 162 GVAGLITPWNAPFMLEtwkIAP---ALATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGFGETAgDALVKHP 238
Cdd:cd07087 102 GVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVA-TALLAEP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 239 -DvqLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIAD 317
Cdd:cd07087 177 fD--HIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 318 EFIEKLKQRVwNIRVGDPLENNTQIGPLIKTEHYNNVKKYLkiaeeEGCEIISG--VIPKELnrgnYVAPTILLNASNEM 395
Cdd:cd07087 255 ELIEELKKAI-KEFYGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGgqVDKEER----YIAPTILDDVSPDS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 396 RVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQN----VRDLrtPFGGSK 471
Cdd:cd07087 325 PLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLlhaaIPNL--PFGGVG 402
|
330 340
....*....|....*....|....
gi 22778556 472 DSGIGREGGHYAFEFYTEQKIIHV 495
Cdd:cd07087 403 NSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
26-487 |
3.54e-59 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 202.88 E-value: 3.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 26 LYINGEFMdAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIA 105
Cdd:PRK09457 3 LWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA-WARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 106 ILESLDTGLPISQTRKQVSRSANNFrfyADTVKSqmYGE-VYQVDDEFINYTvrsAV------GVAGLITPWNAPFMLET 178
Cdd:PRK09457 81 EVIARETGKPLWEAATEVTAMINKI---AISIQA--YHErTGEKRSEMADGA---AVlrhrphGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 179 WKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETaGDALVKHPDVQLISFTGETTTGSTIMRN 258
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 259 -GADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESI-ADEFIEKLKQRVWNIRVGDPL 336
Cdd:PRK09457 232 fAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 337 ENNTQ-IGPLIK---TEHYNNVKKYLkiaEEEGCEIISGVIPKELNRGnYVAPTIlLNASNEMRVVQEEIFGPVIAVMTF 412
Cdd:PRK09457 312 AEPQPfMGAVISeqaAQGLVAAQAQL---LALGGKSLLEMTQLQAGTG-LLTPGI-IDVTGVAELPDEEYFGPLLQVVRY 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22778556 413 NDETEVIEKANDVRYGL-AGYVWTNDMKRGHRVAHaIDSGMLWVNSQ-NVRDLRTPFGgskdsGIGREGGHYAFEFY 487
Cdd:PRK09457 387 DDFDEAIRLANNTRFGLsAGLLSDDREDYDQFLLE-IRAGIVNWNKPlTGASSAAPFG-----GVGASGNHRPSAYY 457
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
61-491 |
8.56e-59 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 202.18 E-value: 8.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 61 ADIDKAVQSAKKAFKGewGNLKQVE-RLEYVYKIGDLIEQHTDEI--AILESLD-TGLPISQTRKQVSRSA-----NNFR 131
Cdd:PTZ00381 7 EIIPPIVKKLKESFLT--GKTRPLEfRKQQLRNLLRMLEENKQEFseAVHKDLGrHPFETKMTEVLLTVAEiehllKHLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 132 FYADTVKSQMYGeVYQVDDEFInytVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIID 211
Cdd:PTZ00381 85 EYLKPEKVDTVG-VFGPGKSYI---IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 212 QAgLPDGVFNIVHGfGETAGDALVKHPdVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAA 291
Cdd:PTZ00381 161 KY-LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 292 TWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVwnIR-VGDPLENNTQIGPLIKTEHYNNVKKYLKiaEEEGCEIIS 370
Cdd:PTZ00381 238 AWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAI--KEfFGEDPKKSEDYSRIVNEFHTKRLAELIK--DHGGKVVYG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 371 GVIPKElNRgnYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDS 450
Cdd:PTZ00381 314 GEVDIE-NK--YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSS 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 22778556 451 GMLWVNSQ--NVRDLRTPFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:PTZ00381 391 GAVVINDCvfHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPK 433
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
61-493 |
1.17e-58 |
|
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: 200.14 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 61 ADIDKAVQSAKKAFKGewGNLKQVE-RLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTR-KQVSRSANNFRFYADTVK 138
Cdd:cd07135 5 DEIDSIHSRLRATFRS--GKTKDLEyRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 139 SQMYGEVYQVDD---EFINYTVR-SAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAg 214
Cdd:cd07135 83 KWAKDEKVKDGPlafMFGKPRIRkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 215 LPDGVFNIVHGFGETAGDALVKHPDvqLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWG 294
Cdd:cd07135 162 LDPDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 295 IFSFNGERCTANSRLYLHESIADEFIEKLKqRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLkiaEEEGCEIisgVIP 374
Cdd:cd07135 240 KFGNAGQICVAPDYVLVDPSVYDEFVEELK-KVLDEFYPGGANASPDYTRIVNPRHFNRLKSLL---DTTKGKV---VIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 375 KELNRG-NYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGML 453
Cdd:cd07135 313 GEMDEAtRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 22778556 454 WVNSQ----NVRDLrtPFGGSKDSGIGREGGHYAFEFYTEQKII 493
Cdd:cd07135 393 VINDTlihvGVDNA--PFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
155-494 |
2.21e-58 |
|
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: 199.65 E-value: 2.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 155 YTVRSAVGVAGLITPWNAPFMLetwKIAP---ALATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGFGETAg 231
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEEN- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 232 DALVKHPdVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYL 311
Cdd:cd07136 170 QELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 312 HESIADEFIEKLKQRVwNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEeegceIISGVIPKELNRgnYVAPTILLNA 391
Cdd:cd07136 249 HESVKEKFIKELKEEI-KKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK-----IVFGGNTDRETL--YIEPTILDNV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 392 SNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSG--------MLWVNSQnvrdl 463
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggcindtiMHLANPY----- 395
|
330 340 350
....*....|....*....|....*....|.
gi 22778556 464 rTPFGGSKDSGIGREGGHYAFEFYTEQKIIH 494
Cdd:cd07136 396 -LPFGGVGNSGMGSYHGKYSFDTFSHKKSIL 425
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
162-491 |
2.63e-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: 199.25 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 162 GVAGLITPWNAPFMLetwKIAP---ALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVfNIVHGFGETAgDALVKHP 238
Cdd:cd07133 103 GVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVVTGGADVA-AAFSSLP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 239 DVQLIsFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADE 318
Cdd:cd07133 178 FDHLL-FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 319 FIEKLKQRVwNIRVGDpLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEIISgVIPK--ELNRGNYVAPTILLNASNEMR 396
Cdd:cd07133 257 FVAAAKAAV-AKMYPT-LADNPDYTSIINERHYARLQGLLEDARAKGARVIE-LNPAgeDFAATRKLPPTLVLNVTDDMR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 397 VVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVN------SQNvrDLrtPFGGS 470
Cdd:cd07133 334 VMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtllhvAQD--DL--PFGGV 409
|
330 340
....*....|....*....|.
gi 22778556 471 KDSGIGREGGHYAFEFYTEQK 491
Cdd:cd07133 410 GASGMGAYHGKEGFLTFSHAK 430
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
52-486 |
4.18e-58 |
|
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: 200.52 E-value: 4.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 52 INSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFR 131
Cdd:TIGR01238 65 VGQVFHANLAHVQAAIDSAQQAFP-TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 132 FYADtvksqmygevyQVDDEFINYTVRSaVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIID 211
Cdd:TIGR01238 144 YYAK-----------QVRDVLGEFSVES-RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 212 QAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGA---DALKRFSMELGGKSPIIVFEDADLERAL 288
Cdd:TIGR01238 212 EAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAqreDAPVPLIAETGGQNAMIVDSTALPEQVV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 289 DAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEEGCEI 368
Cdd:TIGR01238 292 RDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKI 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 369 ISGVI--PKELNRGNYVAPTIL-LNASNEMrvvQEEIFGPVIAVMTFN-DE-TEVIEKANDVRYGLAGYVWTNDMKRGHR 443
Cdd:TIGR01238 372 AQLTLddSRACQHGTFVAPTLFeLDDIAEL---SEEVFGPVLHVVRYKaRElDQIVDQINQTGYGLTMGVHSRIETTYRW 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 22778556 444 VAHAIDSGMLWVNSQNVRDL--RTPFGGSKDSGIGREGG--HYAFEF 486
Cdd:TIGR01238 449 IEKHARVGNCYVNRNQVGAVvgVQPFGGQGLSGTGPKAGgpHYLYRL 495
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
60-490 |
1.50e-55 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 200.93 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 60 AADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDE---IAILE---SLDTGlpISQTRKQVsrsanNF-RF 132
Cdd:COG4230 592 AADVEAALAAAQAAFPA-WSATPVEERAAILERAADLLEAHRAElmaLLVREagkTLPDA--IAEVREAV-----DFcRY 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 133 YADtvksqmygevyQVDDEFINYTVRSAVGVAGLITPWNAP---FmleTWKIAPALATGNTVILKPAEWSPLTANRMAEI 209
Cdd:COG4230 664 YAA-----------QARRLFAAPTVLRGRGVFVCISPWNFPlaiF---TGQVAAALAAGNTVLAKPAEQTPLIAARAVRL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 210 IDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTI-----MRNGADAlkRFSMELGGKSPIIVfeD--- 281
Cdd:COG4230 730 LHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInrtlaARDGPIV--PLIAETGGQNAMIV--Dssa 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 282 ------AD-LERALDAAtwgifsfnGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNV 354
Cdd:COG4230 806 lpeqvvDDvLASAFDSA--------GQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANL 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 355 KKYLKIAEEEGCEIISGVIPKELNRGNYVAPTIL-LNASNEMrvvQEEIFGPVIAVMTF--NDETEVIEKANDVRYGLAG 431
Cdd:COG4230 878 EAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIeIDSISDL---EREVFGPVLHVVRYkaDELDKVIDAINATGYGLTL 954
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22778556 432 YVWT-NDmKRGHRVAHAIDSGMLWVN---------SQnvrdlrtPFGGSKDSGIG-REGG-HYAFEFYTEQ 490
Cdd:COG4230 955 GVHSrID-ETIDRVAARARVGNVYVNrniigavvgVQ-------PFGGEGLSGTGpKAGGpHYLLRFATER 1017
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
28-493 |
2.34e-55 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 195.35 E-value: 2.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 28 INGEFMDAEDRGTFDNISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAIL 107
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP-LWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 108 ESLDTGLPISQTRKQVSRSANNFRFYADTVKSQMYGEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALAT 187
Cdd:PLN02419 197 ITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 188 GNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAgDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFS 267
Cdd:PLN02419 277 GNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQ 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 268 MELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESiADEFIEKLKQRVWNIRVGDPLENNTQIGPLIK 347
Cdd:PLN02419 356 SNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEPDADLGPVIS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 348 TEHYNNVKKYLKIAEEEGCEII---SGVIPKELNRGNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKAND 424
Cdd:PLN02419 435 KQAKERICRLIQSGVDDGAKLLldgRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINK 514
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 425 VRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQnvrdLRTP-----FGGSKDSGIGREG--GHYAFEFYTEQKII 493
Cdd:PLN02419 515 NKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVP----IPVPlpffsFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
43-487 |
5.67e-55 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 192.36 E-value: 5.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 43 NISPFSNEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQ 122
Cdd:PLN02315 38 SVNPANNQPIAEVVEASLEDYEEGLRACEEAAK-IWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VSRSANNFRfYADTVKSQMYGEVyqVDDEFINYT---VRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWS 199
Cdd:PLN02315 117 VQEIIDMCD-FAVGLSRQLNGSI--IPSERPNHMmmeVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 200 PL----TANRMAEIIDQAGLPDGVFNIVHGfGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSP 275
Cdd:PLN02315 194 PLitiaMTKLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 276 IIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVK 355
Cdd:PLN02315 273 IIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 356 KYLKIAEEEGCEIISG--VIPKElnrGNYVAPTIlLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYV 433
Cdd:PLN02315 353 KGIEIIKSQGGKILTGgsAIESE---GNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSI 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22778556 434 WTndmkRGHRV------AHAIDSGMLWVN-SQNVRDLRTPFGGSKDSGIGREGGHYAFEFY 487
Cdd:PLN02315 429 FT----RNPETifkwigPLGSDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
44-490 |
9.93e-55 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 198.11 E-value: 9.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 44 ISPFSNEK-INSVASGQAADIDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDE-IAIL-----ESLDTGlpI 116
Cdd:PRK11904 567 VSPADRRRvVGEVAFADAEQVEQALAAARAAFPA-WSRTPVEERAAILERAADLLEANRAElIALCvreagKTLQDA--I 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 117 SQTRKQVsrsanNF-RFYADTVKSQMY---------GEVyqvddefiNYTVRSAVGVAGLITPWNAPFMLETWKIAPALA 186
Cdd:PRK11904 644 AEVREAV-----DFcRYYAAQARRLFGapeklpgptGES--------NELRLHGRGVFVCISPWNFPLAIFLGQVAAALA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 187 TGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTI-----MRNGAD 261
Cdd:PRK11904 711 AGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInrtlaARDGPI 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 262 AlkRFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQ 341
Cdd:PRK11904 791 V--PLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTD 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 342 IGPLIKTEHYNNVKKYLKIAEEEGCEIISGVIPKELNRGNYVAPTILLNASneMRVVQEEIFGPVIAVMTFN--DETEVI 419
Cdd:PRK11904 869 VGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDS--ISQLEREVFGPILHVIRYKasDLDKVI 946
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 420 EKANDVRYGLagyvwT------NDmKRGHRVAHAIDSGMLWVN---------SQnvrdlrtPFGGSKDSGIG-REGG-HY 482
Cdd:PRK11904 947 DAINATGYGL-----TlgihsrIE-ETADRIADRVRVGNVYVNrnqigavvgVQ-------PFGGQGLSGTGpKAGGpHY 1013
|
....*...
gi 22778556 483 AFEFYTEQ 490
Cdd:PRK11904 1014 LLRFATEK 1021
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
49-482 |
7.91e-54 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 195.85 E-value: 7.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 49 NEKINSVASGQAADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDE-IAIL-----ESLDTGlpISQTRKQ 122
Cdd:PRK11905 578 DDVVGTVTEASAEDVERALAAAQAAFP-EWSATPAAERAAILERAADLMEAHMPElFALAvreagKTLANA--IAEVREA 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 123 VsrsanNF-RFYADtvksqmygevyQVDDEFINyTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPL 201
Cdd:PRK11905 655 V-----DFlRYYAA-----------QARRLLNG-PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPL 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 202 TANRMAEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKR---FSMELGGKSPIIV 278
Cdd:PRK11905 718 IAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGQNAMIV 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 279 FEDADLERALDAATWGIFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYL 358
Cdd:PRK11905 798 DSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHI 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 359 KIAEEEGCEIISGVIPKELNRGNYVAPTILLNASneMRVVQEEIFGPVIAVMTF--NDETEVIEKANDVRYGLAGYVWTN 436
Cdd:PRK11905 878 EAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDS--ISDLEREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSR 955
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 22778556 437 DMKRGHRVAHAIDSGMLWVN---------SQnvrdlrtPFGGSKDSGIG-REGG-HY 482
Cdd:PRK11905 956 IDETIAHVTSRIRAGNIYVNrniigavvgVQ-------PFGGEGLSGTGpKAGGpLY 1005
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
15-474 |
1.18e-50 |
|
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: 180.86 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 15 EELANKLDDIKLYINGEFMDAEDRGtfDNISPFS-NEKINSVASGQAADIDKAVQSAKKAfKGEWGNLKQVERLEYVYKI 93
Cdd:cd07123 24 AELKSLTVEIPLVIGGKEVRTGNTG--KQVMPHDhAHVLATYHYADAALVEKAIEAALEA-RKEWARMPFEDRAAIFLKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 94 GDLIE--------------Q----HTDEI-AILESLDTglpisqtrkqvsrsannFRF--------YADTVKSQMYGEVY 146
Cdd:cd07123 101 ADLLSgkyryelnaatmlgQgknvWQAEIdAACELIDF-----------------LRFnvkyaeelYAQQPLSSPAGVWN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 147 QVDdefinYtvRSAVGVAGLITPWNAPFMLETWKIAPALaTGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGF 226
Cdd:cd07123 164 RLE-----Y--RPLEGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 227 GETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALK------RFSMELGGKSPIIVFEDADLERALDAATWGIFSFNG 300
Cdd:cd07123 236 GPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 301 ERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKIAEEE-GCEIISGVIPKElNR 379
Cdd:cd07123 316 QKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDD-SV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 380 GNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDE--TEVIEKANDV-RYGLAGYVWTNDMK------RGHRVAhaidS 450
Cdd:cd07123 395 GYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfEETLELVDTTsPYALTGAIFAQDRKaireatDALRNA----A 470
|
490 500 510
....*....|....*....|....*....|.
gi 22778556 451 GMLWVNsqnvrDLRT-------PFGGSKDSG 474
Cdd:cd07123 471 GNFYIN-----DKPTgavvgqqPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
65-491 |
5.90e-45 |
|
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: 163.55 E-value: 5.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 65 KAVQSAKKAFkgEWGNLKQVE-RLEYVYKIGDLIEQHTDEIaiLESLDTGLPISQTRKQVSRSA---NNFRFYADTVKSQ 140
Cdd:cd07132 2 EAVRRAREAF--SSGKTRPLEfRIQQLEALLRMLEENEDEI--VEALAKDLRKPKFEAVLSEILlvkNEIKYAISNLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 141 MYGE------VYQVDDEFINytvRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAG 214
Cdd:cd07132 78 MKPEpvkknlATLLDDVYIY---KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 215 LPDGVFNIVHGFGETagDALVKHpDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWG 294
Cdd:cd07132 155 DKECYPVVLGGVEET--TELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 295 IFSFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNtQIGPLIKTEHYNNVKKYLkiaeeEGCEIISG--V 372
Cdd:cd07132 232 KFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLL-----SGGKVAIGgqT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 373 IPKElnrgNYVAPTILLNASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGM 452
Cdd:cd07132 306 DEKE----RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGG 381
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 22778556 453 LWVNS----QNVRDLrtPFGGSKDSGIGREGGHYAFEFYTEQK 491
Cdd:cd07132 382 VCVNDtimhYTLDSL--PFGGVGNSGMGAYHGKYSFDTFSHKR 422
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
55-480 |
7.09e-45 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 169.38 E-value: 7.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 55 VASGQAADIDKAVQSAKKAfkGE-WGNLKQVERLEYVYKIGDLIEQHTdeiailESLdTGLPISQTRKQVS------RSA 127
Cdd:PRK11809 676 VREATPAEVEQALESAVNA--APiWFATPPAERAAILERAADLMEAQM------QTL-MGLLVREAGKTFSnaiaevREA 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 128 NNF-RFYADtvksqmygevyQVDDEFINYTVRSaVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRM 206
Cdd:PRK11809 747 VDFlRYYAG-----------QVRDDFDNDTHRP-LGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQA 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 207 AEIIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGADALKR------FSMELGGKSPIIVFE 280
Cdd:PRK11809 815 VRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGGQNAMIVDS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 281 DADLER--------ALDAAtwgifsfnGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYN 352
Cdd:PRK11809 895 SALTEQvvadvlasAFDSA--------GQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKA 966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 353 NVKKYLKIAEEEGCEIISGVIPK--ELNRGNYVAPT-ILLNASNEMrvvQEEIFGPVIAVMTFNDE--TEVIEKANDVRY 427
Cdd:PRK11809 967 NIERHIQAMRAKGRPVFQAARENseDWQSGTFVPPTlIELDSFDEL---KREVFGPVLHVVRYNRNqlDELIEQINASGY 1043
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22778556 428 GLAGYVWTndmkrghR----VAHAIDS---GMLWVNsqnvRDL------RTPFGGSKDSGIGREGG 480
Cdd:PRK11809 1044 GLTLGVHT-------RidetIAQVTGSahvGNLYVN----RNMvgavvgVQPFGGEGLSGTGPKAG 1098
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
162-493 |
3.21e-43 |
|
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: 158.73 E-value: 3.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 162 GVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGfGETAGDALVKHpDVQ 241
Cdd:cd07137 103 GVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ-KWD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 242 LISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALD---AATWGifSFNGERCTANSRLYLHESIADE 318
Cdd:cd07137 180 KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRriaGGKWG--CNNGQACIAPDYVLVEESFAPT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 319 FIEKLKQRVWNIRVGDPLENNtQIGPLIKTEHYNNVKKYLKIAEEEGCEIISGvipkELNRGN-YVAPTILLNASNEMRV 397
Cdd:cd07137 258 LIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVADKIVHGG----ERDEKNlYIEPTILLDPPLDSSI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 398 VQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVRDL--RTPFGGSKDSGI 475
Cdd:cd07137 333 MTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAidTLPFGGVGESGF 412
|
330
....*....|....*...
gi 22778556 476 GREGGHYAFEFYTEQKII 493
Cdd:cd07137 413 GAYHGKFSFDAFSHKKAV 430
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
157-493 |
1.11e-36 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 141.72 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 157 VRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGfGETAGDALVK 236
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEG-AVTETTALLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 237 HpDVQLISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIVFEDADLE---RALDAATWGifSFNGERCTANSRLYLHE 313
Cdd:PLN02174 187 Q-KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKvtvRRIIAGKWG--CNNGQACISPDYILTTK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 314 SIADEFIEKLKQRVWNIRVGDPLENNtQIGPLIKTEHYNNVKKYLKiaEEEGCEIIsgVIPKELNRGNY-VAPTILLNAS 392
Cdd:PLN02174 264 EYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLD--EKEVSDKI--VYGGEKDRENLkIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 393 NEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNSQNVR-DLRT-PFGGS 470
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHlALHTlPFGGV 418
|
330 340
....*....|....*....|...
gi 22778556 471 KDSGIGREGGHYAFEFYTEQKII 493
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
65-469 |
1.65e-35 |
|
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: 137.75 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 65 KAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTrKQVSRSANNFRFYADTVKSQMY-- 142
Cdd:cd07084 3 RALLAADISTKA-ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIYSYRIph 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 143 --GEVYQVDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAG-LPDGV 219
Cdd:cd07084 81 epGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 220 FNIVHGFGETaGDALVKHPDVQLISFTGETTTGSTIMRNGADAlkRFSMELGGKSPIIVFEDADlerALDAATWGI---- 295
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQ---AVDYVAWQCvqdm 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 296 FSFNGERCTANSRLYLHESIADE-FIEKLKQRVWNIRVGDPLenntqIGPLIktehYNNVKKYLKIAEEEGCEII--SGV 372
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLL-----LGPVQ----TFTTLAMIAHMENLLGSVLlfSGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 373 IPKEL----NRGNYVAPTILLNASNEMR---VVQEEIFGPVIAVMTFNDETE--VIEKANDVRYGLAGYVWTNDMKRGHR 443
Cdd:cd07084 306 ELKNHsipsIYGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQE 385
|
410 420
....*....|....*....|....*.
gi 22778556 444 VAhaidsGMLWVNSQNVRDLRTPFGG 469
Cdd:cd07084 386 LI-----GNLWVAGRTYAILRGRTGV 406
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
162-493 |
3.58e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 137.17 E-value: 3.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 162 GVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAgLPDGVFNIVHGfGETAGDALVKHPdVQ 241
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHK-WD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 242 LISFTGETTTGSTIMRNGADALKRFSMELGGKSPIIV---FEDADLERALD---AATWGifSFNGERCTANSRLYLHESI 315
Cdd:PLN02203 187 KIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNrivGGKWG--SCAGQACIAIDYVLVEERF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 316 ADEFIEKLKQRVWNIRVGDPLENNTqIGPLIKTEHYNNVKKYLKIAEEEGCEIISGVI-PKELnrgnYVAPTILLNASNE 394
Cdd:PLN02203 265 APILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRVAASIVHGGSIdEKKL----FIEPTILLNPPLD 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 395 MRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDSGMLWVNS---QNVRDlRTPFGGSK 471
Cdd:PLN02203 340 SDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDaiiQYACD-SLPFGGVG 418
|
330 340
....*....|....*....|..
gi 22778556 472 DSGIGREGGHYAFEFYTEQKII 493
Cdd:PLN02203 419 ESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
133-480 |
3.07e-30 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 123.53 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 133 YADTVKSQMYGEVYQVDDEFINYTVRSAV----------GVAGLITPWNAPF--MLEtwKIAPALATGNTVILKPAEWSP 200
Cdd:cd07128 107 YASLGRRELPNAHFLVEGDVEPLSKDGTFvgqhiltprrGVAVHINAFNFPVwgMLE--KFAPALLAGVPVIVKPATATA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 201 LTANRMAEIIDQAG-LPDGVFNIVHGfgeTAGDaLVKHPDVQ-LISFTGETTTGST------IMRNGAdalkRFSMELGG 272
Cdd:cd07128 185 YLTEAVVKDIVESGlLPEGALQLICG---SVGD-LLDHLGEQdVVAFTGSAATAAKlrahpnIVARSI----RFNAEADS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 273 KSPIIVFEDAdlerALDAATWGIF---------SFNGERCTANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIG 343
Cdd:cd07128 257 LNAAILGPDA----TPGTPEFDLFvkevaremtVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 344 PLIKTEHYNNVKKylKIAE-EEGCEIISG------VIPKELNRGNYVAPTILL--NASNEMRVVQEEIFGPVIAVMTFND 414
Cdd:cd07128 333 PLVSREQREDVRA--AVATlLAEAEVVFGgpdrfeVVGADAEKGAFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDS 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22778556 415 ETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAIDS--GMLWVNSQNVRDLRT----PFGGSKDSGIGREGG 480
Cdd:cd07128 411 LAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLNRDSAKESTghgsPLPQLVHGGPGRAGG 482
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
63-437 |
1.16e-28 |
|
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: 118.03 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 63 IDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTRKQVSRSANNFRFYADTVKSQMY 142
Cdd:cd07129 1 VDAAAAAAAAAFE-SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREGSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 143 GEVyQVDDEFINYT------VRS---AVGVAGLITPWNAPFML-----ETwkiAPALATGNTVILK--PAEwsPLTANRM 206
Cdd:cd07129 80 LDA-RIDPADPDRQplprpdLRRmlvPLGPVAVFGASNFPLAFsvaggDT---ASALAAGCPVVVKahPAH--PGTSELV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 207 AEIIDQA----GLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMrngADALKR-----FSMELGGKSPII 277
Cdd:cd07129 154 ARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALF---DAAAARpepipFYAELGSVNPVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 278 VFEDADLERALDAATWGIFSF---NGERCTANSRLYLHESIA-DEFIEKLKQRVwniRVGDPLennTQIGPLIkTEHYNN 353
Cdd:cd07129 231 ILPGALAERGEAIAQGFVGSLtlgAGQFCTNPGLVLVPAGPAgDAFIAALAEAL---AAAPAQ---TMLTPGI-AEAYRQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 354 VKKylKIAEEEGCEIISGviPKELNRGNYVAPTILL-NASNEMR--VVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLA 430
Cdd:cd07129 304 GVE--ALAAAPGVRVLAG--GAAAEGGNQAAPTLFKvDAAAFLAdpALQEEVFGPASLVVRYDDAAELLAVAEALEGQLT 379
|
....*..
gi 22778556 431 GYVWTND 437
Cdd:cd07129 380 ATIHGEE 386
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
162-487 |
9.97e-25 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 107.48 E-value: 9.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 162 GVAGLITPWNAPfmleTW----KIAPALATGNTVILKPAEWSPLTANRMAEIIDQAG-LPDGVFNIVHGfgeTAGDAL-- 234
Cdd:PRK11903 150 GVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG---SSAGLLdh 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 235 VKHPDVqlISFTGETTTGSTIMRNGADALK--RFSMELGGKSPIIVFEDAdlerALDAATWGIFSFN---------GERC 303
Cdd:PRK11903 223 LQPFDV--VSFTGSAETAAVLRSHPAVVQRsvRVNVEADSLNSALLGPDA----APGSEAFDLFVKEvvremtvksGQKC 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 304 TANSRLYLHESIADEFIEKLKQRVWNIRVGDPLENNTQIGPLIKTEHYNNVKKYLKiAEEEGCEIISG-----VIPKELN 378
Cdd:PRK11903 297 TAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDgggfaLVDADPA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 379 RGNYVAPTILL--NASNEMRVVQEEIFGPVIAVMTFNDETEVIEKANDVRYGLAGYVWTNDMKRGHRVAHAI-DS-GMLW 454
Cdd:PRK11903 376 VAACVGPTLLGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELaDShGRVH 455
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 22778556 455 VNSQNVRDLRT------P---FGGSKDSGIGRE-GGHYAFEFY 487
Cdd:PRK11903 456 VISPDVAALHTghgnvmPqslHGGPGRAGGGEElGGLRALAFY 498
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
68-387 |
5.93e-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: 73.41 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 68 QSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLP----ISQTRKQVSRSANNFRFYADTVKsQMYG 143
Cdd:cd07077 1 ESAKNAQRT-LAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYirslIANWIAMMGCSESKLYKNIDTER-GITA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 144 EVYQVDDE-----FINYTVRSAVGVAGLITPWNAPfMLETWKIAPALATGNTVILKPAEWSPLTaNRMAEIIDQAGLPDG 218
Cdd:cd07077 79 SVGHIQDVllpdnGETYVRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFT-NRALALLFQAADAAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 219 -----VFNIVHGFGETAgDALVKHPDVQLISFTGetttGSTIMR------NGADALKrFSmelGGKSPIIVFEDADLERA 287
Cdd:cd07077 157 gpkilVLYVPHPSDELA-EELLSHPKIDLIVATG----GRDAVDaavkhsPHIPVIG-FG---AGNSPVVVDETADEERA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 288 LDAATWGIFsFNGERCTANSRLYLHESIADEFIE--KLKQRVWNIRV-------------GDPLENNTQIGPLI----KT 348
Cdd:cd07077 228 SGSVHDSKF-FDQNACASEQNLYVVDDVLDPLYEefKLKLVVEGLKVpqetkplskettpSFDDEALESMTPLEcqfrVL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 22778556 349 EHYNNVKKYLKIAEEEGCEIISGVIPKELNRGNYVAPTI 387
Cdd:cd07077 307 DVISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYI 345
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
63-326 |
5.53e-13 |
|
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: 70.76 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 63 IDKAVQSAKKAFKGeWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGLPISQTR--KQVSRSANNFRFYADTVKSQ 140
Cdd:cd07081 1 LDDAVAAAKVAQQG-LSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKviKNHFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 141 MYGEvyqvDDEFINYTVRSAVGVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQA----GLP 216
Cdd:cd07081 80 VLTG----DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 217 DGVFNIVHGFGETAGDALVKHPDVQLISFTGetttGSTIMRNGADALKRFSMELGGKSPIIVFEDADLERALDAATWGIF 296
Cdd:cd07081 156 ENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKT 231
|
250 260 270
....*....|....*....|....*....|
gi 22778556 297 SFNGERCTANSRLYLHESIADEFIEKLKQR 326
Cdd:cd07081 232 FDNGVICASEQSVIVVDSVYDEVMRLFEGQ 261
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
162-444 |
4.87e-10 |
|
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: 61.74 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 162 GVAGLITPWNAPFMLETWKIAPALATGNTVILKPAEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETAGdALVKHPDVQ 241
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 242 LISFTGETTTGstimrngadalKRFSMELGGKspiIVFEDADLE--------RALDAATW----GIFSFNGERCTANSRL 309
Cdd:cd07126 223 MTLFTGSSKVA-----------ERLALELHGK---VKLEDAGFDwkilgpdvSDVDYVAWqcdqDAYACSGQKCSAQSIL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 310 YLHESIADE-FIEKLK----QRvwnirvgdPLENNTqIGPLI--KTEHY-NNVKKYLKIaeeEGCEIISGviPKELNRGN 381
Cdd:cd07126 289 FAHENWVQAgILDKLKalaeQR--------KLEDLT-IGPVLtwTTERIlDHVDKLLAI---PGAKVLFG--GKPLTNHS 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22778556 382 YVA------PTILLNASNEMR------VVQEEIFGPVIAVMTFNDETE--VIEKANDVRYGLAGYVWTNDMKRGHRV 444
Cdd:cd07126 355 IPSiygayePTAVFVPLEEIAieenfeLVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
178-311 |
7.18e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 61.34 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 178 TWKIAPA----LATGNTVILKP--AEWSPL--TANRMAEIIDQAGL-PDGVFNIVHGFGETAGDALVKHPDVQLISFTGE 248
Cdd:cd07127 207 TWNGYPGlfasLATGNPVIVKPhpAAILPLaiTVQVAREVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGS 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22778556 249 TTTGSTIMRNGADALkrFSMELGGKSPIIVFEDADLERALDAATWGIFSFNGERCTANSRLYL 311
Cdd:cd07127 287 NAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYV 347
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
61-325 |
3.28e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 55.71 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 61 ADIDKAVQSAKKAFKgEWGNLKQVERLEYVYKIGDLIEQHTDEIAILESLDTGL-----PISQTRKQVSRSANNFRFYAd 135
Cdd:cd07121 4 ATVDDAVAAAKAAQK-QYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMgrvedKIAKNHLAAEKTPGTEDLTT- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 136 TVKSQMYGevyqvddefINYTVRSAVGVAGLITPWNAPfmLETwKIAPA---LATGNTVILKP----AEWSPLTANRMAE 208
Cdd:cd07121 82 TAWSGDNG---------LTLVEYAPFGVIGAITPSTNP--TET-IINNSismLAAGNAVVFNPhpgaKKVSAYAVELINK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 209 IIDQAGLPDGVFNIVHGFGETAGDALVKHPDVQLISFTGETTTGSTIMRNGadalKRFSMELGGKSPIIVFEDADLERAL 288
Cdd:cd07121 150 AIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSG----KKAIGAGAGNPPVVVDETADIEKAA 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 22778556 289 DAATWGIfSF-NGERCTANSRLYLHESIADEFIEKLKQ 325
Cdd:cd07121 226 RDIVQGA-SFdNNLPCIAEKEVIAVDSVADYLIAAMQR 262
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
63-326 |
8.05e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.34 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 63 IDKAVQSAKKAFKgEWGNL--KQVERLeyVYKIGDLIEQHTDEIAILESLDTGLPISQ--TRKQVSRSANNFRFYADtVK 138
Cdd:cd07122 1 VDELVERARKAQR-EFATFsqEQVDKI--VEAVAWAAADAAEELAKMAVEETGMGVVEdkVIKNHFASEYVYNDIKD-MK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 139 SqmYGeVYQVDDEFINYTVRSAVGV-AGLITPWN----APFmletwKIAPALATGNTVILKPAEWSPLTANRMAEIIDQA 213
Cdd:cd07122 77 T--VG-VIEEDEEKGIVEIAEPVGViAALIPSTNptstAIF-----KALIALKTRNAIIFSPHPRAKKCSIEAAKIMREA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 214 ----GLPDGVFNIVHGFGETAGDALVKHPDVQLIsftgeTTTGSTIMRNGAdalkrFSM---ELG---GKSPIIVFEDAD 283
Cdd:cd07122 149 avaaGAPEGLIQWIEEPSIELTQELMKHPDVDLI-----LATGGPGMVKAA-----YSSgkpAIGvgpGNVPAYIDETAD 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22778556 284 LERAldaATWGIFS--F-NGERCTANSRLYLHESIADEFIEKLKQR 326
Cdd:cd07122 219 IKRA---VKDIILSktFdNGTICASEQSVIVDDEIYDEVRAELKRR 261
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
158-325 |
1.17e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 51.06 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 158 RSAVGVAGLITPWNAPfmLETWkIAPA---LATGNTVILKP----AEWSPLTANRMAEIIDQAGLPDGVFNIVHGFGETA 230
Cdd:PRK15398 127 YAPFGVIGAVTPSTNP--TETI-INNAismLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIET 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22778556 231 GDALVKHPDVQLISFTGETTTGSTIMRNGadalKRFSMELGGKSPIIVFEDADLERALDAATWGIfSF-NGERCTANSRL 309
Cdd:PRK15398 204 AQRLMKHPGIALLVVTGGPAVVKAAMKSG----KKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFdNNLPCIAEKEV 278
|
170
....*....|....*.
gi 22778556 310 YLHESIADEFIEKLKQ 325
Cdd:PRK15398 279 IVVDSVADELMRLMEK 294
|
|
| |
