|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
24-455 |
0e+00 |
|
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: 764.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 24 IDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEEFLQP 103
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 104 EQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVH 183
Cdd:cd07100 81 EPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 184 IDLDEVDRLtgfmIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQ 263
Cdd:cd07100 161 IDSDQVEAI----IADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 264 SCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWY 343
Cdd:cd07100 237 SCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 344 YPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSD 423
Cdd:cd07100 317 YPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSD 396
|
410 420 430
....*....|....*....|....*....|..
gi 499235697 424 PRLPFGGVKQSGYGRELSHHGIREFVNIKTFY 455
Cdd:cd07100 397 PRLPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-453 |
0e+00 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 535.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEFLQPEQSE---IDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNV 158
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLADEPADaaaVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 159 TGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfmIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPY 238
Cdd:PRK09406 163 PQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAI----LRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 239 IVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHS 318
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 319 QVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQD 398
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 399 VERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:PRK09406 399 EAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKT 453
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
3-455 |
0e+00 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 526.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 3 VTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAE 82
Cdd:PRK13968 10 ISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 83 VNKCAWVCDYFADHAEEFLQPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCA 162
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 163 IAIEKLFRDAGFPEHLYRAVHIDLDEVDRltgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLE 242
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQ----MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 243 DADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQR 322
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 323 SVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERA 402
Cdd:PRK13968 326 TLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 499235697 403 LGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFY 455
Cdd:PRK13968 406 RQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-453 |
5.25e-167 |
|
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: 478.85 E-value: 5.25e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:COG1012 23 FDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEFL-QPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTG 160
Cdd:COG1012 103 EVDRAADFLRYYAGEARRLYgETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIV 240
Cdd:COG1012 183 SALLLAELLEEAGLPAGVLNVVTGDGSEVGAA---LVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 241 LEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQV 320
Cdd:COG1012 260 LDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 321 QRSVEAGAELLWGGHVPN-APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDV 399
Cdd:COG1012 340 EDAVAEGAELLTGGRRPDgEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDL 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 400 ERALGIARRLEAGSCFINT-MVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:COG1012 420 ARARRVARRLEAGMVWINDgTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
2-453 |
4.91e-165 |
|
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: 472.79 E-value: 4.91e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:pfam00171 9 IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEfLQPEQSEIDGAKGIVAF-EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTG 160
Cdd:pfam00171 89 EVDRAIDVLRYYAGLARR-LDGETLPSDPGRLAYTRrEPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVHidldEVDRLTG-FMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYI 239
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVT----GSGAEVGeALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 240 VLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQ 319
Cdd:pfam00171 244 VLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 320 VQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDV 399
Cdd:pfam00171 324 VEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDL 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 400 ERALGIARRLEAGSCFINTMVKSDPR-LPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:pfam00171 404 ERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
5-453 |
1.05e-157 |
|
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: 453.81 E-value: 1.05e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVN 84
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCDYFADHAEEFL-QPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAI 163
Cdd:cd07103 82 YAASFLEWFAEEARRIYgRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 164 AIEKLFRDAGFPEHLYRAVHIDLDEVdrlTGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLED 243
Cdd:cd07103 162 ALAELAEEAGLPAGVLNVVTGSPAEI---GEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 244 ADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRS 323
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 324 VEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERAL 403
Cdd:cd07103 319 VAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 499235697 404 GIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07103 399 RVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKY 448
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
25-453 |
1.47e-148 |
|
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: 430.09 E-value: 1.47e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 25 DSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEEFLQPE 104
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 105 -QSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVH 183
Cdd:cd07078 81 iPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 184 IDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQ 263
Cdd:cd07078 161 GDGDEVGAA---LASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 264 SCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVP-NAPGW 342
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 343 YYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKS 422
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|..
gi 499235697 423 -DPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07078 398 aEPSAPFGGVKQSGIGREGGPYGLEEYTEPKT 429
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
5-456 |
8.78e-128 |
|
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: 377.74 E-value: 8.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVN 84
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCDYFADHAEEFLQP-EQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAI 163
Cdd:cd07102 81 GMLERARYMISIAEEALADiRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 164 AIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfmIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLED 243
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAAL----IADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 244 ADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRS 323
Cdd:cd07102 237 ADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 324 VEAGAELLWGGH---VPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVE 400
Cdd:cd07102 317 IAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 499235697 401 RALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
5-456 |
1.24e-127 |
|
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: 377.25 E-value: 1.24e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVN 84
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCDYFADHAeefLQPE-QSEIDGAKGIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVKHAPNVT 159
Cdd:cd07106 82 GAVAWLRYTASLD---LPDEvIEDDDTRRVELRRKPLGVVAAIVPWNFPLllaaWKI----APALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 160 GCAIAIEKLFRDAgFPEHLYRAVHiDLDEV-DRLTgfmiDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPY 238
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVS-GGDELgPALT----SHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 239 IVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHS 318
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 319 QVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQD 398
Cdd:cd07106 309 LVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 499235697 399 VERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07106 389 LERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
24-448 |
5.24e-125 |
|
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: 369.94 E-value: 5.24e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 24 IDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAwvcDYFADHAEEFLQP 103
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAI---AILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 104 E----QSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPN--VTGcAIAIEKLFRDAGFPEH 177
Cdd:cd07104 79 EgeilPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRtpVTG-GLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 178 LYRAVHIDLDEV-DRltgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAG 256
Cdd:cd07104 158 VLNVVPGGGSEIgDA----LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 257 RLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHv 336
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 337 pnAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFI 416
Cdd:cd07104 313 --YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430
....*....|....*....|....*....|...
gi 499235697 417 NTM-VKSDPRLPFGGVKQSGYGRELSHHGIREF 448
Cdd:cd07104 391 NDQtVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
2-453 |
9.62e-124 |
|
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: 367.83 E-value: 9.62e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEFL--QPEQSEIDGAKGIVAF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAP 156
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRgeTIPVDAYEYNERRIAFtvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 157 NVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEV-DRLtgfmIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGS 235
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEI----VTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 236 DPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDL 315
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 316 VHSQVQRSVEAGAELLWGGHVPnaPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVF 395
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 396 SQDVERALGIARRLEAGSCFIN--TMVKSDpRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINdsTRFRWD-NLPFGGFKKSGIGREGVRYTMLEMTEEKT 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
4-456 |
3.80e-123 |
|
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: 366.11 E-value: 3.80e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRR--WRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFA---DHAEEFLQPeqSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK---HA 155
Cdd:cd07114 81 QVRYLAEWYRYYAglaDKIEGAVIP--VDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKpseHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 156 PNVTgcaIAIEKLFRDAGFPEHLYRAVhidldevdrlTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRS 228
Cdd:cd07114 159 PAST---LELAKLAEEAGFPPGVVNVV----------TGFgpetgeaLVEHPLVAKIAFTGGTETGRHIARAAAENLAPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 229 VLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIA 308
Cdd:cd07114 226 TLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 309 REDLRDLVHSQVQRSVEAGAELLWGGHVPNAP----GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIAN 384
Cdd:cd07114 306 TERQLEKVERYVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALAN 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499235697 385 DSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07114 386 DSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
2-456 |
1.34e-121 |
|
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: 362.74 E-value: 1.34e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:cd07088 15 IDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAE----EFLQpeqSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPN 157
Cdd:cd07088 95 EVEFTADYIDYMAEWARriegEIIP---SDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 158 VTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDP 237
Cdd:cd07088 172 TPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDA---LVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 238 YIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVH 317
Cdd:cd07088 249 AIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 318 SQVQRSVEAGAELLWGGHVPN-APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFS 396
Cdd:cd07088 329 EMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYT 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499235697 397 QDVERALGIARRLEAGSCFINtmvksdpRLPF-------GGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07088 409 ENLNTAMRATNELEFGETYIN-------RENFeamqgfhAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
5-456 |
1.92e-117 |
|
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: 351.88 E-value: 1.92e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRR--WRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV-A 81
Cdd:cd07139 19 VSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRrA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEFLQPE-QSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTG 160
Cdd:cd07139 99 QGPGPAALLRYYAALARDFPFEErRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLTGfmidHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIV 240
Cdd:cd07139 179 DAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVR----HPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 241 LEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQV 320
Cdd:cd07139 255 LDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 321 QRSVEAGAELLWGGHVPNAP--GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQD 398
Cdd:cd07139 335 AKGRAEGARLVTGGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTAD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 499235697 399 VERALGIARRLEAGSCFINTMVkSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07139 415 VERGLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
5-449 |
8.73e-117 |
|
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: 349.60 E-value: 8.73e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVN 84
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCDYFADHAEEFLQPEQ----SEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTG 160
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKvptgLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVHIDLDevdrlTGF-MIDHPVIKaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYI 239
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGA-----TGAaLIDAGVDK-VAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 240 VLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQ 319
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 320 VQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDV 399
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 499235697 400 ERALGIARRLEAGSCFIN--TMVKSDPRLPFGGVKQSGYGRELSHHGIREFV 449
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFC 446
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
23-453 |
2.18e-116 |
|
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: 348.03 E-value: 2.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 23 QIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGkpFSQAVAEVNkCAWVCDYFADHAEEFLQ 102
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG--ATAAWAGFN-VDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 103 PE----QSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEHL 178
Cdd:cd07105 78 IIggsiPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 179 YRAVHIDLDEVDRLTGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRL 258
Cdd:cd07105 158 LNVVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 259 LNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQtAVMGDPFAKSTEVGPIAREDLRDLVHSqvqrSVEAGAELLWGGHVP- 337
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAE-KLFAGPVVLGSLVSAAAADRVKELVDD----ALSKGAKLVVGGLADe 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 338 NAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFIN 417
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430
....*....|....*....|....*....|....*..
gi 499235697 418 TM-VKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07105 393 GMtVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKW 429
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
5-456 |
5.30e-116 |
|
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: 347.79 E-value: 5.30e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFR--RWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAE 82
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDkgPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 83 VNKCAWVCDYFAD-----HAEEFlqpeQSEIDGAKGIVAFEPLGVILGVMPWNFPYW---QVLRFAapiLMAGNGIVVKH 154
Cdd:cd07118 82 IEGAADLWRYAASlartlHGDSY----NNLGDDMLGLVLREPIGVVGIITPWNFPFLilsQKLPFA---LAAGCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 155 APNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGG 234
Cdd:cd07118 155 SEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQA---MTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 235 SDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRD 314
Cdd:cd07118 232 KNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 315 LVHSQVQRSVEAGAELLWGG-HVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSA 393
Cdd:cd07118 312 KITDYVDAGRAEGATLLLGGeRLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 394 VFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07118 392 VWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-452 |
6.84e-115 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 346.29 E-value: 6.84e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVN 84
Cdd:PLN02278 45 YNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCDYFADHAEE---FLQPeqSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGC 161
Cdd:PLN02278 125 YGASFLEYFAEEAKRvygDIIP--SPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 162 AIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVL 241
Cdd:PLN02278 203 ALAAAELALQAGIPPGVLNVVMGDAPEIGDA---LLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 242 EDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQ 321
Cdd:PLN02278 280 DDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 322 RSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVER 401
Cdd:PLN02278 360 DAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQR 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 499235697 402 ALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:PLN02278 440 AWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
6-452 |
7.11e-115 |
|
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: 344.70 E-value: 7.11e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 6 NPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNK 85
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 86 CAwvcDYFADHAEEFLQPE----QSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK--HAPNVT 159
Cdd:cd07150 85 TP---ELLRAAAGECRRVRgetlPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKpsEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 160 GCAIAieKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYI 239
Cdd:cd07150 162 GLKIA--EIMEEAGLPKGVFNVVTGGGAEVGDE---LVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 240 VLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQ 319
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 320 VQRSVEAGAELLWGGHVpnaPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDV 399
Cdd:cd07150 317 VEDAVAKGAKLLTGGKY---DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 499235697 400 ERALGIARRLEAGSCFIN-TMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:cd07150 394 QRAFKLAERLESGMVHINdPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
5-453 |
2.31e-114 |
|
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: 344.10 E-value: 2.31e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQA-VAEV 83
Cdd:cd07138 19 INPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLArAAQV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFADHAEEFlqPEQSEIDGAkgIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK---HAPnvtG 160
Cdd:cd07138 99 GLGIGHLRAAADALKDF--EFEERRGNS--LVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKpseVAP---L 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIV 240
Cdd:cd07138 172 SAIILAEILDEAGLPAGVFNLVNGDGPVVGEA---LSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 241 LEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQV 320
Cdd:cd07138 249 LDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 321 QRSVEAGAELLWGGhvPNAP-----GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVF 395
Cdd:cd07138 329 QKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVW 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 499235697 396 SQDVERALGIARRLEAGSCFINtMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07138 407 SADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKS 463
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
31-453 |
1.97e-112 |
|
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: 335.35 E-value: 1.97e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 31 ADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEEFLQPEQSEID- 109
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 110 GAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEV 189
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 190 -DRLTgfmiDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAA 268
Cdd:cd06534 163 gAALL----SHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 269 KRFIVRKEIIGEFTKKIVqrmqtavmgdpfakstevgpiaredlrdlvhsqvqrsveagaellwgghvpnapgwyyppTV 348
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 349 LSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINT-MVKSDPRLP 427
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDsSIGVGPEAP 338
|
410 420
....*....|....*....|....*.
gi 499235697 428 FGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKT 364
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
2-438 |
6.33e-112 |
|
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: 337.74 E-value: 6.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNkcawVCDYFADHAEEFLQPEQ-----SEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAP 156
Cdd:cd07151 92 EWG----AAMAITREAATFPLRMEgrilpSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 157 N--VTGCAIaIEKLFRDAGFPEHLYRAVHIDLDEV-DRltgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELG 233
Cdd:cd07151 168 DtpITGGLL-LAKIFEEAGLPKGVLNVVVGAGSEIgDA----FVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 234 GSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLR 313
Cdd:cd07151 243 GNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 314 DLVHSQVQRSVEAGAELLWGGHVpnaPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSA 393
Cdd:cd07151 323 DGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 499235697 394 VFSQDVERALGIARRLEAGSCFINTM-VKSDPRLPFGGVKQSGYGR 438
Cdd:cd07151 400 VFTSDLERGVQFARRIDAGMTHINDQpVNDEPHVPFGGEKNSGLGR 445
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
4-453 |
1.27e-111 |
|
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: 336.88 E-value: 1.27e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADF--RRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:cd07112 6 TINPATGRVLAEVAACDAADVDRAVAAARRAFesGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 -EVNKCAWVCDYFAdhaeEFLQPEQSEI----DGAKGIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVV 152
Cdd:cd07112 86 vDVPSAANTFRWYA----EAIDKVYGEVaptgPDALALITREPLGVVGAVVPWNFPLlmaaWKI----APALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 153 KHAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLTGFmidHPVIKAVSVTGSTGAGQAVAAKAGKA-LKRSVLE 231
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGL---HMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 232 LGGSDPYIVLEDA-DLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIARE 310
Cdd:cd07112 235 CGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 311 DLRDLVHSQVQRSVEAGAELLWGG--HVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEF 388
Cdd:cd07112 315 AHFDKVLGYIESGKAEGARLVAGGkrVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 389 GLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07112 395 GLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKT 459
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
4-455 |
3.15e-111 |
|
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: 335.81 E-value: 3.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEV 83
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFADHAEEfLQPEQSEIDGakGIVAF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTG 160
Cdd:cd07090 81 DSSADCLEYYAGLAPT-LSGEHVPLPG--GSFAYtrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVHIDLDevdrlTG-FMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYI 239
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGE-----TGqLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 240 VLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQ 319
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 320 VQRSVEAGAELLWGG-----HVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAV 394
Cdd:cd07090 313 IESAKQEGAKVLCGGervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499235697 395 FSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFY 455
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
4-453 |
6.87e-111 |
|
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: 334.53 E-value: 6.87e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA-E 82
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 83 VNKCAWVCDYFADHA----EEFLQPEqseiDGAKGIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVKH 154
Cdd:cd07093 81 IPRAAANFRFFADYIlqldGESYPQD----GGALNYVLRQPVGVAGLITPWNLPLmlltWKI----APALAFGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 155 APNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEV-DRLTGfmidHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELG 233
Cdd:cd07093 153 SEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAgAALVA----HPDVDLISFTGETATGRTIMRAAAPNLKPVSLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 234 GSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLR 313
Cdd:cd07093 229 GKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 314 DLVHSQVQRSVEAGAELLWGGHVPNAP----GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFG 389
Cdd:cd07093 309 EKVLGYVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499235697 390 LGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07093 389 LAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKN 452
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
5-456 |
1.79e-110 |
|
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: 334.22 E-value: 1.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPA-TGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEV 83
Cdd:cd07097 19 RNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFAdhAEEFLQPEQSEIDGAKGIVAF---EPLGVILGVMPWNFPY----WQvlrfAAPILMAGNGIVVKHAP 156
Cdd:cd07097 99 TRAGQIFRYYA--GEALRLSGETLPSTRPGVEVEttrEPLGVVGLITPWNFPIaipaWK----IAPALAYGNTVVFKPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 157 NVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEV-DRLtgfmIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGS 235
Cdd:cd07097 173 LTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQAL----VEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 236 DPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDL 315
Cdd:cd07097 249 NPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 316 VHSQVQRSVEAGAELLWGGH-VPNA-PGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSA 393
Cdd:cd07097 329 DLRYIEIARSEGAKLVYGGErLKRPdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 394 VFSQDVERALGIARRLEAGSCFIN-TMVKSDPRLPFGGVKQSGYG-RELSHHGIREFVNIKTFYL 456
Cdd:cd07097 409 IVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
5-454 |
2.12e-110 |
|
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: 333.44 E-value: 2.12e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRW-RSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPfsQAVAEV 83
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAP--VMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCD---YFADHAEEFLQPEQSEID-----GAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHA 155
Cdd:cd07089 80 MQVDGPIGhlrYFADLADSFPWEFDLPVPalrggPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 156 PNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEV-DRLTgfmiDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGG 234
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALT----TDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 235 SDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRD 314
Cdd:cd07089 236 KSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 315 LVHSQVQRSVEAGAELLWGGHVPN--APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGS 392
Cdd:cd07089 316 RVEGYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499235697 393 AVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTF 454
Cdd:cd07089 396 GVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
6-456 |
1.35e-109 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 331.25 E-value: 1.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 6 NPATGEQLAEYPVMIAGQIDSVLRQADAdfRRWRSTSFgERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNK 85
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALAAS--YRSTLTRY-QRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 86 cawVCDYFADHAEEFLQPEQSEID--------GAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPN 157
Cdd:cd07146 82 ---AADVLRFAAAEALRDDGESFScdltangkARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 158 VTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEV-DRltgfMIDHPVIKAVSVTGSTGAGQAVAAKAGkaLKRSVLELGGSD 236
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIgDE----LITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 237 PYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLV 316
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 317 HSQVQRSVEAGAELLWGGHVPNApgwYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFS 396
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQRQGA---LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499235697 397 QDVERALGIARRLEAGSCFINTMVKSD-PRLPFGGVKQSGYG-RELSHHGIREFVNIKTFYL 456
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFRsELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
5-452 |
2.24e-107 |
|
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: 325.44 E-value: 2.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA-EV 83
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFADHAEEFLQPEQSE-IDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCA 162
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAGEyLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 163 IAIEKLFRDaGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLE 242
Cdd:cd07092 162 LLLAELAAE-VLPPGVVNVVCGGGASAGDA---LVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 243 DADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQR 322
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 323 sVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERA 402
Cdd:cd07092 318 -APAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 499235697 403 LGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:cd07092 397 MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
4-453 |
5.97e-107 |
|
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: 325.32 E-value: 5.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEypVMIAGQ--IDSVLRQADADFR--RWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQ- 78
Cdd:cd07091 23 TINPATEEVICQ--VAEADEedVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEEs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 79 AVAEVNKCAWVCDYFADHAEEfLQPEQSEIDGAK-GIVAFEPLGVILGVMPWNFPywqVLRFA---APILMAGNGIVVKH 154
Cdd:cd07091 101 AKGDVALSIKCLRYYAGWADK-IQGKTIPIDGNFlAYTRREPIGVCGQIIPWNFP---LLMLAwklAPALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 155 APNVTGCAIAIEKLFRDAGFPEHLyravhidldeVDRLTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKA-LK 226
Cdd:cd07091 177 AEQTPLSALYLAELIKEAGFPPGV----------VNIVPGFgptagaaISSHMDVDKIAFTGSTAVGRTIMEAAAKSnLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 227 RSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGP 306
Cdd:cd07091 247 KVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 307 IAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDS 386
Cdd:cd07091 327 QVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDT 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499235697 387 EFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07091 407 EYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKA 473
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
2-453 |
9.23e-107 |
|
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: 324.16 E-value: 9.23e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEfLQPEQSEID---GAKGIVAF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHA 155
Cdd:cd07149 81 EVDRAIETLRLSAEEAKR-LAGETIPFDaspGGEGRIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 156 PNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGkaLKRSVLELGGS 235
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDA---LVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 236 DPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDL 315
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 316 VHSQVQRSVEAGAELLWGGHVPNApgwYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVF 395
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499235697 396 SQDVERALGIARRLEAGSCFINTMvkSDPR---LPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMINDS--STFRvdhMPYGGVKESGTGREGPRYAIEEMTEIKL 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
6-452 |
4.82e-106 |
|
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: 322.71 E-value: 4.82e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 6 NPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKP-----FSQAV 80
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmvdasLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVcdyfADHAEEFLQPEQ---SEIDGAKGI-VAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAP 156
Cdd:cd07098 82 VTCEKIRWT----LKHGEKALRPESrpgGLLMFYKRArVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 157 NVTGCAI----AIEKLFRDAGFPEHLyravhidldeVDRLTGF------MIDHPVIKAVSVTGSTGAGQAVAAKAGKALK 226
Cdd:cd07098 158 QVAWSSGfflsIIRECLAACGHDPDL----------VQLVTCLpetaeaLTSHPVIDHITFIGSPPVGKKVMAAAAESLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 227 RSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGP 306
Cdd:cd07098 228 PVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 307 IAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAP----GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAI 382
Cdd:cd07098 308 MISPARFDRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 383 ANDSEFGLGSAVFSQDVERALGIARRLEAGSCFIN-----TMVKSdprLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:cd07098 388 ANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvnYYVQQ---LPFGGVKGSGFGRFAGEEGLRGLCNPK 459
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
5-452 |
2.80e-105 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 321.09 E-value: 2.80e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA-EV 83
Cdd:PRK13473 22 YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNdEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFAD---HAEEFLQPEQSEidGAKGIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVKHAP 156
Cdd:PRK13473 102 PAIVDVFRFFAGaarCLEGKAAGEYLE--GHTSMIRRDPVGVVASIAPWNYPLmmaaWKL----APALAAGNTVVLKPSE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 157 NVTGCAIAIEKLFRDAgFPEHLYRAVHIDLDEV-DRLTGfmidHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGS 235
Cdd:PRK13473 176 ITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVG----HPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 236 DPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDL 315
Cdd:PRK13473 251 APVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 316 VHSQVQRSVEAG-AELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAV 394
Cdd:PRK13473 331 VAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSV 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 395 FSQDVERALGIARRLEAGSCFINT--MVKSDprLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:PRK13473 411 WTRDVGRAHRVSARLQYGCTWVNThfMLVSE--MPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
2-453 |
7.22e-105 |
|
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: 319.38 E-value: 7.22e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHA-----EEFLQPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAP 156
Cdd:cd07094 81 EVDRAIDTLRLAAEEAerirgEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 157 NVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKalKRSVLELGGSD 236
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDA---FAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 237 PYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLV 316
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 317 HSQVQRSVEAGAELLWGGHVPNApgwYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFS 396
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGERDGA---LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 499235697 397 QDVERALGIARRLEAGSCFIN--TMVKSDpRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNdsSAFRTD-WMPFGGVKESGVGREGVPYAMEEMTEEKT 450
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
4-456 |
1.48e-104 |
|
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: 318.61 E-value: 1.48e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV-AE 82
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 83 VNKCAWVCDYFADHAEEFlqpEQSEI---DGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVT 159
Cdd:cd07115 81 VPRAADTFRYYAGWADKI---EGEVIpvrGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 160 GCAIAIEKLFRDAGFPEHLyravhidldeVDRLTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLEL 232
Cdd:cd07115 158 LSALRIAELMAEAGFPAGV----------LNVVTGFgevagaaLVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 233 GGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDL 312
Cdd:cd07115 228 GGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 313 RDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGS 392
Cdd:cd07115 308 FDRVLDYVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499235697 393 AVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07115 388 GVWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
2-452 |
3.73e-103 |
|
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: 315.89 E-value: 3.73e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFR-RWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQ-A 79
Cdd:cd07144 25 IKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 80 VAEVNKCAWVCDYFADHAEEFlQPEQSEIDGAK-GIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVKH 154
Cdd:cd07144 105 LGDLDEIIAVIRYYAGWADKI-QGKTIPTSPNKlAYTLHEPYGVCGQIIPWNYPLamaaWKL----APALAAGNTVVIKP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 155 APNVTGCAIAIEKLFRDAGFPEHLyravhidldeVDRLTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKALKR 227
Cdd:cd07144 180 AENTPLSLLYFANLVKEAGFPPGV----------VNIIPGYgavagsaLAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 228 SVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRM-QTAVMGDPFAKSTEVGP 306
Cdd:cd07144 250 VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 307 IAREDLRDLVHSQVQRSVEAGAELLWGGHV---PNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIA 383
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGAKLVYGGEKapeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKA 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499235697 384 NDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:cd07144 410 NDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
5-456 |
5.44e-101 |
|
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: 310.05 E-value: 5.44e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQL-AEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEV 83
Cdd:cd07131 19 RNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFADHAEE-FLQPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCA 162
Cdd:cd07131 99 QEAIDMAQYAAGEGRRlFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 163 IAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLE 242
Cdd:cd07131 179 LKLVELFAEAGLPPGVVNVVHGRGEEVGEA---LVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 243 DADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQR 322
Cdd:cd07131 256 DADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 323 SVEAGAELLWGGHVPN----APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQD 398
Cdd:cd07131 336 GKEEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTED 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 399 VERALGIARRLEAGSCFIN-TMVKSDPRLPFGGVKQSGYG-RELSHHGIREFVNIKTFYL 456
Cdd:cd07131 416 VNKAFRARRDLEAGITYVNaPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
4-456 |
6.86e-100 |
|
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: 307.32 E-value: 6.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPvmiAGQIDSVLRQADA-----DFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQ 78
Cdd:cd07119 17 IINPANGEVIATVP---EGTAEDAKRAIAAarrafDSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 79 AVAEVNKCAWVCDYFADHAEEFLQPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNV 158
Cdd:cd07119 94 SEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 159 TGCAIAIEKLFRDAGFPEHLYRAVHIDLDEV-DRLTGfmidHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDP 237
Cdd:cd07119 174 PLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAE----SPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 238 YIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVH 317
Cdd:cd07119 250 NIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 318 SQVQRSVEAGAELLWGGHVPNAP----GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSA 393
Cdd:cd07119 330 SYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGA 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 394 VFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07119 410 VWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
1-454 |
2.62e-99 |
|
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: 305.65 E-value: 2.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 1 MIVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRT-CMKRLAELLREQAEKHGRIITLEMGKPFSQA 79
Cdd:cd07082 17 TIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIdCLHKFADLLKENKEEVANLLMWEIGKTLKDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 80 VAEVNKCAwvcDYFADHAEEF--LQPEQSEID---GAKGIVAF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIV 151
Cdd:cd07082 97 LKEVDRTI---DYIRDTIEELkrLDGDSLPGDwfpGTKGKIAQvrrEPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 152 VKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVdrlTGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKalKRSVLE 231
Cdd:cd07082 174 FKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREI---GDPLVTHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 232 LGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIARED 311
Cdd:cd07082 249 LGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 312 LRDLVHSQVQRSVEAGAELLWGGH--VPNapgwYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFG 389
Cdd:cd07082 329 SADFVEGLIDDAVAKGATVLNGGGreGGN----LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYG 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499235697 390 LGSAVFSQDVERALGIARRLEAGSCFINTMVKSDP-RLPFGGVKQSGYGRELSHHGIREFVNIKTF 454
Cdd:cd07082 405 LQASIFTKDINKARKLADALEVGTVNINSKCQRGPdHFPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
5-453 |
3.11e-99 |
|
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: 304.93 E-value: 3.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFR-RWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEV 83
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFADHAEEFlqpEQSEIDGAKGIVAF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTG 160
Cdd:cd07109 82 EAAARYFEYYGGAADKL---HGETIPLGPGYFVYtvrEPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVhidldevdrlTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELG 233
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVV----------TGLgaeagaaLVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 234 GSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMG----DPfakstEVGPIAR 309
Cdd:cd07109 229 GKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpgleDP-----DLGPLIS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 310 EDLRDLVHSQVQRSVEAGAELLWGGHVPNAP---GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDS 386
Cdd:cd07109 304 AKQLDRVEGFVARARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGT 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499235697 387 EFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDP-RLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07109 384 DYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKT 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
4-455 |
6.80e-99 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 304.88 E-value: 6.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQA-VAE 82
Cdd:PRK13252 26 VINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETsVVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 83 VNKCAWVCDYFADHAEEfLQPEQSEIDGAkgivAF-----EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPN 157
Cdd:PRK13252 106 IVTGADVLEYYAGLAPA-LEGEQIPLRGG----SFvytrrEPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 158 VTGCAIAIEKLFRDAGFPEHLYRAVhidldEVDRLTGFMI-DHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSD 236
Cdd:PRK13252 181 TPLTALKLAEIYTEAGLPDGVFNVV-----QGDGRVGAWLtEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 237 PYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLV 316
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 317 HSQVQRSVEAGAELLWGGHVPN----APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGS 392
Cdd:PRK13252 336 LGYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 393 AVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFY 455
Cdd:PRK13252 416 GVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
4-452 |
3.40e-98 |
|
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: 302.35 E-value: 3.40e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEV 83
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFADHAEeflQPEQS-------EIDGAKGIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVV 152
Cdd:cd07110 81 DDVAGCFEYYADLAE---QLDAKaeravplPSEDFKARVRREPVGVVGLITPWNFPLlmaaWKV----APALAAGCTVVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 153 KHAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDR-LTGfmidHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLE 231
Cdd:cd07110 154 KPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAA----HPGIDKISFTGSTATGSQVMQAAAQDIKPVSLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 232 LGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIARED 311
Cdd:cd07110 230 LGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 312 LRDLVHSQVQRSVEAGAELLWGGHVPNAP--GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFG 389
Cdd:cd07110 310 QYEKVLSFIARGKEEGARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 390 LGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:cd07110 390 LAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
10-437 |
1.08e-96 |
|
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: 297.67 E-value: 1.08e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 10 GEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWV 89
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 90 CDyfadHAEEFLQPEQSEI----DGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPN--VTGcAI 163
Cdd:cd07152 81 LH----EAAGLPTQPQGEIlpsaPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRtpVSG-GV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 164 AIEKLFRDAGFPEHLYRAVHIDLDEVDRLTgfmiDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLED 243
Cdd:cd07152 156 VIARLFEEAGLPAGVLHVLPGGADAGEALV----EDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 244 ADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRS 323
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 324 VEAGAELLWGGHvpnAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERAL 403
Cdd:cd07152 312 VAAGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
410 420 430
....*....|....*....|....*....|....*
gi 499235697 404 GIARRLEAGSCFIN-TMVKSDPRLPFGGVKQSGYG 437
Cdd:cd07152 389 ALADRLRTGMLHINdQTVNDEPHNPFGGMGASGNG 423
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
5-453 |
2.20e-96 |
|
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: 297.30 E-value: 2.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVN 84
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCDYFADHAEEFLQPE--QSEIDG-AKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGC 161
Cdd:cd07101 81 DVAIVARYYARRAERLLKPRrrRGAIPVlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 162 AIAIEKLFRDAGFPEHLYRAVhidLDEVDRLTGFMIDHpvIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVL 241
Cdd:cd07101 161 ALWAVELLIEAGLPRDLWQVV---TGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 242 EDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQ 321
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 322 RSVEAGAELLWGGH-VPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVE 400
Cdd:cd07101 316 DAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 499235697 401 RALGIARRLEAGSCFIN-----TMVKSDPrlPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07101 396 RGRRIAARLRAGTVNVNegyaaAWASIDA--PMGGMKDSGLGRRHGAEGLLKYTETQT 451
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
4-453 |
2.96e-95 |
|
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: 295.41 E-value: 2.96e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRR---WRSTSFGERRTCMKRLAELLreqaEKHGRII----TLEMGKPF 76
Cdd:cd07141 26 TINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLI----ERDRAYLasleTLDNGKPF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 77 S-QAVAEVNKCAWVCDYFADHAEEfLQPEQSEIDGAkgIVAF---EPLGVILGVMPWNFPY----WQVlrfaAPILMAGN 148
Cdd:cd07141 102 SkSYLVDLPGAIKVLRYYAGWADK-IHGKTIPMDGD--FFTYtrhEPVGVCGQIIPWNFPLlmaaWKL----APALACGN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 149 GIVVKHAPNVTGCAIAIEKLFRDAGFPEHLyravhidldeVDRLTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKA 221
Cdd:cd07141 175 TVVLKPAEQTPLTALYLASLIKEAGFPPGV----------VNVVPGYgptagaaISSHPDIDKVAFTGSTEVGKLIQQAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 222 GKA-LKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAK 300
Cdd:cd07141 245 GKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 301 STEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAV 380
Cdd:cd07141 325 KTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 381 AIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
4-453 |
3.47e-94 |
|
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: 291.97 E-value: 3.47e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEV 83
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFADHAEEFlqpEQSEIDGAKGIVAF---EPLGVILGVMPWNFPY-WQVLRFAAPiLMAGNGIVVKHAPNVT 159
Cdd:cd07107 81 MVAAALLDYFAGLVTEL---KGETIPVGGRNLHYtlrEPYGVVARIVAFNHPLmFAAAKIAAP-LAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 160 GCAIAIEKLFRDAgFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYI 239
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAA---LVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 240 VLEDADLAQAVDACVAGrlLN---AGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLV 316
Cdd:cd07107 233 VFPDADPEAAADAAVAG--MNftwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 317 HSQVQRSVEAGAELLWGGHVPNAP----GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGS 392
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499235697 393 AVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKN 451
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
4-453 |
1.13e-93 |
|
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: 290.42 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPF-SQAVAE 82
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 83 VNKCAWVCDYFADHAeeflqpeqSEIDG-----AKGIVAF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKH 154
Cdd:cd07108 81 AAVLADLFRYFGGLA--------GELKGetlpfGPDVLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 155 APNVTGCAIAIEKLFRdagfpEHLYRAVhidldeVDRLTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKALKR 227
Cdd:cd07108 153 AEDAPLAVLLLAEILA-----QVLPAGV------LNVITGYgeecgaaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 228 SVLELGGSDPYIVLEDADLAQAVDACVAG-RLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGP 306
Cdd:cd07108 222 VSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 307 IAREDLRDLVHSQVQRSVEA-GAELLWGGHVP----NAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVA 381
Cdd:cd07108 302 IISEKQFAKVCGYIDLGLSTsGATVLRGGPLPgegpLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 382 IANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIRE-FVNIKT 453
Cdd:cd07108 382 MANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEhFTQKKT 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
1-439 |
2.34e-93 |
|
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: 290.23 E-value: 2.34e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 1 MIVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV 80
Cdd:cd07086 14 TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDYFAD-----HAEEFlqpeQSEIDGAKGIVAFEPLGVILGVMPWNFPY----WQvlrfAAPILMAGNGIV 151
Cdd:cd07086 94 GEVQEMIDICDYAVGlsrmlYGLTI----PSERPGHRLMEQWNPLGVVGVITAFNFPVavpgWN----AAIALVCGNTVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 152 VKHAPNVTGCAIAIEKLFRDA----GFPEHLYRAVHIDlDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKR 227
Cdd:cd07086 166 WKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGG-GDGGEL---LVHDPRVPLVSFTGSTEVGRRVGETVARRFGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 228 SVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPI 307
Cdd:cd07086 242 VLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 308 AREDLRDLVHSQVQRSVEAGAELLWGGHVP--NAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIAND 385
Cdd:cd07086 322 INQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINND 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 386 SEFGLGSAVFSQDV---ERALGiARRLEAGSCFINTmvksdP------RLPFGGVKQSGYGRE 439
Cdd:cd07086 402 VPQGLSSSIFTEDLreaFRWLG-PKGSDCGIVNVNI-----PtsgaeiGGAFGGEKETGGGRE 458
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
5-452 |
2.60e-91 |
|
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: 284.14 E-value: 2.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVN 84
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCDYFADHAEEF---LQP----EQSEidGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPN 157
Cdd:cd07147 84 RAIDTFRIAAEEATRIygeVLPldisARGE--GRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 158 VTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLTgfmiDHPVIKAVSVTGSTGAGQAVAAKAGKalKRSVLELGGSDP 237
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLV----TDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 238 YIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVH 317
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 318 SQVQRSVEAGAELLWGGHVPNApgwYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQ 397
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGKRDGA---LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 499235697 398 DVERALGIARRLEAGSCFINTM--VKSDPrLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:cd07147 393 DLEKALRAWDELEVGGVVINDVptFRVDH-MPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
6-453 |
2.77e-90 |
|
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: 282.48 E-value: 2.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 6 NPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNK 85
Cdd:cd07085 22 NPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 86 CAWVCDyFADHAEEFLQPEQSEiDGAKGIVAF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCA 162
Cdd:cd07085 102 GLEVVE-FACSIPHLLKGEYLE-NVARGIDTYsyrQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 163 IAIEKLFRDAGFPEHLYRAVHIDLDEVDrltgFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRsVLELGGS-DPYIVL 241
Cdd:cd07085 180 MRLAELLQEAGLPDGVLNVVHGGKEAVN----ALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR-VQALGGAkNHAVVM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 242 EDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQ 321
Cdd:cd07085 255 PDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 322 RSVEAGAELLWGGHVPNAPGW----YYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQ 397
Cdd:cd07085 335 SGVEEGAKLVLDGRGVKVPGYengnFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTR 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 398 DVERALGIARRLEAGSCFINTMVKSdPR--LPFGGVKQSGYGrelSHH-----GIREFVNIKT 453
Cdd:cd07085 415 SGAAARKFQREVDAGMVGINVPIPV-PLafFSFGGWKGSFFG---DLHfygkdGVRFYTQTKT 473
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
50-456 |
4.58e-89 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 277.00 E-value: 4.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 50 MKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEEFlQPE--QSEIDGAKGIVAFEPLGVILGVM 127
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRY-EGEiiQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 128 PWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEV-DRLTGfmidHPVIKAVS 206
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAG----NPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 207 VTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIV 286
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 287 QRMQTAVMGDPFAKST-EVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFG 365
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 366 PVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINtmvksdpRLPF-------GGVKQSGYGR 438
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN-------RENFeamqgfhAGWRKSGIGG 388
|
410
....*....|....*...
gi 499235697 439 ELSHHGIREFVNIKTFYL 456
Cdd:PRK10090 389 ADGKHGLHEYLQTQVVYL 406
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
2-452 |
3.38e-88 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 277.17 E-value: 3.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:PRK11241 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEFL-------QPEQseidgaKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKH 154
Cdd:PRK11241 108 EISYAASFIEWFAEEGKRIYgdtipghQADK------RLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 155 APNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDrltGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGG 234
Cdd:PRK11241 182 ASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVG---GELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 235 SDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRD 314
Cdd:PRK11241 259 NAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 315 LVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAV 394
Cdd:PRK11241 339 KVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 499235697 395 FSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:PRK11241 419 YARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
5-453 |
4.66e-88 |
|
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: 276.72 E-value: 4.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRR-W-RSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA- 81
Cdd:cd07143 27 YNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEfLQPEQSEIDGAK-GIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVKHAP 156
Cdd:cd07143 107 DVQASADTFRYYGGWADK-IHGQVIETDIKKlTYTRHEPIGVCGQIIPWNFPLlmcaWKI----APALAAGNTIVLKPSE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 157 NVTGCAIAIEKLFRDAGFPEHLYRAVHIDldevDRLTGFMI-DHPVIKAVSVTGSTGAGQAVAAKAGKA-LKRSVLELGG 234
Cdd:cd07143 182 LTPLSALYMTKLIPEAGFPPGVINVVSGY----GRTCGNAIsSHMDIDKVAFTGSTLVGRKVMEAAAKSnLKKVTLELGG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 235 SDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRD 314
Cdd:cd07143 258 KSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 315 LVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAV 394
Cdd:cd07143 338 RIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAV 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 499235697 395 FSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07143 418 FTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKA 476
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-453 |
1.98e-87 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 276.37 E-value: 1.98e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEFLQPE--QSEIDGA-KGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNV 158
Cdd:PRK09407 114 EVLDVALTARYYARRAPKLLAPRrrAGALPVLtKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 159 TGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDrltGFMIDHpvIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPY 238
Cdd:PRK09407 194 PLTALAAVELLYEAGLPRDLWQVVTGPGPVVG---TALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 239 IVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHS 318
Cdd:PRK09407 269 IVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 319 QVQRSVEAGAELLWGGHV-PNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQ 397
Cdd:PRK09407 349 HVDDAVAKGATVLAGGKArPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTG 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 398 DVERALGIARRLEAGSCFIN-------TMVKSdprlPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:PRK09407 429 DTARGRAIAARIRAGTVNVNegyaaawGSVDA----PMGGMKDSGLGRRHGAEGLLKYTESQT 487
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
1-456 |
4.94e-87 |
|
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: 273.95 E-value: 4.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 1 MIVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV 80
Cdd:cd07117 17 TIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AevnkcawvCD--YFADHAEEFLQPEQSEIDGAK-------GIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAG 147
Cdd:cd07117 97 A--------VDipLAADHFRYFAGVIRAEEGSANmidedtlSIVLREPIGVVGQIIPWNFPFlmaaWKL----APALAAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 148 NGIVVKHAPNVTGCAIAIEKLFRDAgfpehLYRAVhidldeVDRLTG-------FMIDHPVIKAVSVTGSTGAGQAVAAK 220
Cdd:cd07117 165 NTVVIKPSSTTSLSLLELAKIIQDV-----LPKGV------VNIVTGkgsksgeYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 221 AGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAK 300
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 301 STEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGH--VPN--APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADD 376
Cdd:cd07117 314 DTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHrlTENglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 377 DEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRElSHHGIRE-FVNIKTFY 455
Cdd:cd07117 394 DEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRE-THKSMLDaYTQMKNIY 472
|
.
gi 499235697 456 L 456
Cdd:cd07117 473 I 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
4-456 |
9.39e-87 |
|
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: 273.22 E-value: 9.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRR--WRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQA-V 80
Cdd:cd07142 23 TIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDYFADHAEEfLQPEQSEIDGA-KGIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVKHA 155
Cdd:cd07142 103 AEVPLAARLFRYYAGWADK-IHGMTLPADGPhHVYTLHEPIGVVGQIIPWNFPLlmfaWKV----GPALACGNTIVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 156 PNVTGCAIAIEKLFRDAGFPEHLYRAVhidldevdrlTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKA-LKR 227
Cdd:cd07142 178 EQTPLSALLAAKLAAEAGLPDGVLNIV----------TGFgptagaaIASHMDVDKVAFTGSTEVGKIIMQLAAKSnLKP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 228 SVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPI 307
Cdd:cd07142 248 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 308 AREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSE 387
Cdd:cd07142 328 VDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSK 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499235697 388 FGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07142 408 YGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
1-445 |
4.30e-86 |
|
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: 271.52 E-value: 4.30e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 1 MIVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV 80
Cdd:cd07559 17 YFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 -AEVNKCAWVCDYFAD--HAEEflqPEQSEIDGAK-GIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVV 152
Cdd:cd07559 97 aADIPLAIDHFRYFAGviRAQE---GSLSEIDEDTlSYHFHEPLGVVGQIIPWNFPLlmaaWKL----APALAAGNTVVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 153 KHAPNVTGCAIAIEKLFRDAgfpehLYRAVhidldeVDRLTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKAL 225
Cdd:cd07559 170 KPASQTPLSILVLMELIGDL-----LPKGV------VNVVTGFgseagkpLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 226 KRSVLELGGSDPYIVLEDA-----DLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAK 300
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 301 STEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGH----VPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADD 376
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499235697 377 DEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRElSHHGI 445
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRE-THKMM 466
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
5-453 |
6.59e-86 |
|
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: 271.24 E-value: 6.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFR-RWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKP--FSQAVa 81
Cdd:cd07113 20 TNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSihLSRAF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAE----EFLQPEQSEIDGAKgIVAF---EPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGI 150
Cdd:cd07113 99 EVGQSANFLRYFAGWATkingETLAPSIPSMQGER-YTAFtrrEPVGVVAGIVPWNFSVmiavWKI----GAALATGCTI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 151 VVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDevdrLTGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVL 230
Cdd:cd07113 174 VIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA----VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 231 ELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIARE 310
Cdd:cd07113 250 ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 311 DLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGL 390
Cdd:cd07113 330 PHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGL 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499235697 391 GSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07113 410 TASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKS 472
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
4-456 |
9.13e-85 |
|
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: 267.67 E-value: 9.13e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPvmiAGQIDSVLRQADADFRRWRSTSFGE----RRTCMKRLAELLREQAEKHGRIITLEMGKPFSQA 79
Cdd:cd07120 1 SIDPATGEVIGTYA---DGGVAEAEAAIAAARRAFDETDWAHdprlRARVLLELADAFEANAERLARLLALENGKILGEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 80 VAEVNKCAWVCDYFADHAE----EFLQPEQseidGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHA 155
Cdd:cd07120 78 RFEISGAISELRYYAGLARteagRMIEPEP----GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 156 PNVTGCAIAIEKLFRDA-GFPEHlyrAVHIDLDEVDRLTGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGG 234
Cdd:cd07120 154 GQTAQINAAIIRILAEIpSLPAG---VVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 235 SDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRD 314
Cdd:cd07120 231 KTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 315 LVHSQVQRSVEAGAE-LLWGGHVPN--APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLG 391
Cdd:cd07120 311 RVDRMVERAIAAGAEvVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 392 SAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:cd07120 391 ASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
4-453 |
1.49e-84 |
|
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: 267.82 E-value: 1.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRR--WRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV- 80
Cdd:cd07140 25 TINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDYFADHAEEfLQPEQSEIDGAK-----GIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHA 155
Cdd:cd07140 105 THVGMSIQTFRYFAGWCDK-IQGKTIPINQARpnrnlTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 156 PNVTGCAIAIEKLFRDAGFPEHLyraVHIdLDEVDRLTGFMI-DHPVIKAVSVTGSTGAGQAVAAKAGKA-LKRSVLELG 233
Cdd:cd07140 184 QVTPLTALKFAELTVKAGFPKGV---INI-LPGSGSLVGQRLsDHPDVRKLGFTGSTPIGKHIMKSCAVSnLKKVSLELG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 234 GSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLR 313
Cdd:cd07140 260 GKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 314 DLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDD-EAV-AIANDSEFGLG 391
Cdd:cd07140 340 DKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvDGVlQRANDTEYGLA 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499235697 392 SAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07140 420 SGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKT 481
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
2-452 |
5.89e-82 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 261.59 E-value: 5.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRR-----WRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPF 76
Cdd:PLN02467 25 IPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 77 SQAVAEVNKCAWVCDYFADHAEEfLQPEQSE-----IDGAKGIVAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAG 147
Cdd:PLN02467 105 DEAAWDMDDVAGCFEYYADLAEA-LDAKQKApvslpMETFKGYVLKEPLGVVGLITPWNYPLlmatWKV----APALAAG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 148 NGIVVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVhidldevdrlTGFMID-------HPVIKAVSVTGSTGAGQAVAAK 220
Cdd:PLN02467 180 CTAVLKPSELASVTCLELADICREVGLPPGVLNVV----------TGLGTEagaplasHPGVDKIAFTGSTATGRKIMTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 221 AGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAK 300
Cdd:PLN02467 250 AAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 301 STEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVPN--APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDE 378
Cdd:PLN02467 330 GCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDE 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499235697 379 AVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTmvkSDP---RLPFGGVKQSGYGRELSHHGIREFVNIK 452
Cdd:PLN02467 410 AIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINC---SQPcfcQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-437 |
4.51e-80 |
|
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: 257.15 E-value: 4.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPA-TGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV 80
Cdd:cd07124 48 IESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDYFADHAEEFLQPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTG 160
Cdd:cd07124 128 ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRltgFMIDHPVIKAVSVTGSTGAGQAVAAKAGK------ALKRSVLELGG 234
Cdd:cd07124 208 IAAKLVEILEEAGLPPGVVNFLPGPGEEVGD---YLVEHPDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 235 SDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRD 314
Cdd:cd07124 285 KNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARD 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 315 lvhsQVQRSVEAGAE---LLWGGHVPN--APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFG 389
Cdd:cd07124 365 ----RIRRYIEIGKSegrLLLGGEVLElaAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYG 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 499235697 390 LGSAVFSQD---VERALgiaRRLEAGSCFIN-----TMVKsdpRLPFGGVKQSGYG 437
Cdd:cd07124 441 LTGGVFSRSpehLERAR---REFEVGNLYANrkitgALVG---RQPFGGFKMSGTG 490
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
4-456 |
2.45e-77 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 249.43 E-value: 2.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRR--WRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:PRK09847 39 TVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 E-VNKCAWVCDYFADHAEEFLQPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTG 160
Cdd:PRK09847 119 DdIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 CAIAIEKLFRDAGFPEHLYRAVhidldevdrlTGFMID-------HPVIKAVSVTGSTGAGQAVAAKAGKA-LKRSVLEL 232
Cdd:PRK09847 199 SAIRLAGLAKEAGLPDGVLNVV----------TGFGHEagqalsrHNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWLEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 233 GGSDPYIVLEDA-DLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIARED 311
Cdd:PRK09847 269 GGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 312 LRDLVHSQVQRSvEAGAELLWGGHVPNAPGwYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLG 391
Cdd:PRK09847 349 HADSVHSFIREG-ESKGQLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLG 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 392 SAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYL 456
Cdd:PRK09847 427 AAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
4-449 |
5.98e-75 |
|
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: 242.69 E-value: 5.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLreqaEKHGRII----TLEMGKPfsqa 79
Cdd:cd07111 41 TINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHI----QKHQRLFavleSLDNGKP---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 80 VAEVNKC--AWVCDYFADHAeefLQPEQSEIDGAkgivAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVK 153
Cdd:cd07111 113 IRESRDCdiPLVARHFYHHA---GWAQLLDTELA----GWKPVGVVGQIVPWNFPLlmlaWKI----CPALAMGNTVVLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 154 HAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfmIDHPVIKAVSVTGSTGAGQAVA-AKAGKAlKRSVLEL 232
Cdd:cd07111 182 PAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSAL----ANHPGVDKVAFTGSTEVGRALRrATAGTG-KKLSLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 233 GGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDL 312
Cdd:cd07111 257 GGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 313 RDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGS 392
Cdd:cd07111 337 LKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAA 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 499235697 393 AVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFV 449
Cdd:cd07111 417 SVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
4-457 |
2.40e-74 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 242.79 E-value: 2.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFRR--WRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV- 80
Cdd:PLN02466 77 TLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAk 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDYFADHAEEfLQPEQSEIDGAKGI-VAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVKHA 155
Cdd:PLN02466 157 AELPMFARLFRYYAGWADK-IHGLTVPADGPHHVqTLHEPIGVAGQIIPWNFPLlmfaWKV----GPALACGNTIVLKTA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 156 PNVTGCAIAIEKLFRDAGFPEHLYRAVhidldevdrlTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKA-LKR 227
Cdd:PLN02466 232 EQTPLSALYAAKLLHEAGLPPGVLNVV----------SGFgptagaaLASHMDVDKLAFTGSTDTGKIVLELAAKSnLKP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 228 SVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPI 307
Cdd:PLN02466 302 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 308 AREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSE 387
Cdd:PLN02466 382 IDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTR 461
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 388 FGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYLP 457
Cdd:PLN02466 462 YGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTP 531
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
4-457 |
1.22e-73 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 240.11 E-value: 1.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 4 TINPATGEQLAEYPVMIAGQIDSVLRQADADFR--RWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQA-V 80
Cdd:PLN02766 40 TRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGkA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDYFADHAEEfLQPEQSEIDGA-KGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVT 159
Cdd:PLN02766 120 VDIPAAAGLLRYYAGAADK-IHGETLKMSRQlQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 160 GCAIAIEKLFRDAGFPEHLYRAVhidldevdrlTGF-------MIDHPVIKAVSVTGSTGAGQAVAAKAGKA-LKRSVLE 231
Cdd:PLN02766 199 LSALFYAHLAKLAGVPDGVINVV----------TGFgptagaaIASHMDVDKVSFTGSTEVGRKIMQAAATSnLKQVSLE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 232 LGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIARED 311
Cdd:PLN02766 269 LGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 312 LRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLG 391
Cdd:PLN02766 349 QFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLA 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499235697 392 SAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRELSHHGIREFVNIKTFYLP 457
Cdd:PLN02766 429 AGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
6-453 |
6.06e-64 |
|
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: 213.97 E-value: 6.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 6 NPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNK 85
Cdd:TIGR01722 22 NPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 86 CAWVCDYfADHAEEFLQPEQSEiDGAKGIVAF---EPLGVILGVMPWNFPYWQVLrFAAPILMA-GNGIVVKHAPNVTGC 161
Cdd:TIGR01722 102 GLEVVEH-ACGVNSLLKGETST-QVATRVDVYsirQPLGVCAGITPFNFPAMIPL-WMFPIAIAcGNTFVLKPSEKVPSA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 162 AIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfmIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVL 241
Cdd:TIGR01722 179 AVKLAELFSEAGAPDGVLNVVHGDKEAVDRL----LEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 242 EDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEiIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQ 321
Cdd:TIGR01722 255 PDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 322 RSVEAGAELLWGGHVPNAPGW----YYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQ 397
Cdd:TIGR01722 334 GGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTR 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499235697 398 DVERALGIARRLEAGSCFINTMVKSD-PRLPFGGVKQSGYGrelSHH-----GIREFVNIKT 453
Cdd:TIGR01722 414 DGAAARRFQHEIEVGQVGVNVPIPVPlPYFSFTGWKDSFFG---DHHiygkqGTHFYTRGKT 472
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
25-453 |
3.80e-63 |
|
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: 210.46 E-value: 3.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 25 DSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQA-VAEVNKCAWVCDYFADHAEEFLQP 103
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAyLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 104 EQSEID----GAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK---HAPNvtgCAIAIEKLFRDAgFPE 176
Cdd:cd07087 81 RRVSVPlllqPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKpseLAPA---TSALLAKLIPKY-FDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 177 HLYRAVHIDLDEVDRLT--GFmiDHpvikaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACV 254
Cdd:cd07087 157 EAVAVVEGGVEVATALLaePF--DH-----IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 255 AGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMqTAVMGDPFAKSTEVGPIAREDlrdlvhsQVQRSVE--AGAELLW 332
Cdd:cd07087 230 WGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAI-KEFYGEDPKESPDYGRIINER-------HFDRLASllDDGKVVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 333 GGHVpNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAG 412
Cdd:cd07087 302 GGQV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSG 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 499235697 413 SCFIN-TMVK-SDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07087 381 GVCVNdVLLHaAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKS 423
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-435 |
9.58e-63 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 211.72 E-value: 9.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPA-TGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV 80
Cdd:PRK03137 52 IVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDYFADHAEEFLQ--PEQSeIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNV 158
Cdd:PRK03137 132 ADTAEAIDFLEYYARQMLKLADgkPVES-RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 159 TGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDrltGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKA------LKRSVLEL 232
Cdd:PRK03137 211 PVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVG---DYLVDHPKTRFITFTGSREVGLRIYERAAKVqpgqiwLKRVIAEM 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 233 GGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPfAKSTEVGPIAREDL 312
Cdd:PRK03137 288 GGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQAS 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 313 RDLVHSQVQRSVEAGaELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGS 392
Cdd:PRK03137 367 FDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTG 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 499235697 393 AVFSQDVERaLGIARRL-EAGSCFIN-----TMVKSDprlPFGGVKQSG 435
Cdd:PRK03137 446 AVISNNREH-LEKARREfHVGNLYFNrgctgAIVGYH---PFGGFNMSG 490
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-437 |
1.92e-62 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 210.90 E-value: 1.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQ-LAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEV 83
Cdd:cd07125 51 IDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 84 NKCAWVCDYFADHAEE-FLQPEQSEIDGAKGIVAFEPLGVILGVMPWNFPY----WQVlrFAApiLMAGNGIVVKHAPNV 158
Cdd:cd07125 131 REAIDFCRYYAAQARElFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLaiftGQI--AAA--LAAGNTVIAKPAEQT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 159 TGCAIAIEKLFRDAGFPEhlyRAVHIDLDEVDRLTGFMIDHPVIKAVSVTGSTGAGQAVA-AKAGKALKRSVL--ELGGS 235
Cdd:cd07125 207 PLIAARAVELLHEAGVPR---DVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINrALAERDGPILPLiaETGGK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 236 DPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDL 315
Cdd:cd07125 284 NAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 316 VHSQVQRSvEAGAELLWGGHVPNAPGWYYPPTVLSGVkpGMPAYSEEIFGPVATII--EVADDDEAVAIANDSEFGLGSA 393
Cdd:cd07125 364 LRAHTELM-RGEAWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLG 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 499235697 394 VFSQDVERALGIARRLEAGSCFINTM-----VKsdpRLPFGGVKQSGYG 437
Cdd:cd07125 441 IHSRDEREIEYWRERVEAGNLYINRNitgaiVG---RQPFGGWGLSGTG 486
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
1-439 |
2.21e-62 |
|
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: 209.76 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 1 MIVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV 80
Cdd:cd07130 13 VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDY------------FAdhaeeflqpeqSEIDGAKGIVAFEPLGVILGVMPWNFPY----WQvlrfAAPIL 144
Cdd:cd07130 93 GEVQEMIDICDFavglsrqlygltIP-----------SERPGHRMMEQWNPLGVVGVITAFNFPVavwgWN----AAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 145 MAGNGIVVKHAPNVTGCAIAIEKLFRDA----GFPEHLYRAVHIDLDEVDRltgfMIDHPVIKAVSVTGSTGAGQAVAAK 220
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADVGEA----LVKDPRVPLVSFTGSTAVGRQVGQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 221 AGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAK 300
Cdd:cd07130 234 VAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 301 STEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSGvKPGMPAYSEEIFGPVATIIEVADDDEAV 380
Cdd:cd07130 314 GTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 381 AIANDSEFGLGSAVFSQD---VERALGiarrlEAGS-CFI---NTmvksdprlP---------FGGVKQSGYGRE 439
Cdd:cd07130 393 AWNNEVPQGLSSSIFTTDlrnAFRWLG-----PKGSdCGIvnvNI--------GtsgaeiggaFGGEKETGGGRE 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
23-438 |
8.41e-60 |
|
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: 201.73 E-value: 8.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 23 QIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEEFLQ 102
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 103 PEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAV 182
Cdd:cd07095 81 ERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 183 HIDLDEVDRLtgfmIDHPVIKAVSVTGSTGAGQAVAAK-AGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNA 261
Cdd:cd07095 161 QGGRETGEAL----AAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 262 GQSCIAAKRFIVRKEIIG-EFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAP 340
Cdd:cd07095 237 GQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 341 GWYYPPTVLSGVKPGMPAySEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFS---QDVERALgiaRRLEAGSCFIN 417
Cdd:cd07095 317 TAFLSPGIIDVTDAADVP-DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSddeALFERFL---ARIRAGIVNWN 392
|
410 420
....*....|....*....|..
gi 499235697 418 -TMVKSDPRLPFGGVKQSGYGR 438
Cdd:cd07095 393 rPTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
37-448 |
3.61e-59 |
|
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: 200.15 E-value: 3.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 37 RWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQA-VAEVNKCAWVCDYFADHAEEFLQPEQSE----IDGA 111
Cdd:cd07134 13 ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVdLTEILPVLSEINHAIKHLKKWMKPKRVRtpllLFGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 112 KGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK---HAPNVTGCaiaIEKLFRDAgFPEHLYRAVHIDLDE 188
Cdd:cd07134 93 KSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKpseLTPHTSAV---IAKIIREA-FDEDEVAVFEGDAEV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 189 VDRLTGFMIDHpvikaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAA 268
Cdd:cd07134 169 AQALLELPFDH-----IFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 269 KRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTE-----VGPIAREDLRDLVHsqvqRSVEAGAELLWGGhVPNAPGWY 343
Cdd:cd07134 244 DYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPdlariVNDRHFDRLKGLLD----DAVAKGAKVEFGG-QFDAAQRY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 344 YPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVK-- 421
Cdd:cd07134 319 IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhf 398
|
410 420
....*....|....*....|....*..
gi 499235697 422 SDPRLPFGGVKQSGYGRELSHHGIREF 448
Cdd:cd07134 399 LNPNLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
5-443 |
3.00e-58 |
|
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: 198.83 E-value: 3.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEvn 84
Cdd:cd07116 21 ITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCD---YFAD--HAEEflqPEQSEIDGAKGIVAF-EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNV 158
Cdd:cd07116 99 DIPLAIDhfrYFAGciRAQE---GSISEIDENTVAYHFhEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 159 TGCAIAIEKLFRDAgFPEHLYRAVHIDLDEVDRltgFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPY 238
Cdd:cd07116 176 PASILVLMELIGDL-LPPGVVNVVNGFGLEAGK---PLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 239 IVLEDADLAQA--VDACVAGRL---LNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLR 313
Cdd:cd07116 252 IFFADVMDADDafFDKALEGFVmfaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 314 DLVHSQVQRSVEAGAELLWGG---HVPNAPGWYY--PPTVLSGVKpgMPAYSEEIFGPVATIIEVADDDEAVAIANDSEF 388
Cdd:cd07116 332 EKILSYIDIGKEEGAEVLTGGernELGGLLGGGYyvPTTFKGGNK--MRIFQEEIFGPVLAVTTFKDEEEALEIANDTLY 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 389 GLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRLPFGGVKQSGYGRE-----LSHH 443
Cdd:cd07116 410 GLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGREnhkmmLDHY 469
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
2-437 |
6.63e-56 |
|
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: 191.86 E-value: 6.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFR---RWRSTSfgERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQ 78
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNWLPAH--ERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 79 AVAEVNKcawVCDYFADHAEEFLQPEQSEI-----DGAKGIVAF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGI 150
Cdd:cd07148 79 AKVEVTR---AIDGVELAADELGQLGGREIpmgltPASAGRIAFttrEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 151 VVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRltgfMIDHPVIKAVSVTGSTGAGQAVAAKAGKAlKRSVL 230
Cdd:cd07148 156 IVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEK----LVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 231 ELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIARE 310
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 311 DLRDLVHSQVQRSVEAGAELLWGGHVPNAPgwYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGL 390
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 499235697 391 GSAVFSQDVERALGIARRLEAGSCFIN--TMVKSDpRLPFGGVKQSGYG 437
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMVNdhTAFRVD-WMPFAGRRQSGYG 436
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
5-453 |
7.49e-53 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 184.96 E-value: 7.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 5 INPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVN 84
Cdd:PLN00412 36 TNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 85 KCAWVCDYFAD------------HAEEFLQPEQSEIDGAKGIvafePLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVV 152
Cdd:PLN00412 116 RSGDLISYTAEegvrilgegkflVSDSFPGNERNKYCLTSKI----PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 153 KhaPNVTGCAIAIEKL--FRDAGFPEHLYRAVHIDLDEVDrltGFMIDHPVIKAVSVTGSTgAGQAVAAKAGK-ALKrsv 229
Cdd:PLN00412 192 K--PPTQGAVAALHMVhcFHLAGFPKGLISCVTGKGSEIG---DFLTMHPGVNCISFTGGD-TGIAISKKAGMvPLQ--- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 230 LELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPfAKSTEVGPIAR 309
Cdd:PLN00412 263 MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 310 EDLRDLVHSQVQRSVEAGA----------ELLWgghvpnapgwyypPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEA 379
Cdd:PLN00412 342 ESSANFIEGLVMDAKEKGAtfcqewkregNLIW-------------PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499235697 380 VAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDP-RLPFGGVKQSGYGRElshhGIREFVNIKT 453
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQ----GITNSINMMT 479
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
2-453 |
3.31e-52 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 185.34 E-value: 3.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 2 IVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:PLN02419 131 IDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAE----EFLqPEQSeiDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPN 157
Cdd:PLN02419 211 DIFRGLEVVEHACGMATlqmgEYL-PNVS--NGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 158 VTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLTgfmiDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDP 237
Cdd:PLN02419 288 DPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAIC----DDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNH 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 238 YIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIvrkeIIGE---FTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRD 314
Cdd:PLN02419 364 GLVLPDANIDATLNALLAAGFGAAGQRCMALSTVV----FVGDaksWEDKLVERAKALKVTCGSEPDADLGPVISKQAKE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 315 LVHSQVQRSVEAGAELLWGGHVPNAPGW----YYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGL 390
Cdd:PLN02419 440 RICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGN 519
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499235697 391 GSAVFSQDVERALGIARRLEAGSCFINTMVKSD-PRLPFGGVKQSgYGRELSHH---GIREFVNIKT 453
Cdd:PLN02419 520 GAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPlPFFSFTGNKAS-FAGDLNFYgkaGVDFFTQIKL 585
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
24-448 |
2.34e-51 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 181.00 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 24 IDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGK-PFSQAVAEVNKCAWVCDYFADHAEEFLQ 102
Cdd:PTZ00381 9 IPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRhPFETKMTEVLLTVAEIEHLLKHLDEYLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 103 PEQSEIDGA----KGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK---HAPNvtgCAIAIEKLFrDAGFP 175
Cdd:PTZ00381 89 PEKVDTVGVfgpgKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKpseLSPH---TSKLMAKLL-TKYLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 176 EHLYRAVHIDLDEVDRLTGFMIDHpvikaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVA 255
Cdd:PTZ00381 165 PSYVRVIEGGVEVTTELLKEPFDH-----IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 256 GRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMqTAVMGDPFAKSTEVGPIAREdlrdlvhSQVQRSVE----AGAELL 331
Cdd:PTZ00381 240 GKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAI-KEFFGEDPKKSEDYSRIVNE-------FHTKRLAElikdHGGKVV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 332 WGGHVpNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEA 411
Cdd:PTZ00381 312 YGGEV-DIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSS 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 499235697 412 GSCFINTMV--KSDPRLPFGGVKQSGYGrelSHHGIREF 448
Cdd:PTZ00381 391 GAVVINDCVfhLLNPNLPFGGVGNSGMG---AYHGKYGF 426
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
23-453 |
3.12e-51 |
|
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: 178.95 E-value: 3.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 23 QIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV-AEVNKCAWVCDYFADHAEEFL 101
Cdd:cd07135 6 EIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLKKWA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 102 QPEQSEIDGA-----KGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK---HAPNvtgCAIAIEKLFRDAg 173
Cdd:cd07135 86 KDEKVKDGPLafmfgKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKpseLTPH---TAALLAELVPKY- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 174 FPEHLYRAVHIDLDEVDRLTGFMIDHpvikaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDAC 253
Cdd:cd07135 162 LDPDAFQVVQGGVPETTALLEQKFDK-----IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 254 VAGRLLNAGQSCIAAKRFIVRKEIIGEFtkkiVQRMQTAVmgDPFAKStevGPIAREDLRDLVH----SQVQRSVEA-GA 328
Cdd:cd07135 237 LWGKFGNAGQICVAPDYVLVDPSVYDEF----VEELKKVL--DEFYPG---GANASPDYTRIVNprhfNRLKSLLDTtKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 329 ELLWGGhVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARR 408
Cdd:cd07135 308 KVVIGG-EMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTR 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 499235697 409 LEAGSCFIN-TMVK-SDPRLPFGGVKQSGYGRELSHHGIREFVNIKT 453
Cdd:cd07135 387 TRSGGVVINdTLIHvGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
3-453 |
3.60e-51 |
|
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: 180.47 E-value: 3.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 3 VTINP-ATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA 81
Cdd:cd07083 35 VSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 82 EVNKCAWVCDYFADHAEEFL--QPEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVT 159
Cdd:cd07083 115 DVAEAIDFIRYYARAALRLRypAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 160 GCAIAIEKLFRDAGFPEHLYRAVHIDLDEVDrltGFMIDHPVIKAVSVTGSTGAGQAVAAKAGK------ALKRSVLELG 233
Cdd:cd07083 195 VVGYKVFEIFHEAGFPPGVVQFLPGVGEEVG---AYLTEHERIRGINFTGSLETGKKIYEAAARlapgqtWFKRLYVETG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 234 GSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPI--ARED 311
Cdd:cd07083 272 GKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVidAEQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 312 LRDLVHSQVQRSVeagAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDD--EAVAIANDSEFG 389
Cdd:cd07083 352 AKVLSYIEHGKNE---GQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYG 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499235697 390 LGSAVFSQDVERALGIARRLEAGSCFINTmvKSDPRL----PFGGVKQSGYG-RELSHHGIREFVNIKT 453
Cdd:cd07083 429 LTGGVYSRKREHLEEARREFHVGNLYINR--KITGALvgvqPFGGFKLSGTNaKTGGPHYLRRFLEMKA 495
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
25-454 |
3.99e-46 |
|
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: 165.35 E-value: 3.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 25 DSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEkhgRIITlEMGKPFSQ------AVAEVNKCAWVCDYFADHAE 98
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQD---ALAE-AISADFGHrsrhetLLAEILPSIAGIKHARKHLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 99 EFLQPEQSEID----GAKGIVAFEPLGVIlGVM-PWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAg 173
Cdd:cd07133 77 KWMKPSRRHVGllflPAKAEVEYQPLGVV-GIIvPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 174 FPEHLYRAVHIDLDEVDRLTGFMIDHPVIkavsvTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDAC 253
Cdd:cd07133 155 FDEDEVAVVTGGADVAAAFSSLPFDHLLF-----TGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 254 VAGRLLNAGQSCIAAKRFIVRKEIIGEFT---KKIVQRMQTAVMGDPfakstEVGPIAREDLRDLVHSQVQRSVEAGAEL 330
Cdd:cd07133 230 AFGKLLNAGQTCVAPDYVLVPEDKLEEFVaaaKAAVAKMYPTLADNP-----DYTSIINERHYARLQGLLEDARAKGARV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 331 LWGGHVPNAP--GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARR 408
Cdd:cd07133 305 IELNPAGEDFaaTRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRR 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 499235697 409 LEAGSCFIN-TMVK-SDPRLPFGGVKQSGYGRelsHHGIREFvniKTF 454
Cdd:cd07133 385 THSGGVTINdTLLHvAQDDLPFGGVGASGMGA---YHGKEGF---LTF 426
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
1-435 |
9.40e-44 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 160.12 E-value: 9.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 1 MIVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV 80
Cdd:PRK09457 16 AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEV----NKCAWVCDYFADHAEEflqpEQSEIDGAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK--- 153
Cdd:PRK09457 96 TEVtamiNKIAISIQAYHERTGE----KRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKpse 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 154 HAPNVtgcAIAIEKLFRDAGFPEhlyrAVhIDLDEVDRLTGF-MIDHPVIKAVSVTGSTGAG----QAVAAKAGKALkrs 228
Cdd:PRK09457 172 LTPWV---AELTVKLWQQAGLPA----GV-LNLVQGGRETGKaLAAHPDIDGLLFTGSANTGyllhRQFAGQPEKIL--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 229 VLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGE-FTKKIVQRMQTAVMGDPFAKSTE-VGP 306
Cdd:PRK09457 241 ALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDAEPQPfMGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 307 -IAREDLRDLVHSQvQRSVEAGAELLWGGHVPNAPGWYYPPTVL--SGVKpGMPaySEEIFGPVATIIEVADDDEAVAIA 383
Cdd:PRK09457 321 vISEQAAQGLVAAQ-AQLLALGGKSLLEMTQLQAGTGLLTPGIIdvTGVA-ELP--DEEYFGPLLQVVRYDDFDEAIRLA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 499235697 384 NDSEFGLGSAVFSQDVERALGIARRLEAGscFIN-----TMVKSDprLPFGGVKQSG 435
Cdd:PRK09457 397 NNTRFGLSAGLLSDDREDYDQFLLEIRAG--IVNwnkplTGASSA--APFGGVGASG 449
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
110-454 |
4.23e-42 |
|
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: 154.97 E-value: 4.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 110 GAKGIVAFEPLGVILGVMPWNFPYwQvLRFAAPI--LMAGNGIVVK---HAPNVtgcAIAIEKLFRDAgFPEHLYRAVHI 184
Cdd:cd07136 91 PSKSYIYYEPYGVVLIIAPWNYPF-Q-LALAPLIgaIAAGNTAVLKpseLTPNT---SKVIAKIIEET-FDEEYVAVVEG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 185 DLDEVDRLTGFMIDHpvikaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQS 264
Cdd:cd07136 165 GVEENQELLDQKFDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 265 CIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFaKSTEVGPIARED----LRDLVHSQvqrsveagaELLWGGHVpNAP 340
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPL-ESPDYGRIINEKhfdrLAGLLDNG---------KIVFGGNT-DRE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 341 GWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRLEAGSCFIN-TM 419
Cdd:cd07136 309 TLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdTI 388
|
330 340 350
....*....|....*....|....*....|....*.
gi 499235697 420 VK-SDPRLPFGGVKQSGYGrelSHHGIREFvniKTF 454
Cdd:cd07136 389 MHlANPYLPFGGVGNSGMG---SYHGKYSF---DTF 418
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
26-444 |
4.48e-39 |
|
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: 146.60 E-value: 4.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 26 SVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKP-FSQAVAEVNKCAWVCDYFADHAEEFLQPE 104
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPkFEAVLSEILLVKNEIKYAISNLPEWMKPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 105 QseidGAKGIV-----AF---EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFrdagfPE 176
Cdd:cd07132 82 P----VKKNLAtllddVYiykEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-----PK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 177 HL----YRAVHIDLDEVDRLTGFMIDHpvikaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDA 252
Cdd:cd07132 153 YLdkecYPVVLGGVEETTELLKQRFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 253 CVAGRLLNAGQSCIAAKRFIVRKEIigefTKKIVQRMQTAV---MGDPFAKSTEVGPIAREdlrdlvhSQVQRSVeagaE 329
Cdd:cd07132 228 IAWGKFINAGQTCIAPDYVLCTPEV----QEKFVEALKKTLkefYGEDPKESPDYGRIIND-------RHFQRLK----K 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 330 LLWGGHVP-----NAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFS---QDVER 401
Cdd:cd07132 293 LLSGGKVAiggqtDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSnnkKVINK 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 499235697 402 ALgiaRRLEAGSCFIN-TMVKSD-PRLPFGGVKQSGYGRelsHHG 444
Cdd:cd07132 373 IL---SNTSSGGVCVNdTIMHYTlDSLPFGGVGNSGMGA---YHG 411
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
1-439 |
2.11e-36 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 140.35 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 1 MIVTINPATGEQLAEYPVMIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAV 80
Cdd:PLN02315 35 LVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 81 AEVNKCAWVCDYFADHAEEF---LQPeqSEIDGAKGIVAFEPLGVILGVMPWNFPyWQVLRFAAPI-LMAGNGIVVKHAP 156
Cdd:PLN02315 115 GEVQEIIDMCDFAVGLSRQLngsIIP--SERPNHMMMEVWNPLGIVGVITAFNFP-CAVLGWNACIaLVCGNCVVWKGAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 157 NVTGCAIAIEKLFRDA----GFPEHLYRAVhidldevdrLTGFMIDHPV-----IKAVSVTGSTGAG----QAVAAKAGK 223
Cdd:PLN02315 192 TTPLITIAMTKLVAEVleknNLPGAIFTSF---------CGGAEIGEAIakdtrIPLVSFTGSSKVGlmvqQTVNARFGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 224 ALkrsvLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTE 303
Cdd:PLN02315 263 CL----LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 304 VGPIAREDLRDLVHSQVQRSVEAGAELLWGGHVPNAPGWYYPPTVLSgVKPGMPAYSEEIFGPVATIIEVADDDEAVAIA 383
Cdd:PLN02315 339 LGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEIN 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 499235697 384 NDSEFGLGSAVFSQDVERALGIARRLEAGSCFINTMVKSDPRL---PFGGVKQSGYGRE 439
Cdd:PLN02315 418 NSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEiggAFGGEKATGGGRE 476
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
21-437 |
4.21e-34 |
|
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: 133.50 E-value: 4.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 21 AGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEEF 100
Cdd:TIGR01238 73 LAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 101 LQPEQSeidgakgivafEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEHlyr 180
Cdd:TIGR01238 153 LGEFSV-----------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAG--- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 181 AVHIDLDEVDRLTGFMIDHPVIKAVSVTGSTGAGQAVA---AKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGR 257
Cdd:TIGR01238 219 TIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINqtlAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 258 LLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPI----AREDLRDLVH--SQVQRSVeagAELL 331
Cdd:TIGR01238 299 FDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVidaeAKQNLLAHIEhmSQTQKKI---AQLT 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 332 WGGHVPNAPGWYYPPTVLSgvKPGMPAYSEEIFGPVATIIEVADD--DEAVAIANDSEFGLGSAVFSQDVERALGIARRL 409
Cdd:TIGR01238 376 LDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKARelDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHA 453
|
410 420 430
....*....|....*....|....*....|
gi 499235697 410 EAGSCFIN-TMVKSDPRL-PFGGVKQSGYG 437
Cdd:TIGR01238 454 RVGNCYVNrNQVGAVVGVqPFGGQGLSGTG 483
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
10-435 |
4.22e-33 |
|
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: 131.17 E-value: 4.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 10 GEQLAEY----PVMIAGQIDSVLRQADAdfrrWRSTSFGERRTCMKRLAELLreQAEKHGRIITLEM---GKPFSQAvaE 82
Cdd:cd07123 57 AHVLATYhyadAALVEKAIEAALEARKE----WARMPFEDRAAIFLKAADLL--SGKYRYELNAATMlgqGKNVWQA--E 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 83 VNKCAWVCDYF---ADHAEEFL-QPEQSEIDGAKGIVAFEPL-GVILGVMPWNF-------PywqvlrfAAPILMaGNGI 150
Cdd:cd07123 129 IDAACELIDFLrfnVKYAEELYaQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFtaiggnlA-------GAPALM-GNVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 151 VVKHAPNVTGCAIAIEKLFRDAGFPEHLYRAVHIDLDEVdrlTGFMIDHPVIKAVSVTGSTGAGQAVAAKAG------KA 224
Cdd:cd07123 201 LWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV---GDTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryRT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 225 LKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEV 304
Cdd:cd07123 278 YPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 305 GPIAREDLRDLVHSQVQRSVEA-GAELLWGGHVPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDD--EAVA 381
Cdd:cd07123 358 GAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDfeETLE 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499235697 382 IAND-SEFGLGSAVFSQDvERALGIAR---RLEAGSCFINTmvKSD----PRLPFGGVKQSG 435
Cdd:cd07123 438 LVDTtSPYALTGAIFAQD-RKAIREATdalRNAAGNFYIND--KPTgavvGQQPFGGARASG 496
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
27-444 |
8.84e-33 |
|
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: 128.68 E-value: 8.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 27 VLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQA-VAEVNKCAWVCDYFADHAEEFLQPEQ 105
Cdd:cd07137 4 LVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKWMAPEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 106 SEID----GAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFrdagfPEHL--- 178
Cdd:cd07137 84 VKTPlttfPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-----PEYLdtk 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 179 -YRAVHIDLDEVDRLtgfmIDHPVIKaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGR 257
Cdd:cd07137 159 aIKVIEGGVPETTAL----LEQKWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 258 L-LNAGQSCIAAKRFIVRKEiigeFTKKIVQRMQTaVMGDPFAKStevgPIAREDLRDLVHSQ-VQRSV------EAGAE 329
Cdd:cd07137 234 WgCNNGQACIAPDYVLVEES----FAPTLIDALKN-TLEKFFGEN----PKESKDLSRIVNSHhFQRLSrllddpSVADK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 330 LLWGGHVpNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGIARRL 409
Cdd:cd07137 305 IVHGGER-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAET 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 499235697 410 EAGSCFIN-TMVK-SDPRLPFGGVKQSGYGRelsHHG 444
Cdd:cd07137 384 SSGGVTFNdTVVQyAIDTLPFGGVGESGFGA---YHG 417
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
23-437 |
6.65e-32 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 129.55 E-value: 6.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 23 QIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAE-EFL 101
Cdd:PRK11904 586 QVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARrLFG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 102 QPEQSE-IDGAKGIVAFEPLGVILGVMPWNFPywqVLRFAAPI---LMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFPEh 177
Cdd:PRK11904 666 APEKLPgPTGESNELRLHGRGVFVCISPWNFP---LAIFLGQVaaaLAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPK- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 178 lyRAVHIDLDEVDRLTGFMIDHPVIKAVSVTGSTGAGQAV----AAKAGKALkrsVL--ELGGSDPYIVLEDADLAQAVD 251
Cdd:PRK11904 742 --DVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInrtlAARDGPIV---PLiaETGGQNAMIVDSTALPEQVVD 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 252 ACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRsVEAGAELL 331
Cdd:PRK11904 817 DVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLL 895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 332 WGGHVPNAP--GWYYPPTV--LSGVKpgmpAYSEEIFGPVATII--EVADDDEAVAIANDSEFGLGSAVFSQDVERALGI 405
Cdd:PRK11904 896 AQLPLPAGTenGHFVAPTAfeIDSIS----QLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEETADRI 971
|
410 420 430
....*....|....*....|....*....|....*..
gi 499235697 406 ARRLEAGSCFIN-----TMVKSDprlPFGGVKQSGYG 437
Cdd:PRK11904 972 ADRVRVGNVYVNrnqigAVVGVQ---PFGGQGLSGTG 1005
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
21-437 |
6.14e-31 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 126.52 E-value: 6.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 21 AGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEEF 100
Cdd:PRK11905 589 AEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRL 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 101 LQPEQSEidgakgivafePLGVILGVMPWNFPY----WQVLrfAApiLMAGNGIVVKHAPnVTgCAIAIE--KLFRDAGF 174
Cdd:PRK11905 669 LNGPGHK-----------PLGPVVCISPWNFPLaiftGQIA--AA--LVAGNTVLAKPAE-QT-PLIAARavRLLHEAGV 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 175 PEHLYRAVHIDLDEV-DRLTGfmidHPVIKAVSVTGSTGAGQAVAAKAGKALKRSVL---ELGGSDPYIVLEDADLAQAV 250
Cdd:PRK11905 732 PKDALQLLPGDGRTVgAALVA----DPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPEQVV 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 251 DACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPI----AREDLRDlvHSQVQRSVea 326
Cdd:PRK11905 808 ADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVidaeAQANIEA--HIEAMRAA-- 883
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 327 gAELLWGGHVPN--APGWYYPPTVLSgvKPGMPAYSEEIFGPVATIIEV-ADDDEAV--AIaNDSEFGLGSAVFSQDVER 401
Cdd:PRK11905 884 -GRLVHQLPLPAetEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFkADELDRVidDI-NATGYGLTFGLHSRIDET 959
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 499235697 402 ALGIARRLEAGSCFIN-----TMVKSDprlPFGGVKQSGYG 437
Cdd:PRK11905 960 IAHVTSRIRAGNIYVNrniigAVVGVQ---PFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
21-437 |
6.49e-25 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 108.49 E-value: 6.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 21 AGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEE- 99
Cdd:COG4230 592 AADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRl 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 100 FLQPEQseidgakgivaFEPLGVILGVMPWNFPY----WQVLrfAApiLMAGNGIVVKHAPNVTGCAIAIEKLFRDAGFP 175
Cdd:COG4230 672 FAAPTV-----------LRGRGVFVCISPWNFPLaiftGQVA--AA--LAAGNTVLAKPAEQTPLIAARAVRLLHEAGVP 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 176 EHlyrAVHI---DLDEV-DRLTGfmidHPVIKAVSVTGSTGAGQAV----AAKAGKALkrsVL--ELGGSDPYIVLEDAD 245
Cdd:COG4230 737 AD---VLQLlpgDGETVgAALVA----DPRIAGVAFTGSTETARLInrtlAARDGPIV---PLiaETGGQNAMIVDSSAL 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 246 LAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPI----AREDLRDlvHSQVQ 321
Cdd:COG4230 807 PEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVidaeARANLEA--HIERM 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 322 RSVeagAELLWGGHVPNAP--GWYYPPTV--LSGVKpgmpAYSEEIFGPVATIIEV-ADDDEAV--AIaNDSEFGLGSAV 394
Cdd:COG4230 885 RAE---GRLVHQLPLPEECanGTFVAPTLieIDSIS----DLEREVFGPVLHVVRYkADELDKVidAI-NATGYGLTLGV 956
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 499235697 395 FSQDVERALGIARRLEAGSCFIN-----TMVKSDprlPFGGVKQSGYG 437
Cdd:COG4230 957 HSRIDETIDRVAARARVGNVYVNrniigAVVGVQ---PFGGEGLSGTG 1001
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
31-383 |
1.24e-23 |
|
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: 102.70 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 31 ADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVaEVNKCAWVCDYFADHAEEFLQPEQSEIDG 110
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYSYRIPHEPGNHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 111 AKGI---VAFE--PLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAG-FPEHLYRAVHI 184
Cdd:cd07084 87 GQGLkqqSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLING 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 185 DldevDRLTGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKAlkRSVLELGGSDPYIVLEDADLAQAV-DACVAGRLLNAGQ 263
Cdd:cd07084 167 D----GKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVaWQCVQDMTACSGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 264 SCIAAKRFIVRKEIIGE-FTKKIVQRMQTAVMGDpfaksTEVGPIARED-LRDLVH--SQVQRSVEAGAELLWGGHVPNA 339
Cdd:cd07084 241 KCTAQSMLFVPENWSKTpLVEKLKALLARRKLED-----LLLGPVQTFTtLAMIAHmeNLLGSVLLFSGKELKNHSIPSI 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 499235697 340 PGWYYPPTVLSGVKP---GMPAYSEEIFGPVATIIEVADDDEAVAIA 383
Cdd:cd07084 316 YGACVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLALVLE 362
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
19-448 |
2.01e-23 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 102.50 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 19 MIAGQIDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVA-EVNKCAWVCDYFADHA 97
Cdd:PLN02203 3 APGETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRdEVGVLTKSANLALSNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 98 EEFLQPEQSEID----GAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIaieklFRDAG 173
Cdd:PLN02203 83 KKWMAPKKAKLPlvafPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 174 FPEHL-YRAVHIDLDEVDRLTGFMiDHPVIKaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIV---LEDADLAQA 249
Cdd:PLN02203 158 IPKYLdSKAVKVIEGGPAVGEQLL-QHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 250 VDACVAGRLLN-AGQSCIAAKRFIVRKE---IIGEFTKKIVQRMqtavMGDPFAKSTEVGPIARED----LRDLVH-SQV 320
Cdd:PLN02203 236 VNRIVGGKWGScAGQACIAIDYVLVEERfapILIELLKSTIKKF----FGENPRESKSMARILNKKhfqrLSNLLKdPRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 321 QRSVeagaelLWGGHVpNAPGWYYPPTVLsgVKPGMPA--YSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQD 398
Cdd:PLN02203 312 AASI------VHGGSI-DEKKLFIEPTIL--LNPPLDSdiMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNN 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 499235697 399 VERALGIARRLEAGSC-FINTMVK-SDPRLPFGGVKQSGYGRelsHHGIREF 448
Cdd:PLN02203 383 EKLKRRILSETSSGSVtFNDAIIQyACDSLPFGGVGESGFGR---YHGKYSF 431
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
98-448 |
5.46e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 95.11 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 98 EEFLQPEQSEID----GAKGIVAFEPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAG 173
Cdd:PLN02174 87 KNWMAPEKAKTSlttfPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 174 FPEhLYRAVHIDLDEVDRLTGFMIDHpvikaVSVTGSTGAGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDAC 253
Cdd:PLN02174 167 DSS-AVRVVEGAVTETTALLEQKWDK-----IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 254 VAGRL-LNAGQSCIAAKRFIVRKeiigEFTKKIVQRMQTAVmgdpfAKSTEVGPIAREDLRDLVH-------SQVQRSVE 325
Cdd:PLN02174 241 IAGKWgCNNGQACISPDYILTTK----EYAPKVIDAMKKEL-----ETFYGKNPMESKDMSRIVNsthfdrlSKLLDEKE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 326 AGAELLWGGHvPNAPGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERALGI 405
Cdd:PLN02174 312 VSDKIVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERF 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499235697 406 ARRLEAGSCFINTMVK--SDPRLPFGGVKQSGYGrelSHHGIREF 448
Cdd:PLN02174 391 AATVSAGGIVVNDIAVhlALHTLPFGGVGESGMG---AYHGKFSF 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
24-437 |
5.16e-19 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 90.42 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 24 IDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEeflqp 103
Cdd:PRK11809 684 VEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVR----- 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 104 eqSEIDGAkgivAFEPLGVILGVMPWNFPY----WQVlrfaAPILMAGNGIVVKHA---PNVTGCAIAIeklFRDAGFPE 176
Cdd:PRK11809 759 --DDFDND----THRPLGPVVCISPWNFPLaiftGQV----AAALAAGNSVLAKPAeqtPLIAAQAVRI---LLEAGVPA 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 177 hlyravhidlDEVDRLTG-------FMIDHPVIKAVSVTGSTgagqAVAakagKALKRSV--------------LELGGS 235
Cdd:PRK11809 826 ----------GVVQLLPGrgetvgaALVADARVRGVMFTGST----EVA----RLLQRNLagrldpqgrpipliAETGGQ 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 236 DPYIVLEDADLAQAVDACVAGRLLNAGQSCiAAKRFIVRKEIIGEFTKKIVQ-RMQTAVMGDPFAKSTEVGPIAREDLRD 314
Cdd:PRK11809 888 NAMIVDSSALTEQVVADVLASAFDSAGQRC-SALRVLCLQDDVADRTLKMLRgAMAECRMGNPDRLSTDIGPVIDAEAKA 966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 315 LVHSQVQRSVEAGAElLWGGHVPNAPGW----YYPPTV--LSGVKpgmpAYSEEIFGPVATIIEVADD--DEAVAIANDS 386
Cdd:PRK11809 967 NIERHIQAMRAKGRP-VFQAARENSEDWqsgtFVPPTLieLDSFD----ELKREVFGPVLHVVRYNRNqlDELIEQINAS 1041
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 499235697 387 EFGLGSAVFSQDVERALGIARRLEAGSCFIN-TMVKSDPRL-PFGGVKQSGYG 437
Cdd:PRK11809 1042 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrNMVGAVVGVqPFGGEGLSGTG 1094
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
121-406 |
3.42e-18 |
|
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: 86.94 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 121 GVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAG-FPEHLYRAVHIDL-DEVDRLTGFmiD 198
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVgDLLDHLGEQ--D 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 199 HpvikaVSVTGStgagqavaAKAGKALKRSVLELGGSDPYIVleDADlaqAVDACVAG------------------RLL- 259
Cdd:cd07128 224 V-----VAFTGS--------AATAAKLRAHPNIVARSIRFNA--EAD---SLNAAILGpdatpgtpefdlfvkevaREMt 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 260 -NAGQSCIAAKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPIAREDLRDLVHSQVQRsVEAGAELLWGGHVPN 338
Cdd:cd07128 286 vKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 339 AP-------GWYYPPTVLSGVKP-GMPAYSE-EIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQDVERA----LGI 405
Cdd:cd07128 365 EVvgadaekGAFFPPTLLLCDDPdAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFArelvLGA 444
|
.
gi 499235697 406 A 406
Cdd:cd07128 445 A 445
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
121-406 |
2.21e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 78.21 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 121 GVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDAG-FPEHlyrAVHI----DLDEVDRLTGF 195
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAG---ALSVvcgsSAGLLDHLQPF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 196 MIdhpvikaVSVTGSTGAGQAVAAKAGKAlKRSV---LELGGSDPYIVLEDAD-----LAQAVDACVAGRLLNAGQSCIA 267
Cdd:PRK11903 227 DV-------VSFTGSAETAAVLRSHPAVV-QRSVrvnVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 268 AKRFIVRKEIIGEFTKKIVQRMQTAVMGDPFAKSTEVGPiaredlrdLVHSQVQRSVEAG-------AELLWGG------ 334
Cdd:PRK11903 299 IRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGP--------LVSRAQLAAVRAGlaalraqAEVLFDGggfalv 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499235697 335 HVPNAPGWYYPPTVLSGVKP-GMPAYSE-EIFGPVATIIEVADDDEAVAIANDSEFGLGSAVFSQD----VERALGIA 406
Cdd:PRK11903 371 DADPAVAACVGPTLLGASDPdAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDaaflAAAALELA 448
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
24-411 |
3.49e-14 |
|
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: 74.11 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 24 IDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLEMGKPFSQAVAEVNKCAWVCDYFADHAEE--FL 101
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 102 QPEqseIDGAkgIVAFEPLG--------VILGVM----PWNFPywqvlrFA--------APILMAGNGIVVKHAPNVTG- 160
Cdd:cd07129 81 DAR---IDPA--DPDRQPLPrpdlrrmlVPLGPVavfgASNFP------LAfsvaggdtASALAAGCPVVVKAHPAHPGt 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 161 ---CAIAIEKLFRDAGFPEHLYRAVHIDLDEVDRLtgfMIDHPVIKAVSVTGSTGAGQAVAAKAgkaLKRSV-----LEL 232
Cdd:cd07129 150 selVARAIRAALRATGLPAGVFSLLQGGGREVGVA---LVKHPAIKAVGFTGSRRGGRALFDAA---AARPEpipfyAEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 233 GGSDPYIVLEDA------DLAQAVdacVAGRLLNAGQSC-----------IAAKRFIvrkEIIGE-FTKKIVQRMQTAVM 294
Cdd:cd07129 224 GSVNPVFILPGAlaergeAIAQGF---VGSLTLGAGQFCtnpglvlvpagPAGDAFI---AALAEaLAAAPAQTMLTPGI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 295 GDPFAKSTEvgpiaredlrdlvhsqvQRSVEAGAELLWGGHVPnAPGWYYPPTVL--SGVK-PGMPAYSEEIFGPVATII 371
Cdd:cd07129 298 AEAYRQGVE-----------------ALAAAPGVRVLAGGAAA-EGGNQAAPTLFkvDAAAfLADPALQEEVFGPASLVV 359
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 499235697 372 EVADDDEAVAIANDSEFGLGSAVFS--QDVERALGIARRLEA 411
Cdd:cd07129 360 RYDDAAELLAVAEALEGQLTATIHGeeDDLALARELLPVLER 401
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
118-383 |
5.09e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 61.13 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 118 EPLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVKHAPNVTGCAIAIEKLFRDA----GFPEHLYraVHIDLDEVDrLT 193
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLI--GWIDNPSIE-LA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 194 GFMIDHPVIKAVSVTGstgaGQAVAAKAGKALKRSVLELGGSDPYIVLEDADLAQAVDACVAGRLLNAGQSCIAAKRFIV 273
Cdd:cd07081 171 QRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 274 RKEIIGEFTKKIVQRMQTAVMGDPFAKsteVGPIAREDLrDLVHSQVQRSVEAGAELLwGGHVPNAPGWYYPPTVLSGVK 353
Cdd:cd07081 247 VDSVYDEVMRLFEGQGAYKLTAEELQQ---VQPVILKNG-DVNRDIVGQDAYKIAAAA-GLKVPQETRILIGEVTSLAEH 321
|
250 260 270
....*....|....*....|....*....|
gi 499235697 354 pgmPAYSEEIFGPVATIIEVADDDEAVAIA 383
Cdd:cd07081 322 ---EPFAHEKLSPVLAMYRAANFADADAKA 348
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
119-386 |
1.40e-09 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 60.18 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 119 PLGVILGVMPWNFPYWQVL--RFAApiLMAGNGIVVKHAPN-VTGCAIAIE---KLFRDAGF-PEHLYRAVHidlDEVDR 191
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYpgLFAS--LATGNPVIVKPHPAaILPLAITVQvarEVLAEAGFdPNLVTLAAD---TPEEP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 192 LTGFMIDHPVIKAVSVTGSTGAGQAVAAKAGKALKRSvlELGGSDPYIVlEDADLAQAVDACVAGRL-LNAGQSCIAAKR 270
Cdd:cd07127 268 IAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQVYT--EKAGVNTVVV-DSTDDLKAMLRNLAFSLsLYSGQMCTTPQN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 271 FIVRKEII---------GEFTKKIVQRMQtAVMGDPfAKSTEV-GPIAREDLRDLVH--SQVQRSVEAGAELlwgGHVPN 338
Cdd:cd07127 345 IYVPRDGIqtddgrksfDEVAADLAAAID-GLLADP-ARAAALlGAIQSPDTLARIAeaRQLGEVLLASEAV---AHPEF 419
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499235697 339 APGWYYPPTVLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDS 386
Cdd:cd07127 420 PDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARES 467
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
24-424 |
3.00e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 58.76 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 24 IDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLE--MGKpfsqavaevnkcawVCDYFADH---AE 98
Cdd:PRK15398 38 VDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEEtgMGR--------------VEDKIAKNvaaAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 99 -----EFLQPEQseIDGAKGIVAFE--PLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK-H--APNVTGCAIA-IEK 167
Cdd:PRK15398 104 ktpgvEDLTTEA--LTGDNGLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSpHpgAKKVSLRAIElLNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 168 LFRDAGFPEHLYRAV-HIDLDEVDRltgfMIDHPVIKAVSVTGstgaGQAVAAKAGKALKRSVLELGGSDPYIVLEDADL 246
Cdd:PRK15398 182 AIVAAGGPENLVVTVaEPTIETAQR----LMKHPGIALLVVTG----GPAVVKAAMKSGKKAIGAGAGNPPVVVDETADI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 247 AQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEF------------TKKIVQRMQTAVMGDPFAKSTE-VGPIAREDLR 313
Cdd:PRK15398 254 EKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELmrlmekngavllTAEQAEKLQKVVLKNGGTVNKKwVGKDAAKILE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 314 dlvhsQVQRSVEAGAELLwgghvpnapgwyypptvLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFGL--G 391
Cdd:PRK15398 334 -----AAGINVPKDTRLL-----------------IVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhT 391
|
410 420 430
....*....|....*....|....*....|...
gi 499235697 392 SAVFSQDVERALGIARRLEAgSCFintmVKSDP 424
Cdd:PRK15398 392 AIMHSRNVDNLNKMARAIQT-SIF----VKNGP 419
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
24-410 |
1.75e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 53.39 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 24 IDSVLRQADADFRRWRSTSFGERRTCMKRLAELLREQAEKHGRIITLE--MGKpfsqavaevnkcawVCDYFADH----- 96
Cdd:cd07121 6 VDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEEtgMGR--------------VEDKIAKNhlaae 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 97 ---AEEFLQPEQseIDGAKGIVAFE--PLGVILGVMPWNFPYWQVLRFAAPILMAGNGIVVK-H--APNVTGCAIA-IEK 167
Cdd:cd07121 72 ktpGTEDLTTTA--WSGDNGLTLVEyaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNpHpgAKKVSAYAVElINK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 168 LFRDAGFPEHLyrAVHI---DLDEVDRltgfMIDHPVIKAVSVTGstgaGQAVAAKAGKALKRSVLELGGSDPYIVLEDA 244
Cdd:cd07121 150 AIAEAGGPDNL--VVTVeepTIETTNE----LMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 245 DLAQAVDACVAGRLLNAGQSCIAAKRFIVRKEIIGEF-------------TKKIVQRMQTAVMGDPF--AKSTEVGPIAR 309
Cdd:cd07121 220 DIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLiaamqrngayvlnDEQAEQLLEVVLLTNKGatPNKKWVGKDAS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 310 EDLrdlvhSQVQRSVEAGAELLwgghvpnapgwyypptvLSGVKPGMPAYSEEIFGPVATIIEVADDDEAVAIANDSEFG 389
Cdd:cd07121 300 KIL-----KAAGIEVPADIRLI-----------------IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHG 357
|
410 420
....*....|....*....|...
gi 499235697 390 L--GSAVFSQDVERALGIARRLE 410
Cdd:cd07121 358 NrhTAIIHSKNVENLTKMARAMQ 380
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
107-418 |
1.46e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 50.18 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 107 EIDGAKGIVAF-EPLGVILGVMPWNFPYWQVLrFAAPI-LMAGNGIVVKHAPNVTGCAIAIEKLFRDA----GFPEHLyr 180
Cdd:cd07122 82 EEDEEKGIVEIaEPVGVIAALIPSTNPTSTAI-FKALIaLKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGL-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 181 aVHIdLDEVD-RLTGFMIDHPVIKAVSVTGSTGAGQAvAAKAGK-AlkrsvleLG---GSDPYIVLEDADLAQAVDACVA 255
Cdd:cd07122 159 -IQW-IEEPSiELTQELMKHPDVDLILATGGPGMVKA-AYSSGKpA-------IGvgpGNVPAYIDETADIKRAVKDIIL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 256 GRLLNAG------QSCIAAKRfiVRKEIIGEF--------TKKIVQRMQTAVMGDPFAKSTEVgpiaredlrdlvhsqVQ 321
Cdd:cd07122 229 SKTFDNGticaseQSVIVDDE--IYDEVRAELkrrgayflNEEEKEKLEKALFDDGGTLNPDI---------------VG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 322 RSVEAGAELLwGGHVPnapgwyYPPTVL----SGVKPGMPaYSEEIFGPVATIIEVADDDEAVAIAND-SEF-GLG--SA 393
Cdd:cd07122 292 KSAQKIAELA-GIEVP------EDTKVLvaeeTGVGPEEP-LSREKLSPVLAFYRAEDFEEALEKARElLEYgGAGhtAV 363
|
330 340
....*....|....*....|....*
gi 499235697 394 VFSQDVERALGIARRLEAGSCFINT 418
Cdd:cd07122 364 IHSNDEEVIEEFALRMPVSRILVNT 388
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
109-418 |
2.96e-04 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 43.25 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 109 DGAKGI--VAfEPLGVILGVMPWNFPYWQVLrFAAPI-LMAGNGIVVKHAPNVTGCAIAIEKLFRDA----GFPEHLYRa 181
Cdd:PRK13805 97 DDEFGIieIA-EPVGVIAGITPTTNPTSTAI-FKALIaLKTRNPIIFSFHPRAQKSSIAAAKIVLDAavaaGAPKDIIQ- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 182 vHIDLDEVDrLTGFMIDHPVIKAVSVTGstGAGQAVAA-KAGK-AlkrsvleLG---GSDPYIVLEDADLAQAVDACVAG 256
Cdd:PRK13805 174 -WIEEPSVE-LTNALMNHPGIALILATG--GPGMVKAAySSGKpA-------LGvgaGNVPAYIDKTADIKRAVNDILLS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 257 RLLNAGQSCIAAKRFIVRKEIIGEFtkkiVQRMQTavMGDPFAKSTEvgpiaREDLRDLVHSQ---------VQRSVEAG 327
Cdd:PRK13805 243 KTFDNGMICASEQAVIVDDEIYDEV----KEEFAS--HGAYFLNKKE-----LKKLEKFIFGKengalnadiVGQSAYKI 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499235697 328 AELlwgghvpnaPGWYYPPTV------LSGVKPGMPaYSEEIFGPVATIIEVADDDEAVAIAND-SEF-GLG--SAVFSQ 397
Cdd:PRK13805 312 AEM---------AGFKVPEDTkiliaeVKGVGESEP-LSHEKLSPVLAMYKAKDFEDAVEKAEKlVEFgGLGhtAVIYTN 381
|
330 340
....*....|....*....|.
gi 499235697 398 DVERALGIARRLEAGSCFINT 418
Cdd:PRK13805 382 DDELIKEFGLRMKACRILVNT 402
|
|
| |
