|
Name |
Accession |
Description |
Interval |
E-value |
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
9-488 |
0e+00 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 890.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 9 SRLLIDGKLASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGLRVRCVRQLRDVLREHLEEL 88
Cdd:TIGR04284 1 SRLLIDGKLVAGSAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDETDWSRDTALRVRCLRQLRDALRAHVEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGYSWTQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLA 168
Cdd:TIGR04284 81 RELTIAEVGAPRMLTAGAQLEGPVDDLGFAADLAESYAWTTDLGVASPMGIPTRRTLRREAVGVVGAITPWNFPHQINLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 169 KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMAD 248
Cdd:TIGR04284 161 KLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 249 AAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKP 328
Cdd:TIGR04284 241 AAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 329 GTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDD 408
Cdd:TIGR04284 321 GTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 409 AVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAIATAA 488
Cdd:TIGR04284 401 AVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLIATAA 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-485 |
0e+00 |
|
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: 673.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAGAQ 107
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 108 LEGPIDDLRFAADTAEGYSWTQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPD 187
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 188 TPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFV 267
Cdd:cd07089 162 TPLSALLLGEIIAE-TDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 268 VLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSY 347
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 348 LDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGA 427
Cdd:cd07089 321 IARGRDEGARLVTGGGRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1231751504 428 DADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAIA 485
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
11-485 |
0e+00 |
|
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: 535.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGK-LASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWStNTGL--RVRCVRQLRDVLREHLEE 87
Cdd:cd07138 1 FYIDGAwVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WS-ATSVeeRAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 88 LRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGYSWTQDLGHATplgiptrrsVVREAVGVVGAITPWNFP-HQIn 166
Cdd:cd07138 78 LAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNSL---------VVREPIGVCGLITPWNWPlNQI- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 167 LAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVM 246
Cdd:cd07138 148 VLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDE-AGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPT 326
Cdd:cd07138 227 EAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 327 KPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGG-GRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDG 405
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 406 DDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWySADVPFGGYKQSGNGREMGVAGFEEYLETKAIA 485
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAF-NPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
10-485 |
2.50e-177 |
|
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: 506.20 E-value: 2.50e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 10 RLLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWS-TNTGLRVRCVRQLRDVLREHLEE 87
Cdd:COG1012 7 PLFIGGEWVAAASGEtFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPA--WAaTPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 88 LRELTISEVGAPRMLtAGAQLEGPIDDLRFAADTAEGYswtqdLGHATPLGIPTRRS-VVREAVGVVGAITPWNFPHQIN 166
Cdd:COG1012 85 LAALLTLETGKPLAE-ARGEVDRAADFLRYYAGEARRL-----YGETIPSDAPGTRAyVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 167 LAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVM 246
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEE-AGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPT 326
Cdd:COG1012 238 AAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 327 KPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPaEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGD 406
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRP-DGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 407 DDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVN-GGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAIA 485
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINdGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
11-484 |
2.25e-170 |
|
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: 488.24 E-value: 2.25e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGK-LASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNT-GLRVRCVRQLRDVLREHLEEL 88
Cdd:cd07139 1 LFIGGRwVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSpAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGYSWTQDlgHATPLGIPTRrsVVREAVGVVGAITPWNFPHQINLA 168
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEER--RPGSGGGHVL--VRREPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 169 KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTStDHTLGAMLAKDPRVDMVSFTGSTATGRSVMAD 248
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEE-AGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 249 AAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKP 328
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 329 GTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDD 408
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231751504 409 AVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGgvwYSAD--VPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNG---FRLDfgAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-484 |
1.05e-162 |
|
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: 468.16 E-value: 1.05e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 19 SGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVG 97
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRkTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 98 APRMLTAGaQLEGPIDDLRFAADTAEgyswtQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAG 177
Cdd:pfam00171 81 KPLAEARG-EVDRAIDVLRYYAGLAR-----RLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 178 NTVVLKPAPDTPWVAAVIGELIAEHtDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVF 257
Cdd:pfam00171 155 NTVVLKPSELTPLTALLLAELFEEA-GLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 258 LELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVIS 337
Cdd:pfam00171 234 LELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 338 ARQRDRVQSYLDLALAEGGTFACGGgrPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSP 417
Cdd:pfam00171 314 KAQLERVLKYVEDAKEEGAKLLTGG--EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231751504 418 YGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSAD-VPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
55-484 |
1.16e-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: 431.63 E-value: 1.16e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 55 RRAFDDtdWSTNTG-LRVRCVRQLRDVLREHLEELRELTISEVGAPRmLTAGAQLEGPIDDLRFAADTAEGYswtqdLGH 133
Cdd:cd07078 8 RAAFKA--WAALPPaERAAILRKLADLLEERREELAALETLETGKPI-EEALGEVARAADTFRYYAGLARRL-----HGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 134 ATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINI 212
Cdd:cd07078 80 VIPSPDPGELAiVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAE-AGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 213 VTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQG 292
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 293 CAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPaEQAAGF 372
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL-EGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 373 FIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGG-VW 451
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYsVG 397
|
410 420 430
....*....|....*....|....*....|...
gi 1231751504 452 YSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07078 398 AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-485 |
1.19e-139 |
|
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: 409.26 E-value: 1.19e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFDDTdWSTNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAGA 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGW-SRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 107 QLEGPIDDLRFAADTA---EGYSWTQDLGHatplgiptRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 183
Cdd:cd07093 80 DIPRAAANFRFFADYIlqlDGESYPQDGGA--------LNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 184 PAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGK 263
Cdd:cd07093 152 PSEWTPLTAWLLAELANE-AGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 264 SAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDR 343
Cdd:cd07093 231 NPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 344 VQSYLDLALAEGGTFACGGGRP--AEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLS 421
Cdd:cd07093 311 VLGYVELARAEGATILTGGGRPelPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231751504 422 ATVYGADADRAAGVASRLRAGTVNVNggVWYSAD--VPFGGYKQSGNGREMGVAGFEEYLETKAIA 485
Cdd:cd07093 391 AYVWTRDLGRAHRVARRLEAGTVWVN--CWLVRDlrTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-484 |
1.78e-139 |
|
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: 410.16 E-value: 1.78e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 13 IDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGL-RVRCVRQLRDVLREHLEELRE 90
Cdd:cd07119 2 IDGEWVEAASGKtRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQeRAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 91 LTISEVGAPRmltagAQLEGPIDD----LRFAADTAegyswTQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQIN 166
Cdd:cd07119 82 LETLNTGKTL-----RESEIDIDDvancFRYYAGLA-----TKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 167 LAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVM 246
Cdd:cd07119 152 AWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEE-AGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPT 326
Cdd:cd07119 231 RAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 327 KPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQ--AAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHD 404
Cdd:cd07119 311 DADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 405 GDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07119 391 TEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
25-484 |
4.72e-138 |
|
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: 405.45 E-value: 4.72e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 25 FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMLT 103
Cdd:cd07112 4 FATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSrLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 104 AGAQLEGPIDDLRFAADTAEgyswtQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 183
Cdd:cd07112 84 LAVDVPSAANTFRWYAEAID-----KVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 184 PAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAAT-IKKVFLELGG 262
Cdd:cd07112 159 PAEQSPLTALRLAELALE-AGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 263 KSAFVVLDDA-DLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQR 341
Cdd:cd07112 238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 342 DRVQSYLDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLS 421
Cdd:cd07112 318 DKVLGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231751504 422 ATVYGADADRAAGVASRLRAGTVNVNGgvwYSAD---VPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07112 398 ASVWTSDLSRAHRVARRLRAGTVWVNC---FDEGditTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-484 |
9.48e-137 |
|
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: 401.93 E-value: 9.48e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGL-RVRCVRQLRDVLREHLEELRELTISEVGAPRMLTaG 105
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTeRGKLLRRLADLIEANAEELAELETRDNGKLIRET-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLEGPIDDLRF---AADTAEGyswtqdlgHATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVV 181
Cdd:cd07114 80 AQVRYLAEWYRYyagLADKIEG--------AVIPVDKGDYLNfTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 182 LKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELG 261
Cdd:cd07114 152 LKPSEHTPASTLELAKLAEE-AGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 262 GKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQR 341
Cdd:cd07114 231 GKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 342 DRVQSYLDLALAEGGTFACGGGRP--AEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYG 419
Cdd:cd07114 311 EKVERYVARAREEGARVLTGGERPsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231751504 420 LSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07114 391 LAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
11-484 |
1.76e-134 |
|
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: 396.96 E-value: 1.76e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGL-RVRCVRQLRDVLREHLEEL 88
Cdd:cd07091 6 LFINNEFVDSVSGKtFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPReRGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPRMLTAGAQLEGPIDDLR-FA--ADTAEGYSwtqdlghatplgIPTRRSVV----REAVGVVGAITPWNF 161
Cdd:cd07091 86 AALESLDNGKPLEESAKGDVALSIKCLRyYAgwADKIQGKT------------IPIDGNFLaytrREPIGVCGQIIPWNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 162 PHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTAT 241
Cdd:cd07091 154 PLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKE-AGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 242 GRSVMADAAAT-IKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSI 320
Cdd:cd07091 233 GRTIMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 321 KPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTV 400
Cdd:cd07091 313 VVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSK--GYFIQPTVFTDVKDDMKIAKEEIFGPVVTI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 401 IAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLE 480
Cdd:cd07091 391 LKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQ 470
|
....
gi 1231751504 481 TKAI 484
Cdd:cd07091 471 VKAV 474
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
9-482 |
2.67e-134 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 396.59 E-value: 2.67e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 9 SRLLIDGKLASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNT-GLRVRCVRQLRDVLREHLEE 87
Cdd:PRK13473 3 TKLLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTpKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 88 LRELTISEVGAPRMLTAGAQLEGPIDDLRF---AADTAEGYSWTQDL-GHATplgiptrrSVVREAVGVVGAITPWNFPH 163
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFfagAARCLEGKAAGEYLeGHTS--------MIRRDPVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 164 QINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHtdMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGR 243
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI--LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 244 SVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPG 323
Cdd:PRK13473 231 HVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 324 DPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEqAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAH 403
Cdd:PRK13473 311 DPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPD-GKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPF 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231751504 404 DGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETK 482
Cdd:PRK13473 390 DDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-484 |
2.69e-132 |
|
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: 390.35 E-value: 2.69e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFddTDWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPrmlTAGA 106
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAF--PGWSaTPLEERRAALLAIADAIEANAEELARLLTLEQGKP---LAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 107 QLEgpiddLRFAADtaegysWTQdlgHATPLGIP--------TRRSVVREA-VGVVGAITPWNFPHQINLAKLGPALAAG 177
Cdd:cd07106 77 QFE-----VGGAVA------WLR---YTASLDLPdeviedddTRRVELRRKpLGVVAAIVPWNFPLLLAAWKIAPALLAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 178 NTVVLKPAPDTPWVAAVIGELIAEHtdMPPGVINIVTStDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVF 257
Cdd:cd07106 143 NTVVLKPSPFTPLCTLKLGELAQEV--LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 258 LELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVIS 337
Cdd:cd07106 220 LELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 338 ARQRDRVQSYLDLALAEGGTFACGGGRPaeQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSP 417
Cdd:cd07106 300 KMQYDKVKELVEDAKAKGAKVLAGGEPL--DGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSE 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231751504 418 YGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07106 378 YGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-485 |
6.48e-132 |
|
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: 389.48 E-value: 6.48e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWStNTGLRVRC--VRQLRDVLREHLEELRELTISEVGAPrmlTAG 105
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WR-KTTARERAaiLRRWADLIRERAEDLARLLTLEQGKP---LAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLEgpiddLRFAADTAEGYS--WTQDLGHATPLGIPTRR-SVVREAVGVVGAITPWNFPhqINLA--KLGPALAAGNTV 180
Cdd:cd07103 76 ARGE-----VDYAASFLEWFAeeARRIYGRTIPSPAPGKRiLVIKQPVGVVAAITPWNFP--AAMItrKIAPALAAGCTV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 181 VLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLEL 260
Cdd:cd07103 149 VLKPAEETPLSALALAELAEE-AGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 261 GGKSAFVVLDDADLAAAcsVAGFSVCV--HAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISA 338
Cdd:cd07103 228 GGNAPFIVFDDADLDKA--VDGAIASKfrNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 339 RQRDRVQSYLDLALAEGGTFACGGGRPAEqaAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPY 418
Cdd:cd07103 306 RAVEKVEALVEDAVAKGAKVLTGGKRLGL--GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPY 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231751504 419 GLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAIA 485
Cdd:cd07103 384 GLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-486 |
1.90e-127 |
|
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: 378.21 E-value: 1.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTnTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAGAQ 107
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTT-PAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 108 LEGPIDDLRF---AADTAEGYSWTQDL-GHATplgiptrrSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 183
Cdd:cd07092 81 LPGAVDNFRFfagAARTLEGPAAGEYLpGHTS--------MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 184 PAPDTPWVAAVIGELIAEhtDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGK 263
Cdd:cd07092 153 PSETTPLTTLLLAELAAE--VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 264 SAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDR 343
Cdd:cd07092 231 APVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 344 VQSYLDLAlAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSAT 423
Cdd:cd07092 311 VAGFVERA-PAHARVLTGGRRAEGP--GYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231751504 424 VYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAIAT 486
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
27-484 |
2.53e-127 |
|
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: 377.85 E-value: 2.53e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNTG-LRVRCVRQLRDVLREHLEELRELTISEVGAPRMlTAG 105
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGaERAKYLRAIAEGVRERREELAELEARDNGKPLD-EAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLEGPIDDLRFAADTAEGYSWTQDLghATPLGIPTRRSVVR-EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKP 184
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLDAKAER--AVPLPSEDFKARVRrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 185 APDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKS 264
Cdd:cd07110 156 SELTSLTELELAEIAAE-AGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 265 AFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRV 344
Cdd:cd07110 235 PIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 345 QSYLDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATV 424
Cdd:cd07110 315 LSFIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 425 YGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
27-484 |
1.05e-125 |
|
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: 373.70 E-value: 1.05e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNTGL-RVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAG 105
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAeRGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AqlegpidDLRFAADTAEGYS-WTQDL-GHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 183
Cdd:cd07115 79 L-------DVPRAADTFRYYAgWADKIeGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 184 PAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGK 263
Cdd:cd07115 152 PAELTPLSALRIAELMAE-AGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 264 SAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDR 343
Cdd:cd07115 231 SANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 344 VQSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSAT 423
Cdd:cd07115 311 VLDYVDVGREEGARLLTGGKRPGAR--GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231751504 424 VYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07115 389 VWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-484 |
1.12e-124 |
|
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: 371.29 E-value: 1.12e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAGa 106
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 107 QLEGPIDDLRFAADTAEgyswtQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAP 186
Cdd:cd07120 80 EISGAISELRYYAGLAR-----TEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 187 DTPWVAAVIGELIAEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAF 266
Cdd:cd07120 155 QTAQINAAIIRILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 267 VVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQS 346
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 347 YLDLALAEGGTFACGGGRPAEQ-AAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVY 425
Cdd:cd07120 315 MVERAIAAGAEVVLRGGPVTEGlAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVW 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1231751504 426 GADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07120 395 TRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
55-484 |
1.62e-123 |
|
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: 368.20 E-value: 1.62e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 55 RRAFDDTDWSTNTGL-RVRCVRQLRDVLREHLEELRELTISEVGAPrMLTAGAQLEGPIDDLRFAADTA---EGYSWTqD 130
Cdd:cd07118 29 RKAFDKGPWPRMSGAeRAAVLLKVADLIRARRERLALIETLESGKP-ISQARGEIEGAADLWRYAASLArtlHGDSYN-N 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 131 LGHATpLGIptrrsVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVI 210
Cdd:cd07118 107 LGDDM-LGL-----VLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIE-AGLPAGVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 211 NIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAG 290
Cdd:cd07118 180 NIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 291 QGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRpAEQAA 370
Cdd:cd07118 260 ECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGER-LASAA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 371 GFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGV 450
Cdd:cd07118 339 GLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFL 418
|
410 420 430
....*....|....*....|....*....|....
gi 1231751504 451 WYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07118 419 DGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
61-484 |
1.46e-122 |
|
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: 364.93 E-value: 1.46e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 61 TDWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRmLTAGAQLEGPIDDLRFAADTAegyswTQDLGHATPLGI 139
Cdd:cd07104 14 KAWAaTPPQERAAILRKAAEILEERRDEIADWLIRESGSTR-PKAAFEVGAAIAILREAAGLP-----RRPEGEILPSDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 140 PTRRS-VVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDMPPGVINIVTSTDH 218
Cdd:cd07104 88 PGKESmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIFEEAGLPKGVLNVVPGGGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 219 TLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTR 298
Cdd:cd07104 168 EIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 299 LVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGgrpaeQAAGFFIEPTV 378
Cdd:cd07104 248 ILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG-----TYEGLFYQPTV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 379 IAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGG-VWYSADVP 457
Cdd:cd07104 323 LSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQtVNDEPHVP 402
|
410 420
....*....|....*....|....*..
gi 1231751504 458 FGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07104 403 FGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
13-482 |
3.14e-122 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 365.29 E-value: 3.14e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 13 IDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNTGL-RVRCVRQLRDVLREHLEELRE 90
Cdd:TIGR01804 2 IDGEYVEDSAGTtREIINPANGEVIATVHAATPEDVERAIAAARRAQGE--WAAMSPMeRGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 91 LTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGyswtqDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKL 170
Cdd:TIGR01804 80 LETLDTGKTLQETIVADMDSGADVFEFFAGLAPA-----LNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 171 GPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAA 250
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEE-AGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 251 ATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGT 330
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 331 VCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAA--GFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDD 408
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 409 AVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETK 482
Cdd:TIGR01804 394 VIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
27-484 |
3.57e-116 |
|
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: 349.68 E-value: 3.57e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFddTDWSTNTGL-RVRCVRQLRDVLREHLEELRELTISEVGAPrMLTAG 105
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQ--KEWSATSGMeRGRILRKAADLLRERNDEIARLETIDNGKP-IEEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLEGPIDDLRFAADTAEGYSwtqdlGHATPLG----IPTRRsvvrEAVGVVGAITPWNFPHQINLAKLGPALAAGNTVV 181
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLS-----GEHVPLPggsfAYTRR----EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 182 LKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTStDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELG 261
Cdd:cd07090 149 YKPSPFTPLTALLLAEILTE-AGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 262 GKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQR 341
Cdd:cd07090 227 GKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 342 DRVQSYLDLALAEGGTFACGGGRPAEQ---AAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPY 418
Cdd:cd07090 307 EKVLGYIESAKQEGAKVLCGGERVVPEdglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTY 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231751504 419 GLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07090 387 GLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
25-484 |
6.78e-116 |
|
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: 349.72 E-value: 6.78e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 25 FATVNPATEEVLGEAANADAADMDRAIDAARRAFD-DTDWST-NTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRML 102
Cdd:cd07141 24 FPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlGSPWRTmDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 103 TAGAQLEGPIDDLRFAADTAEGYswtqdLGHATPLGIP----TRRsvvrEAVGVVGAITPWNFPHQINLAKLGPALAAGN 178
Cdd:cd07141 104 SYLVDLPGAIKVLRYYAGWADKI-----HGKTIPMDGDfftyTRH----EPVGVCGQIIPWNFPLLMAAWKLAPALACGN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 179 TVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAAT-IKKVF 257
Cdd:cd07141 175 TVVLKPAEQTPLTALYLASLIKE-AGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSnLKRVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 258 LELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVIS 337
Cdd:cd07141 254 LELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 338 ARQRDRVQSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSP 417
Cdd:cd07141 334 EEQFKKILELIESGKKEGAKLECGGKRHGDK--GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTT 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231751504 418 YGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07141 412 YGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
28-485 |
4.78e-115 |
|
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: 346.53 E-value: 4.78e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPrMLTAGAQ 107
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKP-LTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 108 LEGPIDDLRFAADTAEGYSwtqdlGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPD 187
Cdd:cd07109 81 VEAAARYFEYYGGAADKLH-----GETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 188 TPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFV 267
Cdd:cd07109 156 APLTALRLAELAEE-AGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 268 VLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGdPTKPGTVCGPVISARQRDRVQSY 347
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 348 LDLALAEGGTFACGGGRPAEQAA-GFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYG 426
Cdd:cd07109 314 VARARARGARIVAGGRIAEGAPAgGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 427 ADADRAAGVASRLRAGTVNVN-----GGVwysaDVPFGGYKQSGNGREMGVAGFEEYLETKAIA 485
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNnygagGGI----ELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-484 |
5.98e-115 |
|
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: 346.93 E-value: 5.98e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 12 LIDGKLAsGGAGGFATVNPA-TEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNTGL-RVRCVRQLRDVLREHLEELR 89
Cdd:cd07097 4 YIDGEWV-AGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEaRADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 90 ELTISEVGAPrMLTAGAQLEGPIDDLRFAAdtAEGYSWTQDLGHATPLGipTRRSVVREAVGVVGAITPWNFPHQINLAK 169
Cdd:cd07097 81 RLLTREEGKT-LPEARGEVTRAGQIFRYYA--GEALRLSGETLPSTRPG--VEVETTREPLGVVGLITPWNFPIAIPAWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 170 LGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADA 249
Cdd:cd07097 156 IAPALAYGNTVVFKPAELTPASAWALVEILEE-AGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 250 AATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPG 329
Cdd:cd07097 235 AARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 330 TVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDA 409
Cdd:cd07097 315 VDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231751504 410 VRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVN---GGVWYSadVPFGGYKQSGNG-REMGVAGFEEYLETKAI 484
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptAGVDYH--VPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
11-484 |
1.14e-113 |
|
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: 344.01 E-value: 1.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGK-LASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGLRVRCVRQLRDVLREHLEELR 89
Cdd:cd07144 10 LFINNEfVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVEKNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 90 ELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGYSwtqdlGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAK 169
Cdd:cd07144 90 AIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQ-----GKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 170 LGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADA 249
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKE-AGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 250 AATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVA-IAAGTMGSIKPGDPTKP 328
Cdd:cd07144 244 AQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEkFVEHVKQNYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 329 GTVCGPVISARQRDRVQSYLDLALAEGGTFACGG-GRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDD 407
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGeKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231751504 408 DAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
27-484 |
3.13e-113 |
|
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: 342.05 E-value: 3.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFddTDWSTNTGL-RVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAG 105
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAF--PEWRATTPLeRARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLEGpIDDLRFAADTAEGYSwtqdlGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPA 185
Cdd:cd07107 79 DVMVA-AALLDYFAGLVTELK-----GETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 186 PDTPWVAAVIGELIAEHtdMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSA 265
Cdd:cd07107 153 EQAPLSALRLAELAREV--LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 266 FVVLDDADLAAAC--SVAGFSvCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDR 343
Cdd:cd07107 231 LIVFPDADPEAAAdaAVAGMN-FTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 344 VQSYLDLALAEGGTFACGGGRP--AEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLS 421
Cdd:cd07107 310 VMHYIDSAKREGARLVTGGGRPegPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231751504 422 ATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07107 390 AAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
11-484 |
4.73e-112 |
|
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: 339.89 E-value: 4.73e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDdTDWSTN--TGLRVRCVRQLRDVLREHLEE 87
Cdd:cd07143 9 LFINGEFVDSVHGGtVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE-TDWGLKvsGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 88 LRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEgyswtQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINL 167
Cdd:cd07143 88 LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWAD-----KIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 168 AKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMA 247
Cdd:cd07143 163 WKIAPALAAGNTIVLKPSELTPLSALYMTKLIPE-AGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 248 DAAAT-IKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPT 326
Cdd:cd07143 242 AAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 327 KPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGD 406
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNE--GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231751504 407 DDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07143 400 EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
29-485 |
1.04e-111 |
|
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: 337.76 E-value: 1.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 29 NPATEEVLGEAANADAADMDRAIDAARRAFddTDWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRmLTAGAQ 107
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAaTTPSERERILLKAAEIMERRADDLIDLLIDEGGSTY-GKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 108 LEGPIDDLRFAADTAEGYSwtqdlGHATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAP 186
Cdd:cd07150 82 TTFTPELLRAAAGECRRVR-----GETLPSDSPGTVSmSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 187 DTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAF 266
Cdd:cd07150 157 ETPVIGLKIAEIMEE-AGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 267 VVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQS 346
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 347 YLDLALAEGGTFACGGGRpaeqaAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYG 426
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKY-----DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 427 ADADRAAGVASRLRAGTVNVNGGVWYS-ADVPFGGYKQSGNGREMGVAGFEEYLETKAIA 485
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-484 |
3.63e-110 |
|
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: 334.62 E-value: 3.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 13 IDGKLASGGAGGFATV-NPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNTGL-RVRCVRQLRDVLREHLEELRE 90
Cdd:cd07088 2 INGEFVPSSSGETIDVlNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIeRAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 91 LTISEVGAPRMLtAGAQLEGPIDDLRFAADTA---EGYSWTQDLGHATPLgiptrrsVVREAVGVVGAITPWNFPHQINL 167
Cdd:cd07088 80 LIVEEQGKTLSL-ARVEVEFTADYIDYMAEWArriEGEIIPSDRPNENIF-------IFKVPIGVVAGILPWNFPFFLIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 168 AKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMA 247
Cdd:cd07088 152 RKLAPALVTGNTIVIKPSEETPLNALEFAELVDE-AGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 248 DAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTK 327
Cdd:cd07088 231 AAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 328 PGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPaEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDD 407
Cdd:cd07088 311 AATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRP-EGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 408 DAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGvwySADVPFG---GYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07088 390 EAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-484 |
7.00e-110 |
|
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: 334.15 E-value: 7.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 12 LIDGKLASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNTG-LRVRCVRQLRDVLREHLEELRE 90
Cdd:cd07086 2 VIGGEWVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE--WRKVPApRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 91 LTISEVGAPRMLTAGAQLEGpIDdlrfAADTAEGYSWTQDlGHATPLGIPTRRSV-VREAVGVVGAITPWNFPHQINLAK 169
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEM-ID----ICDYAVGLSRMLY-GLTIPSERPGHRLMeQWNPLGVVGVITAFNFPVAVPGWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 170 LGPALAAGNTVVLKPAPDTPWVAAVIGELIAE---HTDMPPGVINIVTStDHTLGAMLAKDPRVDMVSFTGSTATGRSVM 246
Cdd:cd07086 154 AAIALVCGNTVVWKPSETTPLTAIAVTKILAEvleKNGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPT 326
Cdd:cd07086 233 ETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 327 KPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGD 406
Cdd:cd07086 313 DEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 407 DDAVRIANDSPYGLSATVYGAD---ADRAAGvASRLRAGTVNVNGGVwYSADV--PFGGYKQSGNGREMGVAGFEEYLET 481
Cdd:cd07086 393 EEAIAINNDVPQGLSSSIFTEDlreAFRWLG-PKGSDCGIVNVNIPT-SGAEIggAFGGEKETGGGRESGSDAWKQYMRR 470
|
...
gi 1231751504 482 KAI 484
Cdd:cd07086 471 STC 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
28-484 |
1.24e-109 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 334.39 E-value: 1.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFDDT---DWSTNTG-LRVRCVRQLRDVLREHLEELRELTISEVGAPRmlt 103
Cdd:PLN02467 28 VNPATEETIGDIPAATAEDVDAAVEAARKAFKRNkgkDWARTTGaVRAKYLRAIAAKITERKSELAKLETLDCGKPL--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 104 agAQLEGPIDDL----RFAADTAEGYSWTQDlghaTPLGIPT---RRSVVREAVGVVGAITPWNFPHQINLAKLGPALAA 176
Cdd:PLN02467 105 --DEAAWDMDDVagcfEYYADLAEALDAKQK----APVSLPMetfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 177 GNTVVLKPAPDTPWVAAVIGElIAEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKV 256
Cdd:PLN02467 179 GCTAVLKPSELASVTCLELAD-ICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 257 FLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVI 336
Cdd:PLN02467 258 SLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 337 SARQRDRVQSYLDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDS 416
Cdd:PLN02467 338 SEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDS 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231751504 417 PYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:PLN02467 418 HYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-484 |
1.46e-109 |
|
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: 333.16 E-value: 1.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 12 LIDGKLASGGAGG-FATVNPA-TEEVLGEAANADAADMDRAIDAARRAFDDtdW-STNTGLRVRCVRQLRDVLREHLEEL 88
Cdd:cd07131 2 YIGGEWVDSASGEtFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPE--WrKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPRMLTAGAQLEGpIDDLRFAADTAEgyswtQDLGHATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINL 167
Cdd:cd07131 80 ARLVTREMGKPLAEGRGDVQEA-IDMAQYAAGEGR-----RLFGETVPSELPNKDAmTRRQPIGVVALITPWNFPVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 168 AKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMA 247
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVELFAE-AGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 248 DAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTK 327
Cdd:cd07131 233 TCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 328 PGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAE--QAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDG 405
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 406 DDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNG-GVWYSADVPFGGYKQSGNG-REMGVAGFEEYLETKA 483
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNApTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
.
gi 1231751504 484 I 484
Cdd:cd07131 473 V 473
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-484 |
3.06e-109 |
|
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: 328.42 E-value: 3.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 55 RRAFDDtdWSTNTG-LRVRCVRQLRDVLREHLEELRELTISEVGAPRmLTAGAQLEGPIDDLRFAADTAEGYSwtqdlGH 133
Cdd:cd06534 4 RAAFKA--WAALPPaERAAILRKIADLLEERREELAALETLETGKPI-EEALGEVARAIDTFRYAAGLADKLG-----GP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 134 ATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINI 212
Cdd:cd06534 76 ELPSPDPGGEAyVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQE-AGLPPGVVNV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 213 VTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQG 292
Cdd:cd06534 155 VPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 293 CAITTRLVVPRARYDEAVAIAAgtmgsikpgdptkpgtvcgpvisarqrdrvqsyldlalaeggtfacgggrpaeqaagf 372
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEKLV---------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 373 fiepTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGG-VW 451
Cdd:cd06534 257 ----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSsIG 332
|
410 420 430
....*....|....*....|....*....|...
gi 1231751504 452 YSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd06534 333 VGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
15-484 |
1.28e-108 |
|
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: 330.42 E-value: 1.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 15 GKLASGGAGGFATV-NPATEEVLGEAANADAADMDRAIDAARRAfdDTDWS-TNTGLRVRCVRQLRDVLREHLEELRELT 92
Cdd:cd07151 1 GEWRDGTSERTIDVlNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAaTLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 93 ISEVGAPRmLTAGAQLEGPIDDLRFAADTAegyswTQDLGHATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINLAKLG 171
Cdd:cd07151 79 IRESGSTR-IKANIEWGAAMAITREAATFP-----LRMEGRILPSDVPGKENrVYREPLGVVGVISPWNFPLHLSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 172 PALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAA 251
Cdd:cd07151 153 PALALGNAVVLKPASDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 252 TIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTV 331
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 332 CGPVISARQRDRVQSYLDLALAEGGTFACGGgrpaeQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVR 411
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGG-----EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 412 IANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGG-VWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQpVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
9-486 |
1.88e-108 |
|
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: 330.23 E-value: 1.88e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 9 SRLLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGL-RVRCVRQLRDVLREHLE 86
Cdd:cd07142 4 TKLFINGQFVDAASGKtFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYeRSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 87 ELRELTISEVGAPRMLTAGAQLEGPIDDLRFAAdtaegySWTQDL-GHATPLGIPTRRSVVREAVGVVGAITPWNFPHQI 165
Cdd:cd07142 84 ELAALETWDNGKPYEQARYAEVPLAARLFRYYA------GWADKIhGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 166 NLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSV 245
Cdd:cd07142 158 FAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAE-AGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 246 MADAAAT-IKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGD 324
Cdd:cd07142 237 MQLAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 325 PTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHD 404
Cdd:cd07142 317 PFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSK--GYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 405 GDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07142 395 TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
..
gi 1231751504 485 AT 486
Cdd:cd07142 475 VM 476
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
7-484 |
2.17e-108 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 330.69 E-value: 2.17e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 7 GVSRLLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNTGL-RVRCVRQLRDVLREH 84
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGEtFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI--WAAMTAMeRSRILRRAVDILRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 85 LEELRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGYSWTQdlghatplgIPTRRS----VVREAVGVVGAITPWN 160
Cdd:PRK13252 83 NDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQ---------IPLRGGsfvyTRREPLGVCAGIGAWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 161 FPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTStDHTLGAMLAKDPRVDMVSFTGSTA 240
Cdd:PRK13252 154 YPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTE-AGLPDGVFNVVQG-DGRVGAWLTEHPDIAKVSFTGGVP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 241 TGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSI 320
Cdd:PRK13252 232 TGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 321 KPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGR--PAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVL 398
Cdd:PRK13252 312 RIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERltEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 399 TVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEY 478
Cdd:PRK13252 392 SVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHY 471
|
....*.
gi 1231751504 479 LETKAI 484
Cdd:PRK13252 472 TQIKSV 477
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
12-482 |
5.40e-106 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 324.72 E-value: 5.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 12 LIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFddTDWSTNTGL-RVRCVRQLRDVLREHLEELR 89
Cdd:PLN02278 28 LIGGKWTDAYDGKtFPVYNPATGEVIANVPCMGRAETNDAIASAHDAF--PSWSKLTASeRSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 90 ELTISEVGAPrMLTAGAQLEGPIDDLRFAADTAEGYSwtqdlGHATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINLA 168
Cdd:PLN02278 106 QLMTLEQGKP-LKEAIGEVAYGASFLEYFAEEAKRVY-----GDIIPSPFPDRRLlVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 169 KLGPALAAGNTVVLKPAPDTPWVAAVIGELiAEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMAD 248
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAEL-ALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 249 AAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKP 328
Cdd:PLN02278 259 AAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 329 GTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAeqAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDD 408
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHS--LGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 409 AVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETK 482
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-484 |
8.75e-106 |
|
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: 323.53 E-value: 8.75e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWS-TNTGLRVRCVRQLRDVLREHLEEL 88
Cdd:cd07559 3 NFINGEWVAPSKGEyFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGkTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGYSwtqdlGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLA 168
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQE-----GSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 169 KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHtdMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMAD 248
Cdd:cd07559 156 KLAPALAAGNTVVLKPASQTPLSILVLMELIGDL--LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 249 AAATIKKVFLELGGKSAFVVLDDA-------DLAAACSVAGFSVcvHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIK 321
Cdd:cd07559 234 AAENLIPVTLELGGKSPNIFFDDAmdadddfDDKAEEGQLGFAF--NQGEVCTCPSRALVQESIYDEFIERAVERFEAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 322 PGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQ--AAGFFIEPTVIAGLTNEARVAREEIFGPVLT 399
Cdd:cd07559 312 VGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGglDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 400 VIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYL 479
Cdd:cd07559 392 VITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQ 471
|
....*
gi 1231751504 480 ETKAI 484
Cdd:cd07559 472 QTKNI 476
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
13-484 |
4.93e-105 |
|
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: 321.70 E-value: 4.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 13 IDGKLASGGAGGF-ATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGLRVRCVRQLRDVLREHLEELREL 91
Cdd:cd07113 4 IDGRPVAGQSEKRlDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 92 TISEVGAPRMLTAGAQLEGPIDDLRFAADTAegyswTQDLGHATPLGIPTRRS------VVREAVGVVGAITPWNFPHQI 165
Cdd:cd07113 84 ETLCSGKSIHLSRAFEVGQSANFLRYFAGWA-----TKINGETLAPSIPSMQGerytafTRREPVGVVAGIVPWNFSVMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 166 NLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELiAEHTDMPPGVINIVTSTDHTlGAMLAKDPRVDMVSFTGSTATGRSV 245
Cdd:cd07113 159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAEL-AKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 246 MADAAATIKKVFLELGGKSAFVVLDDADLAAACS---VAGFsvcVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKP 322
Cdd:cd07113 237 GRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEgllTAGF---LHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 323 GDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIA 402
Cdd:cd07113 314 GSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGE--GYFVQPTLVLARSADSRLMREETFGPVVSFVP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 403 HDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETK 482
Cdd:cd07113 392 YEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELK 471
|
..
gi 1231751504 483 AI 484
Cdd:cd07113 472 SV 473
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-486 |
1.26e-104 |
|
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: 319.55 E-value: 1.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFddTDWSTnTGL--RVRCVRQLRDVLREHLEELRELTISEVGAPRMlTAG 105
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQ--RAWAA-LGVegRAQRLLRWKRALADHADELAELLHAETGKPRA-DAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLEGPIDDLRFAADTAEGYSWTQDLghATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKP 184
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVLAPRKV--PTGLLMPNKKAtVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 185 APDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLakDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKS 264
Cdd:cd07099 155 SEVTPLVGELLAEAWAA-AGPPQGVLQVVTGDGATGAALI--DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 265 AFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRV 344
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 345 QSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATV 424
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGG--GPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 425 YGADADRAAGVASRLRAGTVNVNGGVWYSA--DVPFGGYKQSGNGREMGVAGFEEYLETKAIAT 486
Cdd:cd07099 390 FSRDLARAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
70-484 |
3.26e-104 |
|
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: 317.86 E-value: 3.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRMlTAGAQLEGPIDDLRFAADTAEGYswTQDlghaTPLGIPTRRSVVR-E 148
Cdd:cd07100 23 RAALLRKLADLLRERKDELARLITLEMGKPIA-EARAEVEKCAWICRYYAENAEAF--LAD----EPIETDAGKAYVRyE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 149 AVGVVGAITPWNFPH-QInlAK-LGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGV-INIVTSTDHTlgAMLA 225
Cdd:cd07100 96 PLGVVLGIMPWNFPFwQV--FRfAAPNLMAGNTVLLKHASNVPGCALAIEELFRE-AGFPEGVfQNLLIDSDQV--EAII 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 226 KDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRAR 305
Cdd:cd07100 171 ADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 306 YDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPaeQAAGFFIEPTVIAGLTNE 385
Cdd:cd07100 251 YDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP--DGPGAFYPPTVLTDVTPG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 386 ARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSG 465
Cdd:cd07100 329 MPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRSG 408
|
410
....*....|....*....
gi 1231751504 466 NGREMGVAGFEEYLETKAI 484
Cdd:cd07100 409 YGRELGRFGIREFVNIKTV 427
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-485 |
9.86e-102 |
|
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: 312.36 E-value: 9.86e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 25 FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWStNTGLRVRC--VRQLRDVLREHLEELRELTISEVGAPrML 102
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MS-NLPAYKRYkiLMKVAELIERRKEELAKLLTIEVGKP-IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 103 TAGAQLEGPIDDLRFAADTA---EGYSWTQDLGHATPLGIPTrrsVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNT 179
Cdd:cd07145 77 QSRVEVERTIRLFKLAAEEAkvlRGETIPVDAYEYNERRIAF---TVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 180 VVLKPAPDTPWVAAVIGELIaEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLE 259
Cdd:cd07145 154 VVVKPSSNTPLTAIELAKIL-EEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 260 LGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISAR 339
Cdd:cd07145 233 LGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 340 QRDRVQSYLDLALAEGGTFACGGGRPaeqaAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYG 419
Cdd:cd07145 313 AVERMENLVNDAVEKGGKILYGGKRD----EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231751504 420 LSATVYGADADRAAGVASRLRAGTVNVNGGVWYSAD-VPFGGYKQSGNGREMGVAGFEEYLETKAIA 485
Cdd:cd07145 389 LQASVFTNDINRALKVARELEAGGVVINDSTRFRWDnLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
9-487 |
1.26e-101 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 313.68 E-value: 1.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 9 SRLLIDGKLASGGAG-GFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGL-RVRCVRQLRDVLREHLE 86
Cdd:PLN02766 21 TKLFINGEFVDAASGkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFeRGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 87 ELRELTISEVGAPRMLTAGAQLEGPIDDLRF---AADTAEGyswtQDLGHATPLGIPTrrsvVREAVGVVGAITPWNFPH 163
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAVDIPAAAGLLRYyagAADKIHG----ETLKMSRQLQGYT----LKEPIGVVGHIIPWNFPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 164 QINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELiAEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGR 243
Cdd:PLN02766 173 TMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHL-AKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 244 SVM-ADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKP 322
Cdd:PLN02766 252 KIMqAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 323 GDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIA 402
Cdd:PLN02766 332 GDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDK--GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 403 HDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETK 482
Cdd:PLN02766 410 FKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
....*
gi 1231751504 483 AIATA 487
Cdd:PLN02766 490 SVVTP 494
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
27-484 |
1.41e-101 |
|
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: 311.99 E-value: 1.41e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFddTDW-STNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAG 105
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWaATPARERGKLLARIADALEARSEELARLLALETGNALRTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLEGPIDDLRFAADTAegyswTQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPA 185
Cdd:cd07108 79 PEAAVLADLFRYFGGLA-----GELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 186 PDTPWVAAVIGELIAEHtdMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSA 265
Cdd:cd07108 154 EDAPLAVLLLAEILAQV--LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 266 FVVLDDADL--AAACSVAGFSVcVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDR 343
Cdd:cd07108 232 MIVFPDADLddAVDGAIAGMRF-TRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 344 VQSYLDLALAE-GGTFACGGGRPAEQ--AAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGL 420
Cdd:cd07108 311 VCGYIDLGLSTsGATVLRGGPLPGEGplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231751504 421 SATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAG-FEEYLETKAI 484
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
11-484 |
6.89e-100 |
|
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: 308.23 E-value: 6.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNT-GLRVRCVRQLRDVLREHLEEL 88
Cdd:cd07117 3 LFINGEWVKGSSGEtIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTvAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGyswtqDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLA 168
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRA-----EEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 169 KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHtdMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMAD 248
Cdd:cd07117 156 KLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV--LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 249 AAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKP 328
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 329 GTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQ--AAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGD 406
Cdd:cd07117 314 DTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231751504 407 DDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07117 394 DEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
28-482 |
1.55e-99 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 306.66 E-value: 1.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFddTDWSTNTGL-RVRCVRQLRDVLREHLEELRELTISEVGAP------R 100
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAF--KTWRATTAKeRSSLLRKWYNLMMENKDDLARLITLENGKPlkeakgE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 101 MLTAGAQLEGpiddlrFAADTAEGYswtqdlGHATPLGIPTRRSVV-REAVGVVGAITPWNFPHQINLAKLGPALAAGNT 179
Cdd:TIGR01780 80 ILYAASFLEW------FAEEAKRVY------GDTIPSPQSDKRLIViKQPVGVCAAITPWNFPAAMITRKAGAALAAGCT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 180 VVLKPAPDTPWVAAVIGELiAEHTDMPPGVINIVTSTD-HTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFL 258
Cdd:TIGR01780 148 VVVKPAEQTPLSALALARL-AEQAGIPKGVLNVITGSRaKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 259 ELGGKSAFVVLDDADLAAAcsVAGFSVCV--HAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVI 336
Cdd:TIGR01780 227 ELGGNAPFIVFDDADLDQA--VEGAMASKfrNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 337 SARQRDRVQSYLDLALAEGGTFACGGGRpaEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDS 416
Cdd:TIGR01780 305 NEKAVEKVEKHIADAVEKGAKVVTGGKR--HELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDT 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231751504 417 PYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETK 482
Cdd:TIGR01780 383 EVGLAAYFFSRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
9-487 |
1.05e-98 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 307.12 E-value: 1.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 9 SRLLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGL-RVRCVRQLRDVLREHLE 86
Cdd:PLN02466 58 TQLLINGQFVDAASGKtFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYeRSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 87 ELRELTISEVGAPRMLTAGAQLEGPIDDLRFAAdtaegySWTQDL-GHATPLGIPTRRSVVREAVGVVGAITPWNFPHQI 165
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAKAELPMFARLFRYYA------GWADKIhGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLM 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 166 NLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSV 245
Cdd:PLN02466 212 FAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHE-AGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 246 MADAA-ATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGD 324
Cdd:PLN02466 291 LELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 325 PTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHD 404
Cdd:PLN02466 371 PFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSK--GYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 405 GDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
...
gi 1231751504 485 ATA 487
Cdd:PLN02466 529 VTP 531
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-479 |
2.09e-97 |
|
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: 302.99 E-value: 2.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKlASGGAGGFATVNPA-TEEVLGEAANADAADMDRAIDAARRAFD---DTDWSTntglRVRCVRQLRDVLREHLE 86
Cdd:cd07124 35 LVIGGK-EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPtwrRTPPEE----RARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 87 ELRELTISEVGAPRMlTAGAQLEGPIDDLRFAADTAEGYswtQDLGHATPLGIPTRrsVVREAVGVVGAITPWNFPHQIN 166
Cdd:cd07124 110 ELAAWMVLEVGKNWA-EADADVAEAIDFLEYYAREMLRL---RGFPVEMVPGEDNR--YVYRPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 167 LAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVM 246
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEE-AGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 247 ADAAAT------IKKVFLELGGKSAFVVLDDADLAAAC-----SVAGFSvcvhaGQGCAITTRLVVPRARYDEAVAIAAG 315
Cdd:cd07124 263 ERAAKVqpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAegivrSAFGFQ-----GQKCSACSRVIVHESVYDEFLERLVE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 316 TMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGgTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVAREEIFG 395
Cdd:cd07124 338 RTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 396 PVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVwYSADV---PFGGYKQSGNGremGV 472
Cdd:cd07124 417 PVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKI-TGALVgrqPFGGFKMSGTG---SK 492
|
....*..
gi 1231751504 473 AGFEEYL 479
Cdd:cd07124 493 AGGPDYL 499
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
81-484 |
2.56e-95 |
|
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: 295.66 E-value: 2.56e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 81 LREHLEELRELTISEVGAPrMLTAGAQLEGPIDDLRFAADTAEGYSWTQDLGHATPLGIPTRRSVVREAVGVVGAITPWN 160
Cdd:cd07149 56 LEERREEFARTIALEAGKP-IKDARKEVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIREPIGVVAAITPFN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 161 FPhqINLA--KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGS 238
Cdd:cd07149 135 FP--LNLVahKVGPAIAAGNAVVLKPASQTPLSALKLAELLLE-AGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 239 TATGRSVMAdaAATIKKVFLELGGKSAFVVLDDADL---AAACSVAGFSvcvHAGQGCAITTRLVVPRARYDEAVAIAAG 315
Cdd:cd07149 212 PAVGEAIAR--KAGLKKVTLELGSNAAVIVDADADLekaVERCVSGAFA---NAGQVCISVQRIFVHEDIYDEFLERFVA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 316 TMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRpaeqaAGFFIEPTVIAGLTNEARVAREEIFG 395
Cdd:cd07149 287 ATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKR-----DGAILEPTVLTDVPPDMKVVCEEVFA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 396 PVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADV-PFGGYKQSGNGREmGVA- 473
Cdd:cd07149 362 PVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGRE-GPRy 440
|
410
....*....|.
gi 1231751504 474 GFEEYLETKAI 484
Cdd:cd07149 441 AIEEMTEIKLV 451
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
9-484 |
6.42e-95 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 296.04 E-value: 6.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 9 SRLLIDGKLASGGAGG-FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWSTNTGLRVRCV-RQLRDVLREHLE 86
Cdd:PRK09847 20 NRLFINGEYTAAAENEtFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVlNKLADLMEAHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 87 ELRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEgyswtQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQIN 166
Cdd:PRK09847 100 ELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAID-----KVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 167 LAKLGPALAAGNTVVLKPAPDTPWVAAVIGELiAEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVM 246
Cdd:PRK09847 175 CWKLGPALAAGNSVILKPSEKSPLSAIRLAGL-AKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 247 ADAA-ATIKKVFLELGGKSAFVVLDDA-DLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGD 324
Cdd:PRK09847 254 KDAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 325 PTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGggrpAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHD 404
Cdd:PRK09847 334 PLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG----RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 405 GDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
70-480 |
6.02e-91 |
|
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: 284.19 E-value: 6.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRMlTAGAQLEGPIDDLRFAADTAegyswTQDLGHATPLGiPTRRSVVRE- 148
Cdd:cd07152 37 RAAVLRRAADLLEEHADEIADWIVRESGSIRP-KAGFEVGAAIGELHEAAGLP-----TQPQGEILPSA-PGRLSLARRv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 149 AVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDMPPGVINIVTStDHTLGAMLAKDP 228
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 229 RVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDE 308
Cdd:cd07152 189 NVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 309 AVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGgrpaeQAAGFFIEPTVIAGLTNEARV 388
Cdd:cd07152 269 YTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGG-----TYDGLFYRPTVLSGVKPGMPA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 389 AREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGG-VWYSADVPFGGYKQSGNG 467
Cdd:cd07152 344 FDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQtVNDEPHNPFGGMGASGNG 423
|
410
....*....|....
gi 1231751504 468 -REMGVAGFEEYLE 480
Cdd:cd07152 424 sRFGGPANWEEFTQ 437
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
62-484 |
5.59e-90 |
|
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: 281.39 E-value: 5.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 62 DWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRmLTAGAQLEGPIDDLRFAADTAegyswTQDLGHATPLGIP 140
Cdd:cd07105 15 AWSkTPPSERRDILLKAADLLESRRDEFIEAMMEETGATA-AWAGFNVDLAAGMLREAASLI-----TQIIGGSIPSDKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 141 TRRS-VVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTS---- 215
Cdd:cd07105 89 GTLAmVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHE-AGLPKGVLNVVTHsped 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 216 TDHTLGAMLAKdPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAI 295
Cdd:cd07105 168 APEVVEALIAH-PAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 296 TTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKpgtvcGPVISARQRDRVQSYLDLALAEGGTFACGGgRPAEQAAGFFIE 375
Cdd:cd07105 247 TERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGG-LADESPSGTSMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 376 PTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGG-VWYSA 454
Cdd:cd07105 321 PTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMtVHDEP 400
|
410 420 430
....*....|....*....|....*....|
gi 1231751504 455 DVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07105 401 TLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
70-482 |
1.76e-89 |
|
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: 280.67 E-value: 1.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRMLtAGAQLEGPIDDLRFAADTAegyswTQDLGHATPLGIPTRRS----- 144
Cdd:cd07147 45 RAAILLHCVARLEERFEELAETIVLEAGKPIKD-ARGEVARAIDTFRIAAEEA-----TRIYGEVLPLDISARGEgrqgl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 145 VVREAVGVVGAITPWNFPhqINLA--KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTsTDHTLGA 222
Cdd:cd07147 119 VRRFPIGPVSAITPFNFP--LNLVahKVAPAIAAGCPFVLKPASRTPLSALILGEVLAE-TGLPKGAFSVLP-CSRDDAD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 223 MLAKDPRVDMVSFTGSTATGRSVMADAAAtiKKVFLELGGKSAFVVLDDADLAAA---CSVAGFSvcvHAGQGCAITTRL 299
Cdd:cd07147 195 LLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDSDADLDFAaqrIIFGAFY---QAGQSCISVQRV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 300 VVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRpaeqaAGFFIEPTVI 379
Cdd:cd07147 270 LVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR-----DGALLEPTIL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 380 AGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSAD-VPF 458
Cdd:cd07147 345 EDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVDhMPY 424
|
410 420
....*....|....*....|....
gi 1231751504 459 GGYKQSGNGREMGVAGFEEYLETK 482
Cdd:cd07147 425 GGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
10-484 |
1.32e-88 |
|
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: 279.38 E-value: 1.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 10 RLLIDGKLASGGAG-GFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDWST-NTGLRVRCVRQLRDVLREHLEE 87
Cdd:cd07140 7 QLFINGEFVDAEGGkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKmNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 88 LRELTISEVGAPRMLTAGAQLEGPIDDLRFAAdtaegySWTQDLGHATplgIPTRRS--------VVREAVGVVGAITPW 159
Cdd:cd07140 87 LATIESLDSGAVYTLALKTHVGMSIQTFRYFA------GWCDKIQGKT---IPINQArpnrnltlTKREPIGVCGIVIPW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 160 NFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGST 239
Cdd:cd07140 158 NYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVK-AGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGST 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 240 ATGRSVMADAA-ATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMG 318
Cdd:cd07140 237 PIGKHIMKSCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 319 SIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPaeQAAGFFIEPTVIAGLTNEARVAREEIFGPVL 398
Cdd:cd07140 317 KMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQV--DRPGFFFEPTVFTDVEDHMFIAKEESFGPIM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 399 TVIA-HDGDDDAV-RIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNggVWYSADV--PFGGYKQSGNGREMGVAG 474
Cdd:cd07140 395 IISKfDDGDVDGVlQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDVaaPFGGFKQSGFGKDLGEEA 472
|
490
....*....|
gi 1231751504 475 FEEYLETKAI 484
Cdd:cd07140 473 LNEYLKTKTV 482
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
15-486 |
8.99e-88 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 278.30 E-value: 8.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 15 GKLASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAfdDTDWS-TNTGLRVRCVRQLRDVLREHLEELRELTI 93
Cdd:PRK09407 24 ARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAaTPVRERAAVLLRFHDLVLENREELLDLVQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 94 SEVGAPRmltAGAQLEgpIDDL----RFAADTAEGYSWTQDLGHATPLgiPTRRSVVREAVGVVGAITPWNFPHQINLAK 169
Cdd:PRK09407 102 LETGKAR---RHAFEE--VLDValtaRYYARRAPKLLAPRRRAGALPV--LTKTTELRQPKGVVGVISPWNYPLTLAVSD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 170 LGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAkdPRVDMVSFTGSTATGRSVMADA 249
Cdd:PRK09407 175 AIPALLAGNAVVLKPDSQTPLTALAAVELLYE-AGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 250 AATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPG 329
Cdd:PRK09407 252 GRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 330 TVCGPVISARQRDRVQSYLDLALAEGGTFACGGgRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDA 409
Cdd:PRK09407 332 ADMGSLISEAQLETVSAHVDDAVAKGATVLAGG-KARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 410 VRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGG---VWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAIAT 486
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyaaAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIAT 490
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
70-484 |
9.51e-88 |
|
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: 276.24 E-value: 9.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRMlTAGAQLEGPIDDLRFAADTAEgyswtQDLGHATPLGIPTRRS----- 144
Cdd:cd07094 45 RMAILERAADLLKKRAEEFAKIIACEGGKPIK-DARVEVDRAIDTLRLAAEEAE-----RIRGEEIPLDATQGSDnrlaw 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 145 VVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAML 224
Cdd:cd07094 119 TIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVE-AGVPEGVLQVVTGEREVLGDAF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 225 AKDPRVDMVSFTGSTATGRSVMADAAatIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRA 304
Cdd:cd07094 198 AADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 305 RYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRpaeqaAGFFIEPTVIAGLTN 384
Cdd:cd07094 276 LYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGER-----DGALFKPTVLEDVPR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 385 EARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSAD-VPFGGYKQ 463
Cdd:cd07094 351 DTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKE 430
|
410 420
....*....|....*....|.
gi 1231751504 464 SGNGREMGVAGFEEYLETKAI 484
Cdd:cd07094 431 SGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-484 |
4.14e-87 |
|
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: 274.51 E-value: 4.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTnTGL--RVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAG 105
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRA-VPLeeRKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 aQLEGPIDDLRFAADTAEGYSWTQDLGHATPLgiptRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPA 185
Cdd:cd07102 78 -EIRGMLERARYMISIAEEALADIRVPEKDGF----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 186 PDTPWVAAVIGELIAEhTDMPPGVINIVTStDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSA 265
Cdd:cd07102 153 PQTPLCGERFAAAFAE-AGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 266 FVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQ 345
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 346 SYLDLALAEGGTFACGGGR-PAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATV 424
Cdd:cd07102 311 AQIADAIAKGARALIDGALfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 425 YGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
30-486 |
4.92e-86 |
|
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: 271.88 E-value: 4.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 30 PATEEVLGEAANADAADMDRAIDAARRAfdDTDWSTNT-GLRVRCVRQLRDVLREHLEELRELTISEVGAPRmltAGAQL 108
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPfAERAAVFLRFHDLVLERRDELLDLIQLETGKAR---RHAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 109 EgpIDDL----RFAADTAEGYSWTQDlgHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKP 184
Cdd:cd07101 78 E--VLDVaivaRYYARRAERLLKPRR--RRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 185 APDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKdpRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKS 264
Cdd:cd07101 154 DSQTALTALWAVELLIE-AGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 265 AFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRV 344
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 345 QSYLDLALAEGGTFACGGgRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATV 424
Cdd:cd07101 311 TAHVDDAVAKGATVLAGG-RARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231751504 425 YGADADRAAGVASRLRAGTVNVNGG---VWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAIAT 486
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNEGyaaAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
10-482 |
7.20e-85 |
|
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: 269.65 E-value: 7.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 10 RLLIDGK-LASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWSTNTG-LRVRCVRQLRDVLREHLEE 87
Cdd:cd07111 23 GHFINGKwVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGhVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 88 LRELTISEVGAPRMLTAGAQLEGPIDDLRFAAdtaegySWTQDLGHATPlgiptrrsvVREAVGVVGAITPWNFPHQINL 167
Cdd:cd07111 101 FAVLESLDNGKPIRESRDCDIPLVARHFYHHA------GWAQLLDTELA---------GWKPVGVVGQIVPWNFPLLMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 168 AKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTlGAMLAKDPRVDMVSFTGSTATGRSVMA 247
Cdd:cd07111 166 WKICPALAMGNTVVLKPAEYTPLTALLFAEICAE-AGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 248 DAAATIKKVFLELGGKSAFVVLDDADLAAAcsVAGF--SVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDP 325
Cdd:cd07111 244 ATAGTGKKLSLELGGKSPFIVFDDADLDSA--VEGIvdAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 326 TKPGTVCGPVISARQRDRVQSYLDLALAEGG-TFACGGGRPAEqaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHD 404
Cdd:cd07111 322 LDKAIDMGAIVDPAQLKRIRELVEEGRAEGAdVFQPGADLPSK---GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFR 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231751504 405 GDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETK 482
Cdd:cd07111 399 TAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
12-482 |
1.34e-83 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 266.39 E-value: 1.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 12 LIDGK-LASGGAGGFATVNPATEEVLGeaanadaADMDRAIDAARRAFDDTD-----WSTNTGL-RVRCVRQLRDVLREH 84
Cdd:PRK11241 14 LINGEwLDANNGEVIDVTNPANGDKLG-------SVPKMGADETRAAIDAANralpaWRALTAKeRANILRRWFNLMMEH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 85 LEELRELTISEVGAPRmltagAQLEGPIDdlrFAADTAEGYS--WTQDLGHATPLGIPTRR-SVVREAVGVVGAITPWNF 161
Cdd:PRK11241 87 QDDLARLMTLEQGKPL-----AEAKGEIS---YAASFIEWFAeeGKRIYGDTIPGHQADKRlIVIKQPIGVTAAITPWNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 162 PHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELiAEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTAT 241
Cdd:PRK11241 159 PAAMITRKAGPALAAGCTMVLKPASQTPFSALALAEL-AIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 242 GRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIK 321
Cdd:PRK11241 238 GRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 322 PGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACgGGRPAEQAAGFFiEPTVIAGLTNEARVAREEIFGPVLTVI 401
Cdd:PRK11241 318 IGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVC-GGKAHELGGNFF-QPTILVDVPANAKVAKEETFGPLAPLF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 402 AHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLET 481
Cdd:PRK11241 396 RFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEI 475
|
.
gi 1231751504 482 K 482
Cdd:PRK11241 476 K 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
75-484 |
2.63e-82 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 260.82 E-value: 2.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 75 RQLRDVLREHLEELRELTISEVGAPRMLtAGAQLEGPIDDLRFAADTAEGYSwtqdlGHAtplgIPTRRS-----VVREA 149
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQL-AEVEVAFTADYIDYMAEWARRYE-----GEI----IQSDRPgenilLFKRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 150 VGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPR 229
Cdd:PRK10090 72 LGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDE-IGLPKGVFNLVLGRGETVGQELAGNPK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 230 VDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEA 309
Cdd:PRK10090 151 VAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 310 VAIAAGTMGSIKPGDPTKPGTV-CGPVISARQRDRVQSYLDLALAEGGTFACGGGRpaEQAAGFFIEPTVIAGLTNEARV 388
Cdd:PRK10090 231 VNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKA--VEGKGYYYPPTLLLDVRQEMSI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 389 AREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGR 468
Cdd:PRK10090 309 MHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGG 388
|
410
....*....|....*.
gi 1231751504 469 EMGVAGFEEYLETKAI 484
Cdd:PRK10090 389 ADGKHGLHEYLQTQVV 404
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-486 |
6.67e-81 |
|
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: 258.77 E-value: 6.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 28 VNPATEEVLGEAANADAADMDRAIDAARRAFddTDWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMltaGA 106
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQ--REWAkTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMV---DA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 107 QLeGPIddlrfaADTAEGYSWTQDLGH--------ATPLGIPTRRSVVR-EAVGVVGAITPWNFP-HQInlakLGPALAA 176
Cdd:cd07098 76 SL-GEI------LVTCEKIRWTLKHGEkalrpesrPGGLLMFYKRARVEyEPLGVVGAIVSWNYPfHNL----LGPIIAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 177 ---GNTVVLKPAPDTPWVAAVIGELIAE---HTDMPPGVINIVTSTDHTlGAMLAKDPRVDMVSFTGSTATGRSVMADAA 250
Cdd:cd07098 145 lfaGNAIVVKVSEQVAWSSGFFLSIIREclaACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 251 ATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGT 330
Cdd:cd07098 224 ESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 331 VCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPA--EQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDD 408
Cdd:cd07098 304 DVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPhpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 409 AVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVN--GGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAIAT 486
Cdd:cd07098 384 AVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
70-472 |
1.98e-80 |
|
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: 257.29 E-value: 1.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAgAQLEGPIDDLRFAADTA---EGYSWTQDLghaTPLGIPTRRSVV 146
Cdd:cd07146 42 RSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVGRAADVLRFAAAEAlrdDGESFSCDL---TANGKARKIFTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 147 REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAK 226
Cdd:cd07146 118 REPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYE-AGLPPDMLSVVTGEPGEIGDELIT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 227 DPRVDMVSFTGSTATGRSVMAdaAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARY 306
Cdd:cd07146 197 HPDVDLVTFTGGVAVGKAIAA--TAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 307 DEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRpaeqaAGFFIEPTVIAGLTNEA 386
Cdd:cd07146 275 DEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR-----QGALYAPTVLDHVPPDA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 387 RVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWY-SADVPFGGYKQSG 465
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFrSELSPFGGVKDSG 429
|
....*..
gi 1231751504 466 NGREMGV 472
Cdd:cd07146 430 LGGKEGV 436
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
70-469 |
6.76e-79 |
|
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: 253.65 E-value: 6.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRmltAGAQLE--GPIDDLRFAADTAEGYSWTQDLGHATPLGIPTRRSVVR 147
Cdd:cd07082 63 RIDCLHKFADLLKENKEEVANLLMWEIGKTL---KDALKEvdRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 148 EAVGVVGAITPWNFPhqINLA--KLGPALAAGNTVVLKPAPDTPWVAAVIGELiAEHTDMPPGVINIVTSTDHTLGAMLA 225
Cdd:cd07082 140 EPLGVVLAIGPFNYP--LNLTvsKLIPALIMGNTVVFKPATQGVLLGIPLAEA-FHDAGFPKGVVNVVTGRGREIGDPLV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 226 KDPRVDMVSFTGSTATGRSVMAdaAATIKKVFLELGGKSAFVVLDDADL--AAACSVAG-FSvcvHAGQGCAITTRLVVP 302
Cdd:cd07082 217 THGRIDVISFTGSTEVGNRLKK--QHPMKRLVLELGGKDPAIVLPDADLelAAKEIVKGaLS---YSGQRCTAIKRVLVH 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 303 RARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRpaeqAAGFFIEPTVIAGL 382
Cdd:cd07082 292 ESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR----EGGNLIYPTLLDPV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 383 TNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADV-PFGGY 461
Cdd:cd07082 368 TPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGR 447
|
....*...
gi 1231751504 462 KQSGNGRE 469
Cdd:cd07082 448 KDSGIGTQ 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
25-482 |
3.89e-78 |
|
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: 251.99 E-value: 3.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 25 FATVNPATEEVLGEAANADAADMDRAIDAARRAFDDtdWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMLT 103
Cdd:cd07116 18 FDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGkTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRET 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 104 AGAQLEGPIDDLRFAADTAEGYSwtqdlGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 183
Cdd:cd07116 96 LAADIPLAIDHFRYFAGCIRAQE-----GSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 184 PAPDTPWVAAVIGELIAEHtdMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGK 263
Cdd:cd07116 171 PAEQTPASILVLMELIGDL--LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 264 SAFV----VLDDADLAAACSVAGFSV-CVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISA 338
Cdd:cd07116 249 SPNIffadVMDADDAFFDKALEGFVMfALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 339 RQRDRVQSYLDLALAEGGTFACGGGRP--AEQAAGFFIEPTVIAGlTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDS 416
Cdd:cd07116 329 EQLEKILSYIDIGKEEGAEVLTGGERNelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDT 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231751504 417 PYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETK 482
Cdd:cd07116 408 LYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
26-484 |
1.42e-74 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 241.95 E-value: 1.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 26 ATVNPATEEVLGEAANADAADMDRAIDAARRAFDDTDwSTNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPrMLTAG 105
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRDYR-TTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLEGPIDDLRFAADTAEGYSWTQDlghATPLGIPTRRSVVR-EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKP 184
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADEP---ADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 185 APDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLaKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKS 264
Cdd:PRK09406 159 ASNVPQTALYLADLFRR-AGFPDGCFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 265 AFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRV 344
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 345 QSYLDLALAEGGTFACGGGRPAeqAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATV 424
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPD--GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 425 YGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
11-485 |
1.85e-72 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 238.30 E-value: 1.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKLASGgAGGFATVNPA-TEEVLGEAANADAADMDRAIDAARRAFDDtdWS-TNTGLRVRCVRQLRDVLREHLEEL 88
Cdd:PRK03137 39 LIIGGERITT-EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET--WKkWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPRMLTAGAQLEGpIDDLRFAA----DTAEGYSWTQDLG-----HATPLGiptrrsvvreaVGVVgaITPW 159
Cdd:PRK03137 116 SAWLVKEAGKPWAEADADTAEA-IDFLEYYArqmlKLADGKPVESRPGehnryFYIPLG-----------VGVV--ISPW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 160 NFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIaEHTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGST 239
Cdd:PRK03137 182 NFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVL-EEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 240 ATGRSVMADAAAT------IKKVFLELGGKSAFVVLDDADL-AAACSVA----GFSvcvhaGQGCAITTRLVVPRARYDE 308
Cdd:PRK03137 261 EVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLdLAAESIVasafGFS-----GQKCSACSRAIVHEDVYDE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 309 AVAIAAGTMGSIKPGDPTKPGTVcGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEqaaGFFIEPTVIAGLTNEARV 388
Cdd:PRK03137 336 VLEKVVELTKELTVGNPEDNAYM-GPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSK---GYFIQPTIFADVDPKARI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 389 AREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVwYSADV---PFGGYKQSG 465
Cdd:PRK03137 412 MQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGC-TGAIVgyhPFGGFNMSG 490
|
490 500
....*....|....*....|....
gi 1231751504 466 NGREmgvAGFEEYL----ETKAIA 485
Cdd:PRK03137 491 TDSK---AGGPDYLllflQAKTVS 511
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
10-484 |
6.93e-72 |
|
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: 235.49 E-value: 6.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 10 RLLIDGKLASGGAGGFATV-NPATEEVLGEAANADAADMDRAIDAARRAFDDtdWS-TNTGLRVRCVRQLRDVLREHLEE 87
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVyNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSaTPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 88 LRELTISEVGAPRMLTAGAQLEGpIDDLRFAADTAegyswTQDLGHATP---LGIPTRrsVVREAVGVVGAITPWNFPHQ 164
Cdd:cd07085 80 LARLITLEHGKTLADARGDVLRG-LEVVEFACSIP-----HLLKGEYLEnvaRGIDTY--SYRQPLGVVAGITPFNFPAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 165 INLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAkDPRVDMVSFTGSTATGRS 244
Cdd:cd07085 152 IPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQE-AGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 245 VMADAAATIKKVFLELGGKSAFVVLDDADL-AAACSVAGfSVCVHAGQGC-AITTRLVVPRArYDEAVAIAAGTMGSIKP 322
Cdd:cd07085 230 IYERAAANGKRVQALGGAKNHAVVMPDADLeQTANALVG-AAFGAAGQRCmALSVAVAVGDE-ADEWIPKLVERAKKLKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 323 GDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGG--GRPAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTV 400
Cdd:cd07085 308 GAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 401 IAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGV-----WYSadvpFGGYKQS--GNGREMGVA 473
Cdd:cd07085 388 VRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpvplaFFS----FGGWKGSffGDLHFYGKD 463
|
490
....*....|.
gi 1231751504 474 GFEEYLETKAI 484
Cdd:cd07085 464 GVRFYTQTKTV 474
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
11-479 |
1.87e-70 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 232.83 E-value: 1.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKLASGgAGGFATVNPA-TEEVLGEAANADAADMDRAIDAARRAFDDtdWS-TNTGLRVRCVRQLRDVLREHLEEL 88
Cdd:TIGR01237 35 LVINGERVET-ENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA--WKkTDPEERAAILFKAAAIVRRRRHEF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPrMLTAGAQLEGPIDDLRFAADTAEGYSwtqdlGHATPLGIPTRRS-VVREAVGVVGAITPWNFPHQINL 167
Cdd:TIGR01237 112 SALLVKEVGKP-WNEADAEVAEAIDFMEYYARQMIELA-----KGKPVNSREGETNqYVYTPTGVTVVISPWNFPFAIMV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 168 AKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMA 247
Cdd:TIGR01237 186 GMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEE-AGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 248 DAAAT------IKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIK 321
Cdd:TIGR01237 265 RAAKVqpgqkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 322 PGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEqaaGFFIEPTVIAGLTNEARVAREEIFGPVLTVI 401
Cdd:TIGR01237 345 VGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSK---GYFIGPTIFADVDRKARLAQEEIFGPVVAFI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 402 AHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVwYSADV---PFGGYKQSGNGREmgvAGFEEY 478
Cdd:TIGR01237 422 RASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNI-TGAIVgyqPFGGFKMSGTDSK---AGGPDY 497
|
.
gi 1231751504 479 L 479
Cdd:TIGR01237 498 L 498
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
20-471 |
8.06e-70 |
|
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: 230.17 E-value: 8.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 20 GGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFddTDWSTNTG-LRVRCVRQLRDVLREHLEELRELTISEVGa 98
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAF--KEWRDVPApKRGEIVRQIGDALRKKKEALGKLVSLEMG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 99 pRMLTAGaqlEGPIDDLRFAADTAEGYSWTqdLGHATplgIPTRRS--VVREA---VGVVGAITPWNFP---HQINLAKl 170
Cdd:cd07130 86 -KILPEG---LGEVQEMIDICDFAVGLSRQ--LYGLT---IPSERPghRMMEQwnpLGVVGVITAFNFPvavWGWNAAI- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 171 gpALAAGNTVVLKPAPDTPWVAAVIGELIA---EHTDMPPGVINIVTStDHTLGAMLAKDPRVDMVSFTGSTATGRSVMA 247
Cdd:cd07130 156 --ALVCGNVVVWKPSPTTPLTAIAVTKIVArvlEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 248 DAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTK 327
Cdd:cd07130 233 AVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 328 PGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRpaEQAAGFFIEPTVIAGLtNEARVAREEIFGPVLTVIAHDGDD 407
Cdd:cd07130 313 DGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKV--IDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 408 DAVRIANDSPYGLSATVYGADADRAAGVASRLRA--GTVNVN--------GGVwysadvpFGGYKQSGNGREMG 471
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNigtsgaeiGGA-------FGGEKETGGGRESG 456
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
70-477 |
1.32e-67 |
|
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: 223.13 E-value: 1.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRElTISE--VGAPRMLTAGAQLEGPIDDLRFAADTAEGysWTQD-LGHATPLGIPTRRSVV 146
Cdd:cd07133 22 RRDRLDRLKALLLDNQDALAE-AISAdfGHRSRHETLLAEILPSIAGIKHARKHLKK--WMKPsRRHVGLLFLPAKAEVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 147 REAVGVVGAITPWNFPhqINLAkLGP---ALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDmpPGVINIVTStDHTLGAM 223
Cdd:cd07133 99 YQPLGVVGIIVPWNYP--LYLA-LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFD--EDEVAVVTG-GADVAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 224 LAKDPrVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPR 303
Cdd:cd07133 173 FSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 304 ARYDEAVAIAAGTMGSIKPGDPTKPGtvCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAAGFFIEPTVIAGLT 383
Cdd:cd07133 252 DKLEEFVAAAKAAVAKMYPTLADNPD--YTSIINERHYARLQGLLEDARAKGARVIELNPAGEDFAATRKLPPTLVLNVT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 384 NEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSA--DVPFGGY 461
Cdd:cd07133 330 DDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAqdDLPFGGV 409
|
410
....*....|....*.
gi 1231751504 462 KQSGNGREMGVAGFEE 477
Cdd:cd07133 410 GASGMGAYHGKEGFLT 425
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
75-484 |
1.14e-65 |
|
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: 218.25 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 75 RQLRDVLREHLEELRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEgySWTQDLGHATPLGIPTRRSVVR-EAVGVV 153
Cdd:cd07134 27 KRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLK--KWMKPKRVRTPLLLFGTKSKIRyEPKGVC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 154 GAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhtDMPPGVINIVTSTDHTLGAMLAKdpRVDMV 233
Cdd:cd07134 105 LIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIRE--AFDEDEVAVFEGDAEVAQALLEL--PFDHI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 234 SFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLA-AACSVAgFSVCVHAGQGCAITTRLVVPRARYDEAVAI 312
Cdd:cd07134 181 FFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKkAAKKIA-WGKFLNAGQTCIAPDYVFVHESVKDAFVEH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 313 AAGTMGSI-KPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAagfFIEPTVIAGLTNEARVARE 391
Cdd:cd07134 260 LKAEIEKFyGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR---YIAPTVLTNVTPDMKIMQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 392 EIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADV--PFGGYKQSGNGRE 469
Cdd:cd07134 337 EIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPnlPFGGVNNSGIGSY 416
|
410
....*....|....*
gi 1231751504 470 MGVAGFEEYLETKAI 484
Cdd:cd07134 417 HGVYGFKAFSHERAV 431
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-478 |
1.90e-65 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 218.58 E-value: 1.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 27 TVNPATEEVLGEAANADAADMDRAIDAARRAFddTDWS-TNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPrMLTAG 105
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGF--RDWReTNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP-INQAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 106 AQLegpiddlrfaADTAEGYSWTQDLGHATPLGIPT----RRSVVR-EAVGVVGAITPWNFPHQINLAKLGPALAAGNTV 180
Cdd:PRK13968 88 AEV----------AKSANLCDWYAEHGPAMLKAEPTlvenQQAVIEyRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 181 VLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLaKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLEL 260
Cdd:PRK13968 158 LLKHAPNVMGCAQLIAQVFKD-AGIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 261 GGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQ 340
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 341 RDRVQSYLDLALAEGGTFACGGGRPAeqAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGL 420
Cdd:PRK13968 316 RDELHHQVEATLAEGARLLLGGEKIA--GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1231751504 421 SATVYGADADRAAGVASRLRAGTVNVNGGVWYSADVPFGGYKQSGNGREMGVAGFEEY 478
Cdd:PRK13968 394 SATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-484 |
2.50e-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: 211.62 E-value: 2.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEgySWTQDLGHATPLGI-PTRRSVVRE 148
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLK--KWMKPRRVSVPLLLqPAKAYVIPE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 149 AVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHtdMPPGVINIVTSTDHTLGAMLAKdp 228
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY--FDPEAVAVVEGGVEVATALLAE-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 229 RVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDE 308
Cdd:cd07087 176 PFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 309 AVAIAAGTMGSIKPGDPTKPGTVcGPVISARQRDRVQSYLDlalaeGGTFACGGGRpaeQAAGFFIEPTVIAGLTNEARV 388
Cdd:cd07087 256 LIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLLD-----DGKVVIGGQV---DKEERYIAPTILDDVSPDSPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 389 AREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSA--DVPFGGYKQSGN 466
Cdd:cd07087 327 MQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAipNLPFGGVGNSGM 406
|
410
....*....|....*...
gi 1231751504 467 GREMGVAGFEEYLETKAI 484
Cdd:cd07087 407 GAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
70-485 |
1.08e-61 |
|
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: 209.36 E-value: 1.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELrELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEGYSWTQDLGHATPlgiPTRRSVVREA 149
Cdd:cd07083 79 RARLLLKAADLLRRRRREL-IATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYP---GEDNESFYVG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 150 VGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGElIAEHTDMPPGVINIVTSTDHTLGAMLAKDPR 229
Cdd:cd07083 155 LGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFE-IFHEAGFPPGVVQFLPGVGEEVGAYLTEHER 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 230 VDMVSFTGSTATGRSV------MADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPR 303
Cdd:cd07083 234 IRGINFTGSLETGKKIyeaaarLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQ 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 304 ARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEgGTFACGGGRPAeqAAGFFIEPTVIAGLT 383
Cdd:cd07083 314 GAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLE--GEGYFVAPTVVEEVP 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 384 NEARVAREEIFGPVLTVIAHDGDD--DAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVN----GGVwySADVP 457
Cdd:cd07083 391 PKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkitGAL--VGVQP 468
|
410 420
....*....|....*....|....*....
gi 1231751504 458 FGGYKQSGNGREMGVAGF-EEYLETKAIA 485
Cdd:cd07083 469 FGGFKLSGTNAKTGGPHYlRRFLEMKAVA 497
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
55-468 |
3.41e-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: 203.66 E-value: 3.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 55 RRAFddTDWStNTGL--RVRCVRQLRDVLREHLEELRELTISEVGAPR--MLTAGAQLEGPIDdlrFAADTAEGYSWTqd 130
Cdd:cd07095 10 RAAF--PGWA-ALSLeeRAAILRRFAELLKANKEELARLISRETGKPLweAQTEVAAMAGKID---ISIKAYHERTGE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 131 lgHATPlgIPTRRSVVR-EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGV 209
Cdd:cd07095 82 --RATP--MAQGRAVLRhRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEE-AGLPPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 210 INIVTSTDHTlGAMLAKDPRVDMVSFTGSTATGRsvmadaaaTIKKVF---------LELGGKSAFVVLDDADLAAACSV 280
Cdd:cd07095 157 LNLVQGGRET-GEALAAHEGIDGLLFTGSAATGL--------LLHRQFagrpgkilaLEMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 281 AGFSVCVHAGQGCAITTRLVVPR-ARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFA 359
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 360 cgggRPAE--QAAGFFIEPTVIAgLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVAS 437
Cdd:cd07095 308 ----LAMErlVAGTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLA 382
|
410 420 430
....*....|....*....|....*....|....*
gi 1231751504 438 RLRAGTVNVN----GGvwySADVPFGGYKQSGNGR 468
Cdd:cd07095 383 RIRAGIVNWNrpttGA---SSTAPFGGVGLSGNHR 414
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-486 |
1.44e-55 |
|
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: 191.66 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 75 RQLRDVLREHLEELRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEgySWTQDlgHATPLGIPTRRS----VVREAV 150
Cdd:cd07135 34 KQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLK--KWAKD--EKVKDGPLAFMFgkprIRKEPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 151 GVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDmpPGVINIVTSTDHTLGAMLAKdpRV 230
Cdd:cd07135 110 GVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLD--PDAFQVVQGGVPETTALLEQ--KF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 231 DMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAV 310
Cdd:cd07135 186 DKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 311 AIAAGTMGSIKPGDPTKPgTVCGPVISARQRDRVQSYLDlalAEGGTFACGGGRPAEQAagfFIEPTVIAGLTNEARVAR 390
Cdd:cd07135 266 EELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLD---TTKGKVVIGGEMDEATR---FIPPTIVSDVSWDDSLMS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 391 EEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSA--DVPFGGYKQSGNGR 468
Cdd:cd07135 339 EELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGvdNAPFGGVGDSGYGA 418
|
410
....*....|....*...
gi 1231751504 469 EMGVAGFEEYLETKAIAT 486
Cdd:cd07135 419 YHGKYGFDTFTHERTVVK 436
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
70-474 |
3.64e-55 |
|
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: 191.09 E-value: 3.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPrMLTAGAQLEGPIDDLRFAAD---TAEGYSWTQDLghaTPLGIPTRRSVV 146
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREGGKP-LVDAKVEVTRAIDGVELAADelgQLGGREIPMGL---TPASAGRIAFTT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 147 REAVGVVGAITPWNfpHQINLA--KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTsTDHTLGAML 224
Cdd:cd07148 122 REPIGVVVAISAFN--HPLNLIvhQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHE-AGLPEGWCQAVP-CENAVAEKL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 225 AKDPRVDMVSFTGSTATGRSVMADAAATiKKVFLELGGKSAFVVLDDADLAAACSV---AGFsvcVHAGQGCAITTRLVV 301
Cdd:cd07148 198 VTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPlvkGGF---YHAGQVCVSVQRVFV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 302 PRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAagffIEPTVIAG 381
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTT----YAPTVLLD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 382 LTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSAD-VPFGG 460
Cdd:cd07148 350 PPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAG 429
|
410
....*....|....
gi 1231751504 461 YKQSGngreMGVAG 474
Cdd:cd07148 430 RRQSG----YGTGG 439
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
11-468 |
4.26e-55 |
|
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 274486 Cd Length: 484 Bit Score: 191.47 E-value: 4.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKLASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFddTDWStNTGLRVRC--VRQLRDVLREHLEEL 88
Cdd:TIGR03240 1 LFIDGKWRAGQGESFASRNPATQEVLWQGAAASADQVEAAVAAARAAF--PAWA-RLSLEERIavVQRFAALLEERKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPRMLTAG--AQLEGPIDDLRFAADTAEGYSwtqdlghATPLgiPTRRSVVR-EAVGVVGAITPWNFPHQI 165
Cdd:TIGR03240 78 ARVIARETGKPLWETRTevASMIGKVAISIKAYHERTGES-------ENPM--PDGRAVLRhRPHGVVAVFGPYNFPGHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 166 NLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTlGAMLAKDPRVDMVSFTGSTATGRSV 245
Cdd:TIGR03240 149 PNGHIVPALIAGNTVVFKPSELTPWVAEETVKLWEK-AGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 246 MADAAATIKKVF-LELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPR-ARYDEAVAIAAGTMGSIKPG 323
Cdd:TIGR03240 227 HRQFGGRPEKILaLEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRLLVPDgAQGDAFLARLVEVAERLTVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 324 D-PTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAAgfFIEPTVIaGLTNEARVAREEIFGPVLTVIA 402
Cdd:TIGR03240 307 AwDAEPQPFMGAVISLRAAQRLLAAQAKLLALGGKSLLEMRQLDPGAA--FLTPGII-DVTGVAELPDEEHFGPLLQVIR 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 403 HDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVN----GGvwySADVPFGGYKQSGNGR 468
Cdd:TIGR03240 384 YTDFDEAIAIANNTRFGLSAGLLSDDRELYDRFLLEIRAGIVNWNkpltGA---SSAAPFGGIGASGNHR 450
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
10-486 |
1.77e-54 |
|
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: 189.71 E-value: 1.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 10 RLLIDGKLASGGAGGFATV-NPATEEVLGEAANADAADMDRAIDAARRAFddTDWS-TNTGLRVRCVRQLRDVLREHLEE 87
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVtNPATNEVTTKVAFASVDEVDAAVASARETF--LTWGqTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 88 LRELTISEVGAPRMLTAGAQLEGpIDDLRFAADTAegyswTQDLGHATPlGIPTRRSV--VREAVGVVGAITPWNFPHQI 165
Cdd:TIGR01722 80 IAELITAEHGKTHSDALGDVARG-LEVVEHACGVN-----SLLKGETST-QVATRVDVysIRQPLGVCAGITPFNFPAMI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 166 NLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTStDHTLGAMLAKDPRVDMVSFTGSTATGRSV 245
Cdd:TIGR01722 153 PLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSE-AGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 246 MADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGC-AITTRLVVPRARydEAVAIAAGTMGSIKPGD 324
Cdd:TIGR01722 231 HTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCmAISAAVLVGAAD--EWVPEIRERAEKIRIGP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 325 PTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGG-GRPAE-QAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIA 402
Cdd:TIGR01722 309 GDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGrGYKVDgYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 403 HDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNggVWYSADVP---FGGYKQS--GNGREMGVAGFEE 477
Cdd:TIGR01722 389 ADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN--VPIPVPLPyfsFTGWKDSffGDHHIYGKQGTHF 466
|
....*....
gi 1231751504 478 YLETKAIAT 486
Cdd:TIGR01722 467 YTRGKTVTT 475
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
12-488 |
1.32e-52 |
|
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: 185.48 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 12 LIDGKLASGGAGGfATVNPA-TEEVLGEAANADAADMDRAIDAARRAFDDtdWStNTGL--RVRCVRQLRDVLREHLEEL 88
Cdd:cd07125 36 IINGEETETGEGA-PVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAG--WS-ATPVeeRAEILEKAADLLEANRGEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGapRMLTAG-AQLEGPIDDLRFAADTAEGyswtqdLGHATPLGIPT--RRSVVREAVGVVGAITPWNFPHQI 165
Cdd:cd07125 112 IALAAAEAG--KTLADAdAEVREAIDFCRYYAAQARE------LFSDPELPGPTgeLNGLELHGRGVFVCISPWNFPLAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 166 NLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATG--- 242
Cdd:cd07125 184 FTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHE-AGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAkli 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 243 RSVMADAAATIKKVFLELGGKSAFVV--LDDADLAAACSVA-GFSvcvHAGQGCAITTRLVVPRARYDEAVAIAAGTMGS 319
Cdd:cd07125 263 NRALAERDGPILPLIAETGGKNAMIVdsTALPEQAVKDVVQsAFG---SAGQRCSALRLLYLQEEIAERFIEMLKGAMAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 320 IKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFAcggGRPAEQAAGFFIEPTVIAGltNEARVAREEIFGPVLT 399
Cdd:cd07125 340 LKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIA---PAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGPILH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 400 VIAHDGD--DDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVN----GGVwysadV---PFGGYKQSGNGREm 470
Cdd:cd07125 415 VIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitGAI-----VgrqPFGGWGLSGTGPK- 488
|
490 500
....*....|....*....|....
gi 1231751504 471 gvAGFEEYL------ETKAIATAA 488
Cdd:cd07125 489 --AGGPNYLlrfgneKTVSLNTTA 510
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
11-468 |
1.22e-51 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 182.08 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 11 LLIDGKLASGGAGGFATVNPATEEVLGEAANADAADMDRAIDAARRAFddTDWStNTGLRVRC--VRQLRDVLREHLEEL 88
Cdd:PRK09457 3 LWINGDWIAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF--PAWA-RLSFEERQaiVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 89 RELTISEVGAPR--MLTAGAQLEGPIDdLRFAADTAEGYSWTQDLGHATplgiptrrSVVR-EAVGVVGAITPWNFPHQI 165
Cdd:PRK09457 80 AEVIARETGKPLweAATEVTAMINKIA-ISIQAYHERTGEKRSEMADGA--------AVLRhRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 166 NLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTlGAMLAKDPRVDMVSFTGSTATGRSV 245
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQ-AGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 246 MADAAATIKKVF-LELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPR-ARYDEAVAIAAGTMGSIKPG 323
Cdd:PRK09457 229 HRQFAGQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQgAQGDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 324 DP-TKPGTVCGPVISARQRDR-VQSYLDLaLAEGGTFACGGGRPAEQAAgfFIEPTVIaGLTNEARVAREEIFGPVLTVI 401
Cdd:PRK09457 309 RWdAEPQPFMGAVISEQAAQGlVAAQAQL-LALGGKSLLEMTQLQAGTG--LLTPGII-DVTGVAELPDEEYFGPLLQVV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231751504 402 AHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVN----VNGGvwySADVPFGGYKQSGNGR 468
Cdd:PRK09457 385 RYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNwnkpLTGA---SSAAPFGGVGASGNHR 452
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
135-484 |
2.74e-49 |
|
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: 175.00 E-value: 2.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 135 TPLG-IPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHtdMPPGVINIV 213
Cdd:cd07136 85 TPLLnFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET--FDEEYVAVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 214 TSTDHTLGAMLAKdpRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLA-AACSVAgFSVCVHAGQG 292
Cdd:cd07136 163 EGGVEENQELLDQ--KFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKlAAKRIV-WGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 293 CAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVcGPVISARQRDRVQSYLDlalaeGGTFACGGGRpaeQAAGF 372
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLD-----NGKIVFGGNT---DRETL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 373 FIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWY 452
Cdd:cd07136 311 YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMH 390
|
330 340 350
....*....|....*....|....*....|....
gi 1231751504 453 SA--DVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07136 391 LAnpYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
70-479 |
1.42e-48 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 174.64 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGapRMLTAGAqleGPIDDLRFAADTAEGYSwTQDLGHATPLGIPTRRSV-VRE 148
Cdd:PLN02315 80 RGEIVRQIGDALRAKLDYLGRLVSLEMG--KILAEGI---GEVQEIIDMCDFAVGLS-RQLNGSIIPSERPNHMMMeVWN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 149 AVGVVGAITPWNFPhqinLAKLG----PALAAGNTVVLKPAPDTPWVAAVIGELIA---EHTDMPPGVINIVTSTDHtLG 221
Cdd:PLN02315 154 PLGIVGVITAFNFP----CAVLGwnacIALVCGNCVVWKGAPTTPLITIAMTKLVAevlEKNNLPGAIFTSFCGGAE-IG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 222 AMLAKDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVV 301
Cdd:PLN02315 229 EAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 302 PRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGrpAEQAAGFFIEPTVIAg 381
Cdd:PLN02315 309 HESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGS--AIESEGNFVQPTIVE- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 382 LTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADAD---RAAGVASRlRAGTVNVN--------GGV 450
Cdd:PLN02315 386 ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPEtifKWIGPLGS-DCGIVNVNiptngaeiGGA 464
|
410 420
....*....|....*....|....*....
gi 1231751504 451 wysadvpFGGYKQSGNGREMGVAGFEEYL 479
Cdd:PLN02315 465 -------FGGEKATGGGREAGSDSWKQYM 486
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
20-467 |
2.64e-44 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 166.91 E-value: 2.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 20 GGAGGFATV-NPA-TEEVLGEAANADAADMDRAIDAARRAFddTDWStNTGLRVR--CVRQLRDVLREHLEELRELTISE 95
Cdd:PRK11904 558 NGEGEARPVvSPAdRRRVVGEVAFADAEQVEQALAAARAAF--PAWS-RTPVEERaaILERAADLLEANRAELIALCVRE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 96 vgaprmltAGAQLEGPIDDLRFAAD-----TAEGyswTQDLGHATPLGIPT--RRSVVREAVGVVGAITPWNFPHQINLA 168
Cdd:PRK11904 635 --------AGKTLQDAIAEVREAVDfcryyAAQA---RRLFGAPEKLPGPTgeSNELRLHGRGVFVCISPWNFPLAIFLG 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 169 KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRS---V 245
Cdd:PRK11904 704 QVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHE-AGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIinrT 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 246 MADAAATIKKVFLELGGKSAFV---------VLDDADLAAACSvagfsvcvhAGQGCAITTRLVVPRARYDEAVAIAAGT 316
Cdd:PRK11904 783 LAARDGPIVPLIAETGGQNAMIvdstalpeqVVDDVVTSAFRS---------AGQRCSALRVLFVQEDIADRVIEMLKGA 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 317 MGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDlALAEGGTFACGGGRPAEQAAGFFIEPTVIAglTNEARVAREEIFGP 396
Cdd:PRK11904 854 MAELKVGDPRLLSTDVGPVIDAEAKANLDAHIE-RMKREARLLAQLPLPAGTENGHFVAPTAFE--IDSISQLEREVFGP 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 397 VLTVIAHDGDD-DAV--RIaNDSPYGLSATVYGADADRAAGVASRLRAGTVNVN----GGVwysadV---PFGGYKQSGN 466
Cdd:PRK11904 931 ILHVIRYKASDlDKVidAI-NATGYGLTLGIHSRIEETADRIADRVRVGNVYVNrnqiGAV-----VgvqPFGGQGLSGT 1004
|
.
gi 1231751504 467 G 467
Cdd:PRK11904 1005 G 1005
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
76-476 |
3.92e-43 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 159.42 E-value: 3.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 76 QLRDVLR---EHLEELRELTISEVGAPRMLTAGAQLEGPIDDLRFaaDTAEGYSWTQDLGHATPLGI-PTRRSVVREAVG 151
Cdd:PTZ00381 34 QLRNLLRmleENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEH--LLKHLDEYLKPEKVDTVGVFgPGKSYIIPEPLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 152 VVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHtdMPPGVINIVtSTDHTLGAMLAKDPrVD 231
Cdd:PTZ00381 112 VVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY--LDPSYVRVI-EGGVEVTTELLKEP-FD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 232 MVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRARYDEAVA 311
Cdd:PTZ00381 188 HIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 312 IAAGTMGSIKPGDPTKPGTVcGPVISARQRDRVQSYLDlalAEGGTFACGGGRPAEQAagfFIEPTVIAGLTNEARVARE 391
Cdd:PTZ00381 268 ALKEAIKEFFGEDPKKSEDY-SRIVNEFHTKRLAELIK---DHGGKVVYGGEVDIENK---YVAPTIIVNPDLDSPLMQE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 392 EIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSADV--PFGGYKQSGNGRE 469
Cdd:PTZ00381 341 EIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPnlPFGGVGNSGMGAY 420
|
....*..
gi 1231751504 470 MGVAGFE 476
Cdd:PTZ00381 421 HGKYGFD 427
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
70-476 |
5.72e-42 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 155.07 E-value: 5.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEgySWTQDLGHATPLGIPTRRSVVR-E 148
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLP--EWMKPEPVKKNLATLLDDVYIYkE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 149 AVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTD--MPPGVINIVTSTDHTLgamlak 226
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDkeCYPVVLGGVEETTELL------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 227 DPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCaITTRLVVPRARY 306
Cdd:cd07132 174 KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC-IAPDYVLCTPEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 307 DEAVAIAAGTmgSIKP--GDPTKPGTVCGPVISARQRDRVQsyldlALAEGGTFACGG-GRPAEQaagfFIEPTVIAGLT 383
Cdd:cd07132 253 QEKFVEALKK--TLKEfyGEDPKESPDYGRIINDRHFQRLK-----KLLSGGKVAIGGqTDEKER----YIAPTVLTDVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 384 NEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSA--DVPFGGY 461
Cdd:cd07132 322 PSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTldSLPFGGV 401
|
410
....*....|....*
gi 1231751504 462 KQSGNGREMGVAGFE 476
Cdd:cd07132 402 GNSGMGAYHGKYSFD 416
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-484 |
6.37e-42 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 157.99 E-value: 6.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 12 LIDGKLASGGAGGFATV-NPATEEVLGEAANADAADMDRAIDAARRAFddTDW-STNTGLRVRCVRQLRDVLREHLEELR 89
Cdd:PLN02419 117 LIGGSFVESQSSSFIDViNPATQEVVSKVPLTTNEEFKAAVSAAKQAF--PLWrNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 90 ELTISEVGAPRMLTAGAQLEGpIDDLRFAADTAegyswTQDLGHATPL---GIPTRRsvVREAVGVVGAITPWNFPHQIN 166
Cdd:PLN02419 195 MNITTEQGKTLKDSHGDIFRG-LEVVEHACGMA-----TLQMGEYLPNvsnGVDTYS--IREPLGVCAGICPFNFPAMIP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 167 LAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAmLAKDPRVDMVSFTGSTATGRSVM 246
Cdd:PLN02419 267 LWMFPVAVTCGNTFILKPSEKDPGASVILAELAME-AGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 247 ADAAATIKKVFLELGGKSAFVVLDDADLAA---ACSVAGFSVcvhAGQGC-AITTRLVVPRARYDEAVAIAAGTMGSIKP 322
Cdd:PLN02419 345 ARAAAKGKRIQSNMGAKNHGLVLPDANIDAtlnALLAAGFGA---AGQRCmALSTVVFVGDAKSWEDKLVERAKALKVTC 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 323 GdpTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGR---PAEQAaGFFIEPTVIAGLTNEARVAREEIFGPVLT 399
Cdd:PLN02419 422 G--SEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvPGYEK-GNFIGPTILSGVTPDMECYKEEIFGPVLV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 400 VIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNggVWYSADVP---FGGYKQS--GNGREMGVAG 474
Cdd:PLN02419 499 CMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN--VPIPVPLPffsFTGNKASfaGDLNFYGKAG 576
|
490
....*....|
gi 1231751504 475 FEEYLETKAI 484
Cdd:PLN02419 577 VDFFTQIKLV 586
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
150-467 |
2.35e-41 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 154.53 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 150 VGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPapdtPWVAAVIGELIAE--H-TDMPPGVINIVTSTDHTLGAMLAK 226
Cdd:PLN00412 159 LGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP----PTQGAVAALHMVHcfHlAGFPKGLISCVTGKGSEIGDFLTM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 227 DPRVDMVSFTGSTaTGRSVMADAAATikKVFLELGGKSAFVVLDDADL---AAACSVAGFSvcvHAGQGCAITTRLVVPR 303
Cdd:PLN00412 235 HPGVNCISFTGGD-TGIAISKKAGMV--PLQMELGGKDACIVLEDADLdlaAANIIKGGFS---YSGQRCTAVKVVLVME 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 304 ARYDEAVAIAAGTMGSIKPGDPTKPGTVCgPVISARQRDRVQSYLDLALAEGGTFACGGGRpaeqaAGFFIEPTVIAGLT 383
Cdd:PLN00412 309 SVADALVEKVNAKVAKLTVGPPEDDCDIT-PVVSESSANFIEGLVMDAKEKGATFCQEWKR-----EGNLIWPLLLDNVR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 384 NEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYSAD-VPFGGYK 462
Cdd:PLN00412 383 PDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLK 462
|
....*
gi 1231751504 463 QSGNG 467
Cdd:PLN00412 463 DSGIG 467
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
104-465 |
1.12e-40 |
|
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: 153.13 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 104 AGAQLegpIDDLRFAADTAEgyswtqDLGHATPLGIP---TRRSVVREAVGVVGAITPWNFPhQI--NLAkLGPALAaGN 178
Cdd:cd07123 131 AACEL---IDFLRFNVKYAE------ELYAQQPLSSPagvWNRLEYRPLEGFVYAVSPFNFT-AIggNLA-GAPALM-GN 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 179 TVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVMADAAA------T 252
Cdd:cd07123 199 VVLWKPSDTAVLSNYLVYKILEE-AGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEnldryrT 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 253 IKKVFLELGGKSAFVVLDDAD---LAAACSVAGFSVCvhaGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPG 329
Cdd:cd07123 278 YPRIVGETGGKNFHLVHPSADvdsLVTATVRGAFEYQ---GQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 330 TVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRpAEQAAGFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDD-- 407
Cdd:cd07123 355 NFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGK-CDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDfe 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231751504 408 DAVRIAND-SPYGLSATVYGAD--ADRAAGVASRLRAGTVNVN----GGVwySADVPFGGYKQSG 465
Cdd:cd07123 434 ETLELVDTtSPYALTGAIFAQDrkAIREATDALRNAAGNFYINdkptGAV--VGQQPFGGARASG 496
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
70-471 |
9.40e-39 |
|
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: 147.36 E-value: 9.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEvgaprmltAGAQLEGPIDDLRFAADTAEGYS--WTQDLGHATplgiptrrsvvR 147
Cdd:TIGR01238 98 RAAKLDRLADLLELHMPELMALCVRE--------AGKTIHNAIAEVREAVDFCRYYAkqVRDVLGEFS-----------V 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 148 EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKD 227
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQE-AGFPAGTIQLLPGRGADVGAALTSD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 228 PRVDMVSFTGSTATGRSV---MADAAATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVHAGQGCAITTRLVVPRA 304
Cdd:TIGR01238 238 PRIAGVAFTGSTEVAQLInqtLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 305 RYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFA-CGGGRPAEQAAGFFIEPTVIAglT 383
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAqLTLDDSRACQHGTFVAPTLFE--L 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 384 NEARVAREEIFGPVLTVIAHDGD--DDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVwYSADV---PF 458
Cdd:TIGR01238 396 DDIAELSEEVFGPVLHVVRYKARelDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQ-VGAVVgvqPF 474
|
410
....*....|...
gi 1231751504 459 GGYKQSGNGREMG 471
Cdd:TIGR01238 475 GGQGLSGTGPKAG 487
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
140-484 |
6.15e-38 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 143.71 E-value: 6.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 140 PTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDmpPGVINIVTSTDHT 219
Cdd:cd07137 92 PAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLD--TKAIKVIEGGVPE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 220 LGAMLakDPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACS--VAG-FSVCvhAGQGCAIT 296
Cdd:cd07137 170 TTALL--EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRriAGGkWGCN--NGQACIAP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 297 TRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVcGPVISARQRDRVQSYLDlalaEGGTFAC---GGGRPAEQaagFF 373
Cdd:cd07137 246 DYVLVEESFAPTLIDALKNTLEKFFGENPKESKDL-SRIVNSHHFQRLSRLLD----DPSVADKivhGGERDEKN---LY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 374 IEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVWYS 453
Cdd:cd07137 318 IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQY 397
|
330 340 350
....*....|....*....|....*....|...
gi 1231751504 454 A--DVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:cd07137 398 AidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
17-467 |
1.52e-37 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 146.93 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 17 LASGGAGG--FATVNPA-TEEVLGEAANADAADMDRAIDAARRAFddTDWS-TNTGLRVRCVRQLRDVLREHLEELRELT 92
Cdd:PRK11905 559 LAGGDVDGgtRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAF--PEWSaTPAAERAAILERAADLMEAHMPELFALA 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 93 ISEVGAPrMLTAGAQLEGPIDDLRFAADTAEgySWTQDLGHatplgiptrrsvvrEAVGVVGAITPWNFPHQINLAKLGP 172
Cdd:PRK11905 637 VREAGKT-LANAIAEVREAVDFLRYYAAQAR--RLLNGPGH--------------KPLGPVVCISPWNFPLAIFTGQIAA 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 173 ALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGR---SVMADA 249
Cdd:PRK11905 700 ALVAGNTVLAKPAEQTPLIAARAVRLLHE-AGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARliqRTLAKR 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 250 AATIKKVFLELGGKSAFVVlDDADLA----AACSVAGFSvcvHAGQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDP 325
Cdd:PRK11905 779 SGPPVPLIAETGGQNAMIV-DSSALPeqvvADVIASAFD---SAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDP 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 326 TKPGTVCGPVISARQRDRVQSYLDLALAEGGTFAcGGGRPAEQAAGFFIEPTVI--AGLtneaRVAREEIFGPVLTVIAH 403
Cdd:PRK11905 855 WRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVH-QLPLPAETEKGTFVAPTLIeiDSI----SDLEREVFGPVLHVVRF 929
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 404 DGDD-DAVrIA--NDSPYGLSATVYGADADRAAGVASRLRAGTVNVN----GGVwysadV---PFGGYKQSGNG 467
Cdd:PRK11905 930 KADElDRV-IDdiNATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniiGAV-----VgvqPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
12-467 |
4.45e-35 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 139.69 E-value: 4.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 12 LIDGKLASGGAggFATVNPA-TEEVLGEAANADAADMDRAIDAARRAFddTDWS-TNTGLRVRCVRQLRDVLREHLEELR 89
Cdd:COG4230 561 LIAGEAASGEA--RPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAF--PAWSaTPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 90 ELTISEVGapRMLTAG-AQLEGPIDDLRFAADTAEgyswtQDLGHATPLgiptrrsvvrEAVGVVGAITPWNFPHQINLA 168
Cdd:COG4230 637 ALLVREAG--KTLPDAiAEVREAVDFCRYYAAQAR-----RLFAAPTVL----------RGRGVFVCISPWNFPLAIFTG 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 169 KLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSV--- 245
Cdd:COG4230 700 QVAAALAAGNTVLAKPAEQTPLIAARAVRLLHE-AGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInrt 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 246 MADAAATIKKVFLELGGKSAFVV---------LDDAdLAAAcsvagF-SvcvhAGQGCAITTRLVVPRARYDEAVAIAAG 315
Cdd:COG4230 779 LAARDGPIVPLIAETGGQNAMIVdssalpeqvVDDV-LASA-----FdS----AGQRCSALRVLCVQEDIADRVLEMLKG 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 316 TMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDlALAEGGTFACGGGRPAEQAAGFFIEPTVIAglTNEARVAREEIFG 395
Cdd:COG4230 849 AMAELRVGDPADLSTDVGPVIDAEARANLEAHIE-RMRAEGRLVHQLPLPEECANGTFVAPTLIE--IDSISDLEREVFG 925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 396 PVLTVIAHDGDD-DAV--RIaNDSPYGLSATVYGADADRAAGVASRLRAGTVNVN----GGVwysadV---PFGGYKQSG 465
Cdd:COG4230 926 PVLHVVRYKADElDKVidAI-NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNrniiGAV-----VgvqPFGGEGLSG 999
|
..
gi 1231751504 466 NG 467
Cdd:COG4230 1000 TG 1001
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
140-484 |
1.03e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 127.15 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 140 PTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDmpPGVINIVTStdht 219
Cdd:PLN02203 99 PATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLD--SKAVKVIEG---- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 220 lGAMLAK---DPRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVlDDADLAAACSVA-------GFSVCvhA 289
Cdd:PLN02203 173 -GPAVGEqllQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV-DSLSSSRDTKVAvnrivggKWGSC--A 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 290 GQGCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCgPVISARQRDRVQSYLDLALAEgGTFACGGGRPAEQa 369
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMA-RILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDEKK- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 370 agFFIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGG 449
Cdd:PLN02203 326 --LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDA 403
|
330 340 350
....*....|....*....|....*....|....*..
gi 1231751504 450 -VWYSAD-VPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:PLN02203 404 iIQYACDsLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
95-473 |
2.29e-31 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 125.43 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 95 EVGAPRMLTAgaQLEGPIDDLRFAADTAEGYSWTQDLGHATPLGIPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPAL 174
Cdd:cd07084 48 VTGKGWMFAE--NICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGAL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 175 AAGNTVVLKPAPDTPWVAAVIGELIAEHTDMPPGVINIVTSTDHTlGAMLAKDPRVDMVSFTGSTATGRSVMADAAATik 254
Cdd:cd07084 126 AMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAKQA-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 255 KVFLELGGKSAFVVLDDAD-LAAACSVAGFSVCVHAGQGCAITTRLVVP-----RARYDEAVAIAAgtmgSIKPGDPTkp 328
Cdd:cd07084 203 RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPenwskTPLVEKLKALLA----RRKLEDLL-- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 329 gtvcgpvISARQRDRVQSYLDLALAEGGT-FACGGGRPAEQAAGFFIEPTVIAGL--TNEARVAR-----EEIFGPV--L 398
Cdd:cd07084 277 -------LGPVQTFTTLAMIAHMENLLGSvLLFSGKELKNHSIPSIYGACVASALfvPIDEILKTyelvtEEIFGPFaiV 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231751504 399 TVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRL-RAGTVNVNG---GVWYSADVPFGGYKQSGNGREMGVA 473
Cdd:cd07084 350 VEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLwVAGRTYAILrgrTGVAPNQNHGGGPAADPRGAGIGGP 428
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
151-467 |
2.09e-29 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 122.77 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 151 GVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEhTDMPPGVINIVTSTDHTLGAMLAKDPRV 230
Cdd:PRK11809 770 GPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLE-AGVPAGVVQLLPGRGETVGAALVADARV 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 231 DMVSFTGSTATGR------SVMADAAATIKKVFLELGGKSAFVVlDDADLA----AACSVAGFSvcvHAGQGCAITTRLV 300
Cdd:PRK11809 849 RGVMFTGSTEVARllqrnlAGRLDPQGRPIPLIAETGGQNAMIV-DSSALTeqvvADVLASAFD---SAGQRCSALRVLC 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 301 VPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGT-FACGGGRPAEQAAGFFIEPTVI 379
Cdd:PRK11809 925 LQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvFQAARENSEDWQSGTFVPPTLI 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 380 AgLTNEARVAReEIFGPVLTVI--AHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVwYSADV- 456
Cdd:PRK11809 1005 E-LDSFDELKR-EVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNM-VGAVVg 1081
|
330
....*....|...
gi 1231751504 457 --PFGGYKQSGNG 467
Cdd:PRK11809 1082 vqPFGGEGLSGTG 1094
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
55-484 |
5.96e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 116.30 E-value: 5.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 55 RRAFDDtDWSTNTGLRVRCVRQLRDVLREHLEELRELTISEVGAPRMLTAGAQLEGPIDDLRFAADTAEgySWTQDLGHA 134
Cdd:PLN02174 20 RRSFDD-GVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLK--NWMAPEKAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 135 TPLG-IPTRRSVVREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDmpPGVINIV 213
Cdd:PLN02174 97 TSLTtFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLD--SSAVRVV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 214 TSTDHTLGAMLAKdpRVDMVSFTGSTATGRSVMADAAATIKKVFLELGGKSAFVVLDDADLAAACS--VAGFSVCvHAGQ 291
Cdd:PLN02174 175 EGAVTETTALLEQ--KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRriIAGKWGC-NNGQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 292 GCAITTRLVVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVcGPVISARQRDRVQSYLDLALAEgGTFACGGGRPAEQAAg 371
Cdd:PLN02174 252 ACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDM-SRIVNSTHFDRLSKLLDEKEVS-DKIVYGGEKDRENLK- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 372 ffIEPTVIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVASRLRAGTVNVNGGVW 451
Cdd:PLN02174 329 --IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAV 406
|
410 420 430
....*....|....*....|....*....|....*
gi 1231751504 452 YSA--DVPFGGYKQSGNGREMGVAGFEEYLETKAI 484
Cdd:PLN02174 407 HLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
86-448 |
8.51e-26 |
|
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: 109.55 E-value: 8.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 86 EELRELTISEVGAPRmltagAQLEGPID----DLRFAADTAEGYSWTQ---D--LGHATPLGIP-TRRSVVreAVGVVGA 155
Cdd:cd07129 39 DELVARAHAETGLPE-----ARLQGELGrttgQLRLFADLVREGSWLDariDpaDPDRQPLPRPdLRRMLV--PLGPVAV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 156 ITPWNFPHQINLAklG----PALAAGNTVVLKPAPDTPWVAAVIGELI---AEHTDMPPGVINIVTSTDHTLGAMLAKDP 228
Cdd:cd07129 112 FGASNFPLAFSVA--GgdtaSALAAGCPVVVKAHPAHPGTSELVARAIraaLRATGLPAGVFSLLQGGGREVGVALVKHP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 229 RVDMVSFTGSTATGRSVMADAAA--TIKKVFLELGGKSAFVVLDDADLAAACSVA-GF--SVCVHAGQGCAITTRLVVPR 303
Cdd:cd07129 190 AIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGALAERGEAIAqGFvgSLTLGAGQFCTNPGLVLVPA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 304 -ARYDEAVAIAAGTMGSikpgdpTKPGTVCGPVISARQRDRVQSYLDLA----LAEGgtfacGGGRPAEQAAGFFIEPTV 378
Cdd:cd07129 270 gPAGDAFIAALAEALAA------APAQTMLTPGIAEAYRQGVEALAAAPgvrvLAGG-----AAAEGGNQAAPTLFKVDA 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 379 IAGLTNEArvAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADAD--RAAGVASRL--RAGTVNVNG 448
Cdd:cd07129 339 AAFLADPA--LQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDDlaLARELLPVLerKAGRLLFNG 410
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
151-436 |
4.98e-25 |
|
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: 108.13 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 151 GVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDMPPGVINIVTSTdhtLGAMLAKDPRV 230
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLPEGALQLICGS---VGDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 231 DMVSFTGSTATGRSVMADAAATIKKVFLELGGKSA-FVVL------DDADLAAACSVAGFSVCVHAGQGCAITTRLVVPR 303
Cdd:cd07128 223 DVVAFTGSAATAAKLRAHPNIVARSIRFNAEADSLnAAILgpdatpGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 304 ARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDLALAEGGTFACGGGRPAEQAA----GFFIEPTVI 379
Cdd:cd07128 303 ARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGAdaekGAFFPPTLL 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1231751504 380 --AGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVA 436
Cdd:cd07128 383 lcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
151-436 |
4.62e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.09 E-value: 4.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 151 GVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAAVIGELIAEHTDMPPGVINIVTSTDhtlGAMLAKDPRV 230
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGILPAGALSVVCGSS---AGLLDHLQPF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 231 DMVSFTGSTATGRSVMADAAATIKKVFLELGGKSafvvLDDADLA--AACSVAGFSVCVH---------AGQGCAITTRL 299
Cdd:PRK11903 227 DVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADS----LNSALLGpdAAPGSEAFDLFVKevvremtvkSGQKCTAIRRI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 300 VVPRARYDEAVAIAAGTMGSIKPGDPTKPGTVCGPVISARQRDRVQSYLDlALAEGGTFACGGGR----PAEQAAGFFIE 375
Cdd:PRK11903 303 FVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGfalvDADPAVAACVG 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231751504 376 PT--VIAGLTNEARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSATVYGADADRAAGVA 436
Cdd:PRK11903 382 PTllGASDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
127-465 |
6.52e-21 |
|
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: 95.62 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 127 WTQDLGHATPLGIPTRRSVVREAVG-VVGAITpwnFPHQINLAKLGPALAAGNTVVLKPAPDTPWVAA----VIGELIAE 201
Cdd:cd07127 173 WEKPQGKHDPLAMEKTFTVVPRGVAlVIGCST---FPTWNGYPGLFASLATGNPVIVKPHPAAILPLAitvqVAREVLAE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 202 HTDMPPGVINIVTSTDHTLGAMLAKDPRVDMVSFTGSTATGRSVmaDAAATIKKVFLELGGKSAFVVLDDADLAAACSVA 281
Cdd:cd07127 250 AGFDPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWL--EANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 282 GFSVCVHAGQGCAITTRLVVPR---------ARYDE-AVAIAAGTMGSIkpGDPTKPGTVCGPVISARQRDRVQSyldlA 351
Cdd:cd07127 328 AFSLSLYSGQMCTTPQNIYVPRdgiqtddgrKSFDEvAADLAAAIDGLL--ADPARAAALLGAIQSPDTLARIAE----A 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 352 LAEGGTFACGGGRPAEQAAGFFIEPTVIAGLTNEARVA-REEIFGPVLTVIAHDGDDDAVRIANDSPY---GLSATVYGA 427
Cdd:cd07127 402 RQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAyAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYST 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1231751504 428 DA---DRAAGVAsrLRAG---TVNVNGGVWYSADVPFGGYKQSG 465
Cdd:cd07127 482 DPevvERVQEAA--LDAGvalSINLTGGVFVNQSAAFSDFHGTG 523
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
70-284 |
1.15e-06 |
|
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: 50.70 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRmltagaqLEGPIDDLRFAADTAEGyswTQDLghatplgIPTRRS----- 144
Cdd:cd07121 28 REKIIEAIREALLSNAEELAEMAVEETGMGR-------VEDKIAKNHLAAEKTPG---TEDL-------TTTAWSgdngl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 145 --VVREAVGVVGAITPWNFP------HQINLaklgpaLAAGNTVVLKPAPDTPWVAAVIGELIAEHTDMPPGVINIVTS- 215
Cdd:cd07121 91 tlVEYAPFGVIGAITPSTNPtetiinNSISM------LAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDNLVVTv 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751504 216 ---TDHTLGAMLAkDPRVDMVSFTGSTATGRSVMadaaATIKKVFLELGGKSAFVVLDDADL--AAACSVAGFS 284
Cdd:cd07121 165 eepTIETTNELMA-HPDINLLVVTGGPAVVKAAL----SSGKKAIGAGAGNPPVVVDETADIekAARDIVQGAS 233
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
74-413 |
2.99e-06 |
|
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: 49.57 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 74 VRQLRDVLREHLEELRELTISEVGAprmltagaqleGPIDDlRFAADTAEG-YSWTQDLGHATPlGIPTRRS-----VVR 147
Cdd:cd07081 27 FRAAAEAAEDARIDLAKLAVSETGM-----------GRVED-KVIKNHFAAeYIYNVYKDEKTC-GVLTGDEnggtlIIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 148 EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAP---DTPWVAAVIGELIAEHTDMPPGVINIVTSTDHTLGAML 224
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPrakKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 225 AKDPRVDMVsftgsTATGRSVMADAAATIKKVFLELGGKSAFVVLDD-ADLAAACSVAGFSVCVHAGQGCAITTRLVVPR 303
Cdd:cd07081 174 MKFPGIGLL-----LATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDEtADIKRAVQSIVKSKTFDNGVICASEQSVIVVD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 304 ARYDEAVAIAAGTMGSIkpgdptkpgtvcgpvISARQRDRVQsylDLALAEGGTFACGGGRPA---EQAAGF-------- 372
Cdd:cd07081 249 SVYDEVMRLFEGQGAYK---------------LTAEELQQVQ---PVILKNGDVNRDIVGQDAykiAAAAGLkvpqetri 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1231751504 373 -FIEPTVIAgltnEARVAREEIFGPVLTVIAHDGDDDAVRIA 413
Cdd:cd07081 311 lIGEVTSLA----EHEPFAHEKLSPVLAMYRAANFADADAKA 348
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
70-277 |
4.01e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 49.13 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 70 RVRCVRQLRDVLREHLEELRELTISEVGAPRmltagaqLEGPIDDLRFAADTAEGyswTQDLghatplgIPTRRS----- 144
Cdd:PRK15398 60 RQRIIDAIREALLPHAEELAELAVEETGMGR-------VEDKIAKNVAAAEKTPG---VEDL-------TTEALTgdngl 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 145 --VVREAVGVVGAITPWNFP------HQINLaklgpaLAAGNTVVLKPAPD----TPWVAAVIGELIAEHTdmppGVINI 212
Cdd:PRK15398 123 tlIEYAPFGVIGAVTPSTNPtetiinNAISM------LAAGNSVVFSPHPGakkvSLRAIELLNEAIVAAG----GPENL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231751504 213 VTS----TDHTLGAMLAkDPRVDMVSFTGSTATGRSVMadaaATIKKVFLELGGKSAFVVLDDADLAAA 277
Cdd:PRK15398 193 VVTvaepTIETAQRLMK-HPGIALLVVTGGPAVVKAAM----KSGKKAIGAGAGNPPVVVDETADIEKA 256
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
69-308 |
7.16e-06 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 48.37 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 69 LRVRCVRQLRDVLREHLEELRELTISEVGA----------PRMLTAGAQLEGPIDDLRFAADtAEGYS---WTQDLGHAT 135
Cdd:cd07077 17 QRDLIINAIANALYDTRQRLASEAVSERGAyirslianwiAMMGCSESKLYKNIDTERGITA-SVGHIqdvLLPDNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 136 plgiptrrsVVREAVGVVGAITPWNFP-HQINLAKLGpaLAAGNTVVLKPAPDTPWVAAVIG----ELIAEHTdmPPGVI 210
Cdd:cd07077 96 ---------VRAFPIGVTMHILPSTNPlSGITSALRG--IATRNQCIFRPHPSAPFTNRALAllfqAADAAHG--PKILV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 211 NIVTSTDHTLGAMLAKDPRVDMVsftgsTATGRSVMADAA--ATIKKVFLELGGKSAFVVLDDADLAAACSVAGFSVCVH 288
Cdd:cd07077 163 LYVPHPSDELAEELLSHPKIDLI-----VATGGRDAVDAAvkHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFF 237
|
250 260
....*....|....*....|
gi 1231751504 289 AGQGCAITTRLVVPRARYDE 308
Cdd:cd07077 238 DQNACASEQNLYVVDDVLDP 257
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
151-262 |
2.14e-04 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 43.64 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751504 151 GVVGAITPWNFPHQINLAKLGPALAAGNTVVLKpaPDTPwVAAVIGELI--AEHTDMPPGVINIVTSTDHTLGAMLAK-D 227
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALFMGNKPLLK--VDSK-VSVVMEQFLrlLHLCGMPATDVDLIHSDGPTMNKILLEaN 220
|
90 100 110
....*....|....*....|....*....|....*
gi 1231751504 228 PRvdMVSFTGSTATGRSVmadAAATIKKVFLELGG 262
Cdd:cd07126 221 PR--MTLFTGSSKVAERL---ALELHGKVKLEDAG 250
|
|
| |
