|
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: 898.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 9 SALLIDGKLSDGRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTELRVRCVRQLRDAMQQHVEEL 88
Cdd:TIGR04284 1 SRLLIDGKLVAGSAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDETDWSRDTALRVRCLRQLRDALRAHVEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYPWKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLA 168
Cdd:TIGR04284 81 RELTIAEVGAPRMLTAGAQLEGPVDDLGFAADLAESYAWTTDLGVASPMGIPTRRTLRREAVGVVGAITPWNFPHQINLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 169 KLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMAD 248
Cdd:TIGR04284 161 KLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 249 AAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDP 328
Cdd:TIGR04284 241 AAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 329 GTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDD 408
Cdd:TIGR04284 321 GTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 409 AVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLIATAA 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: 701.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMLTASAQ 107
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 108 LEGPVGDLSFAADTAESYPWKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPD 187
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 188 TPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFV 267
Cdd:cd07089 162 TPLSALLLGEIIAE-TDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 268 VLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGY 347
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 348 LDLAVAEGGRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGA 427
Cdd:cd07089 321 IARGRDEGARLVTGGGRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 428 DPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLIA 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: 536.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGK--LSDGrAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEE 87
Cdd:cd07138 1 FYIDGAwvAPAG-TETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSvEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 88 LRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYPWKQDLGEAsplgiatrrTLAREAVGVVGAITPWNFP-HQIn 166
Cdd:cd07138 78 LAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNS---------LVVREPIGVCGLITPWNWPlNQI- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIvEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:cd07138 148 VLKVAPALAAGCTVVLKPSEVAPLSAIILAEIL-DEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPN 326
Cdd:cd07138 227 EAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 327 DPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGA-RPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDG 405
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 406 DDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYcADAPFGGYKQSGIGREMGLLGFEEYLEAKLIA 485
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFN-PGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
11-485 |
2.89e-178 |
|
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: 508.51 E-value: 2.89e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDstDWSRNT-ELRVRCVRQLRDAMQQHVEEL 88
Cdd:COG1012 8 LFIGGEWVAAASGeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP--AWAATPpAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLtASAQLEGPVGDLSFAADTAESYPwkqdlGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQINL 167
Cdd:COG1012 86 AALLTLETGKPLAE-ARGEVDRAADFLRYYAGEARRLY-----GETIPSDAPGTRAYVrREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 168 AKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMA 247
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEE-AGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 248 DAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPND 327
Cdd:COG1012 239 AAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 328 PGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPaDREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDD 407
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRP-DGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 408 DAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYC-ADAPFGGYKQSGIGREMGLLGFEEYLEAKLIA 485
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
11-484 |
1.36e-174 |
|
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: 499.02 E-value: 1.36e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSD-GRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNT-ELRVRCVRQLRDAMQQHVEEL 88
Cdd:cd07139 1 LFIGGRWVApSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSpAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYPWKQDLgEASPLGIATRRtlaREAVGVVGAITPWNFPHQINLA 168
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERR-PGSGGGHVLVR---REPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 169 KLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHAlGALLAKDPRVDMISFTGSTATGRAVMAD 248
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEE-AGLPPGVVNVVPADREV-GEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 249 AAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDP 328
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 329 GTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDD 408
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607908 409 AVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNgGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-484 |
2.56e-163 |
|
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: 469.70 E-value: 2.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 19 DGRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVG 97
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPaAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 98 APRMLTAsaqlegpvGDLSFAADTAESYP--WKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALA 175
Cdd:pfam00171 81 KPLAEAR--------GEVDRAIDVLRYYAglARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 176 AGNTVVLKPAPDTPWCAAALGEIIVEHtDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKK 255
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEA-GLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 256 VFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPL 335
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 336 ISARQRDRVQGYLDLAVAEGGRFACGGarPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIAND 415
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEGAKLLTGG--EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIAND 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 416 SPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCAD-APFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
49-484 |
1.51e-141 |
|
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: 413.53 E-value: 1.51e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 49 RAIEAARRAFDstDWSR-NTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRmLTASAQLEGPVGDLSFAADTAESYpw 127
Cdd:cd07078 2 AAVAAARAAFK--AWAAlPPAERAAILRKLADLLEERREELAALETLETGKPI-EEALGEVARAADTFRYYAGLARRL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 128 kqdLGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFP 206
Cdd:cd07078 77 ---HGEVIPSPDPGELAIVrREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAE-AGLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 207 PGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSAC 286
Cdd:cd07078 153 PGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 287 MHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPa 366
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 367 DREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNV 446
Cdd:cd07078 312 EGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWI 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 15607908 447 NGG-VWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07078 392 NDYsVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-485 |
2.59e-139 |
|
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: 408.36 E-value: 2.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWsRNTELRVRC--VRQLRDAMQQHVEELRELTISEVGAPrmlTAS 105
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT--W-RKTTARERAaiLRRWADLIRERAEDLARLLTLEQGKP---LAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 106 AQlegpvGDLSFAADTAEsypW-----KQDLGEASPLGIATRRTLA-REAVGVVGAITPWNFPhqINLA--KLGPALAAG 177
Cdd:cd07103 76 AR-----GEVDYAASFLE---WfaeeaRRIYGRTIPSPAPGKRILViKQPVGVVAAITPWNFP--AAMItrKIAPALAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 178 NTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVF 257
Cdd:cd07103 146 CTVVLKPAEETPLSALALAELAEE-AGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 258 LELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLIS 337
Cdd:cd07103 225 LELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLIN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 338 ARQRDRVQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSP 417
Cdd:cd07103 305 ERAVEKVEALVEDAVAKGAKVLTGGKRLGLG--GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTP 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 418 YGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLIA 485
Cdd:cd07103 383 YGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-484 |
8.06e-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: 408.24 E-value: 8.06e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 13 IDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSR-NTELRVRCVRQLRDAMQQHVEELRE 90
Cdd:cd07119 2 IDGEWVEAASGkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHlPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 91 LTISEVGAPrmltasaqLEGPVGDLSFAADTAESYP--WKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLA 168
Cdd:cd07119 82 LETLNTGKT--------LRESEIDIDDVANCFRYYAglATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 169 KLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMAD 248
Cdd:cd07119 154 KLAPALAAGNTVVIKPSEVTPLTTIALFELIEE-AGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 249 AAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDP 328
Cdd:cd07119 233 AAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 329 GTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADREV--GFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGD 406
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 407 DDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-484 |
5.76e-138 |
|
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: 404.60 E-value: 5.76e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPrmlTASA 106
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPlEERRAALLAIADAIEANAEELARLLTLEQGKP---LAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 QLEgPVGDLSFAADTAESYPWKQDLGEAsplgiATRRT-LAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPA 185
Cdd:cd07106 77 QFE-VGGAVAWLRYTASLDLPDEVIEDD-----DTRRVeLRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 186 PDTPWCAAALGEIIVEHtdFPPGVVNIVTSSsHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSA 265
Cdd:cd07106 151 PFTPLCTLKLGELAQEV--LPPGVLNVVSGG-DELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 266 FVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQ 345
Cdd:cd07106 228 AIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 346 GYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVY 425
Cdd:cd07106 308 ELVEDAKAKGAKVLAGGEPLDGP--GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 426 GADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07106 386 SSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-485 |
3.89e-136 |
|
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: 400.40 E-value: 3.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEELRELTISEVGAPRMLTAS 105
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAeRARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 106 AQLEGPVGDLSFAADTAesypwKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPA 185
Cdd:cd07093 79 RDIPRAAANFRFFADYI-----LQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 186 PDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSA 265
Cdd:cd07093 154 EWTPLTAWLLAELANE-AGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 266 FVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQ 345
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 346 GYLDLAVAEGGRFACGGARP--ADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGT 423
Cdd:cd07093 313 GYVELARAEGATILTGGGRPelPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607908 424 VYGADPQRAARIASRLRVGTVNVNggVWYCAD--APFGGYKQSGIGREMGLLGFEEYLEAKLIA 485
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGTVWVN--CWLVRDlrTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
11-482 |
6.09e-136 |
|
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: 400.82 E-value: 6.09e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNT-ELRVRCVRQLRDAMQQHVEEL 88
Cdd:cd07091 6 LFINNEFVDSVSGkTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDpRERGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPrmLTASAQlegpvGDLSFAADTAESYPWKQD--LGEASPLGiatRRTLA---REAVGVVGAITPWNFPH 163
Cdd:cd07091 86 AALESLDNGKP--LEESAK-----GDVALSIKCLRYYAGWADkiQGKTIPID---GNFLAytrREPIGVCGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 164 QINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGR 243
Cdd:cd07091 156 LMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKE-AGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 244 AVMADAAAT-IKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRP 322
Cdd:cd07091 235 TIMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 323 GDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIA 402
Cdd:cd07091 315 GDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSK--GYFIQPTVFTDVKDDMKIAKEEIFGPVVTILK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 403 HDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07091 393 FKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
24-484 |
2.29e-133 |
|
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: 393.51 E-value: 2.29e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 24 TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPrmL 102
Cdd:cd07112 3 TFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSpAERKAVLLRLADLIEAHRDELALLETLDMGKP--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 103 TASAQLEGPvgdlsfaaDTAESYPWKQDL-----GEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAG 177
Cdd:cd07112 81 SDALAVDVP--------SAANTFRWYAEAidkvyGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 178 NTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAAT-IKKV 256
Cdd:cd07112 153 NSVVLKPAEQSPLTALRLAELALE-AGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 257 FLELGGKSAFVVLDDADLAAASAVSAFSACMH-AGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPL 335
Cdd:cd07112 232 WLECGGKSPNIVFADAPDLDAAAEAAAAGIFWnQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 336 ISARQRDRVQGYLDLAVAEGGRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIAND 415
Cdd:cd07112 312 VSEAHFDKVLGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607908 416 SPYGLSGTVYGADPQRAARIASRLRVGTVNVNGgvWYCADA--PFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07112 392 SVYGLAASVWTSDLSRAHRVARRLRAGTVWVNC--FDEGDIttPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-482 |
1.01e-132 |
|
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: 391.91 E-value: 1.01e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTEL-RVRCVRQLRDAMQQHVEELREL-------TISEVGA 98
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTeRGKLLRRLADLIEANAEELAELetrdngkLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 99 -----PRMLTASAQLegpvgdlsfaADTAEsypwkqdlGEASPLGIATRRT-LAREAVGVVGAITPWNFPHQINLAKLGP 172
Cdd:cd07114 81 qvrylAEWYRYYAGL----------ADKIE--------GAVIPVDKGDYLNfTRREPLGVVAAITPWNSPLLLLAKKLAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 173 ALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAAT 252
Cdd:cd07114 143 ALAAGNTVVLKPSEHTPASTLELAKLAEE-AGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 253 IKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVC 332
Cdd:cd07114 222 LAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 333 GPLISARQRDRVQGYLDLAVAEGGRFACGGARP--ADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAV 410
Cdd:cd07114 302 GPLATERQLEKVERYVARAREEGARVLTGGERPsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAI 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607908 411 RIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07114 382 ALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
11-482 |
6.40e-132 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 390.42 E-value: 6.40e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELR 89
Cdd:PRK13473 5 LLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTpKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYPWKQDlGEASPLGIATRRtlaREAVGVVGAITPWNFPHQINLAK 169
Cdd:PRK13473 83 RLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAA-GEYLEGHTSMIR---RDPVGVVASIAPWNYPLMMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 170 LGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADA 249
Cdd:PRK13473 159 LAPALAAGNTVVLKPSEITPLTALKLAELAADI--LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 250 AATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPG 329
Cdd:PRK13473 237 ADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 330 TVCGPLISARQRDRVQGYLDLAVAEG-GRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDD 408
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGK--GYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607908 409 AVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-482 |
5.95e-128 |
|
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: 379.36 E-value: 5.95e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDstDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMLTASA 106
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP--SWRRTTpAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 QLEGPVGDLSFAADTAESYPwKQDLGEASPlgiATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAP 186
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLE-GPAAGEYLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 187 DTPWCAAALGEIIVEhtDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAF 266
Cdd:cd07092 156 TTPLTTLLLAELAAE--VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 267 VVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQG 346
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 347 YLDLAvAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYG 426
Cdd:cd07092 314 FVERA-PAHARVLTGGRRAEGP--GYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWT 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15607908 427 ADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07092 391 RDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
27-484 |
7.12e-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: 371.77 E-value: 7.12e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTElRVRCVRQLRDAMQQHVEELRELTISEVGAPrmLTASA 106
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAE-RGRILWRLAELILANADELARLESLDTGKP--IRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 QLegpvgDLSFAADTAESYP-WKQDL-GEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKP 184
Cdd:cd07115 78 RL-----DVPRAADTFRYYAgWADKIeGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 185 APDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKS 264
Cdd:cd07115 153 AELTPLSALRIAELMAE-AGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 265 AFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRV 344
Cdd:cd07115 232 ANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 345 QGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTV 424
Cdd:cd07115 312 LDYVDVGREEGARLLTGGKRPGAR--GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 425 YGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07115 390 WTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
27-484 |
2.13e-123 |
|
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: 367.83 E-value: 2.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMlTAS 105
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTgAERAKYLRAIAEGVRERREELAELEARDNGKPLD-EAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 106 AQLEGPVGDLSFAADTAESYpwKQDLGEASPLGIATRRTLAR-EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKP 184
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQL--DAKAERAVPLPSEDFKARVRrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 185 APDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKS 264
Cdd:cd07110 156 SELTSLTELELAEIAAE-AGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 265 AFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRV 344
Cdd:cd07110 235 PIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 345 QGYLDLAVAEGGRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTV 424
Cdd:cd07110 315 LSFIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 425 YGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-484 |
2.17e-120 |
|
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: 360.12 E-value: 2.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMlTASA 106
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILG-EARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 QLEGPVGDLSFAADTAESYPWKqdLGEASPLGIATrrtLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAP 186
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGR--MIEPEPGSFSL---VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 187 DTPWCAAALGEIIVEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAF 266
Cdd:cd07120 155 QTAQINAAIIRILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 267 VVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQG 346
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 347 YLDLAVAEGGRFACGGARPADREV-GFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVY 425
Cdd:cd07120 315 MVERAIAAGAEVVLRGGPVTEGLAkGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVW 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 426 GADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07120 395 TRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
13-482 |
2.39e-119 |
|
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: 357.97 E-value: 2.39e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 13 IDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDstDWSRNTEL-RVRCVRQLRDAMQQHVEELRE 90
Cdd:TIGR01804 2 IDGEYVEDSAGtTREIINPANGEVIATVHAATPEDVERAIAAARRAQG--EWAAMSPMeRGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 91 LTISEVGAPRMltasaqlEGPVGDLSFAADTAESYPW--KQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLA 168
Cdd:TIGR01804 80 LETLDTGKTLQ-------ETIVADMDSGADVFEFFAGlaPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 169 KLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMAD 248
Cdd:TIGR01804 153 KIAPALAAGNAMVFKPSENTPLTALKVAEIMEE-AGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 249 AAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDP 328
Cdd:TIGR01804 232 AAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 329 GTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADREV--GFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGD 406
Cdd:TIGR01804 312 ATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607908 407 DDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-484 |
1.51e-116 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 350.48 E-value: 1.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 30 PATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPrMLTASAQL 108
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSgAERAAVLLKVADLIRARRERLALIETLESGKP-ISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 109 EGPVGDLSFAADTAesypwKQDLGEA-SPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPD 187
Cdd:cd07118 83 EGAADLWRYAASLA-----RTLHGDSyNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 188 TPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFV 267
Cdd:cd07118 158 TSGTTLMLAELLIE-AGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 268 VLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGY 347
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 348 LDLAVAEGGRFACGGARpADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGA 427
Cdd:cd07118 317 VDAGRAEGATLLLGGER-LASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSK 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607908 428 DPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07118 396 DIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
28-485 |
3.49e-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: 346.91 E-value: 3.49e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPrMLTASAQ 107
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKP-LTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 108 LEGPVGDLSFAADTAESYpwkqdLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPD 187
Cdd:cd07109 81 VEAAARYFEYYGGAADKL-----HGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 188 TPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFV 267
Cdd:cd07109 156 APLTALRLAELAEE-AGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 268 VLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDP-NDPGtvCGPLISARQRDRVQG 346
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGlEDPD--LGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 347 YLDLAVAEGGRFACGGARPADR-EVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVY 425
Cdd:cd07109 313 FVARARARGARIVAGGRIAEGApAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVW 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607908 426 GADPQRAARIASRLRVGTVNVN-----GGVwycaDAPFGGYKQSGIGREMGLLGFEEYLEAKLIA 485
Cdd:cd07109 393 TRDGDRALRVARRLRAGQVFVNnygagGGI----ELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
4-484 |
2.19e-113 |
|
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: 343.18 E-value: 2.19e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 4 WGDGISallidGKlsdgragTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFD-STDWSR-NTELRVRCVRQLRDAM 81
Cdd:cd07141 15 WHDSVS-----GK-------TFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlGSPWRTmDASERGRLLNKLADLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 82 QQHVEELRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYpwkqdLGEASPLG----IATRRtlarEAVGVVGAIT 157
Cdd:cd07141 83 ERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKI-----HGKTIPMDgdffTYTRH----EPVGVCGQII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 158 PWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTG 237
Cdd:cd07141 154 PWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKE-AGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 238 STATGRAVMADAAAT-IKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAAT 316
Cdd:cd07141 233 STEVGKLIQQAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 317 MSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGP 396
Cdd:cd07141 313 AKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDK--GYFIQPTVFSDVTDDMRIAKEEIFGP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 397 VLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFE 476
Cdd:cd07141 391 VQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQ 470
|
....*...
gi 15607908 477 EYLEAKLI 484
Cdd:cd07141 471 EYTEVKTV 478
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-484 |
1.73e-112 |
|
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: 340.40 E-value: 1.73e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 13 IDGKLSDGRAGTFPTV-NPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEELRE 90
Cdd:cd07088 2 INGEFVPSSSGETIDVlNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIeRAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 91 LTISEVGAPRMLtASAQLEGPVGDLSFAADTAESYPwkqdlGEASPLGIATRRT-LAREAVGVVGAITPWNFPHQINLAK 169
Cdd:cd07088 80 LIVEEQGKTLSL-ARVEVEFTADYIDYMAEWARRIE-----GEIIPSDRPNENIfIFKVPIGVVAGILPWNFPFFLIARK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 170 LGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADA 249
Cdd:cd07088 154 LAPALVTGNTIVIKPSEETPLNALEFAELVDE-AGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 250 AATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPG 329
Cdd:cd07088 233 AENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 330 TVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPaDREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDA 409
Cdd:cd07088 313 TDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRP-EGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 410 VRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVwycADAPFG---GYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07088 392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINREN---FEAMQGfhaGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
27-484 |
2.14e-112 |
|
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: 339.74 E-value: 2.14e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWSRNTEL-RVRCVRQLRDAMQQHVEELRELTISEVGAP------ 99
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAF--PEWRATTPLeRARMLRELATRLREHAEELALIDALDCGNPvsamlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 100 RMLTASAQLEgpvgdlSFAADTAESYpwkqdlGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNT 179
Cdd:cd07107 79 DVMVAAALLD------YFAGLVTELK------GETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 180 VVLKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLE 259
Cdd:cd07107 147 VVVKPPEQAPLSALRLAELAREV--LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 260 LGGKSAFVV-LDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISA 338
Cdd:cd07107 225 LGGKNALIVfPDADPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 339 RQRDRVQGYLDLAVAEGGRFACGGARPADREV--GFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDS 416
Cdd:cd07107 305 QQYDRVMHYIDSAKREGARLVTGGGRPEGPALegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 417 PYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07107 385 EYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-484 |
4.73e-112 |
|
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: 339.71 E-value: 4.73e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEEL 88
Cdd:cd07559 3 NFINGEWVAPSKGeYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAeRANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAqlegpvgDLSFAAD---------TAESypwkqdlGEASPLGIATRRTLAREAVGVVGAITPW 159
Cdd:cd07559 81 AVAETLDNGKPIRETLAA-------DIPLAIDhfryfagviRAQE-------GSLSEIDEDTLSYHFHEPLGVVGQIIPW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 160 NFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGST 239
Cdd:cd07559 147 NFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL--LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 240 ATGRAVMADAAATIKKVFLELGGKSA--FVVLDDADLAAASAVSAFSACMHA---GQGCAITTRLVVPRARYEEAVAIAA 314
Cdd:cd07559 225 TVGRLIMQYAAENLIPVTLELGGKSPniFFDDAMDADDDFDDKAEEGQLGFAfnqGEVCTCPSRALVQESIYDEFIERAV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 315 ATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGAR--PADREVGFYIEPTVIAGLTNDARVAREE 392
Cdd:cd07559 305 ERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERltLGGLDKGYFYEPTLIKGGNNDMRIFQEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 393 IFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGL 472
Cdd:cd07559 385 IFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHK 464
|
490
....*....|..
gi 15607908 473 LGFEEYLEAKLI 484
Cdd:cd07559 465 MMLDHYQQTKNI 476
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
46-484 |
7.45e-112 |
|
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: 337.58 E-value: 7.45e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 46 DMGRAIEAARRAFdsTDWS-RNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRmLTASAQLEGPVGDLSFAAdtaeS 124
Cdd:cd07104 1 DVDRAYAAAAAAQ--KAWAaTPPQERAAILRKAAEILEERRDEIADWLIRESGSTR-PKAAFEVGAAIAILREAA----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 125 YPwKQDLGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHT 203
Cdd:cd07104 74 LP-RRPEGEILPSDVPGKESMVrRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 204 DFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAF 283
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 284 SACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGa 363
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 364 rpadREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGT 443
Cdd:cd07104 312 ----TYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15607908 444 VNVNGGVWYC-ADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07104 388 VHINDQTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
27-484 |
7.05e-111 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 335.81 E-value: 7.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEELRELTISEVGAPrMLTAS 105
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMeRGRILRKAADLLRERNDEIARLETIDNGKP-IEEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 106 AQLEGPVGDLSFAADTAESYpwkqdLGEASPLG----IATRRtlarEAVGVVGAITPWNFPHQINLAKLGPALAAGNTVV 181
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTL-----SGEHVPLPggsfAYTRR----EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 182 LKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSShALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELG 261
Cdd:cd07090 149 YKPSPFTPLTALLLAEILTE-AGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 262 GKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQR 341
Cdd:cd07090 227 GKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 342 DRVQGYLDLAVAEGGRFACGGARPADREV---GFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPY 418
Cdd:cd07090 307 EKVLGYIESAKQEGAKVLCGGERVVPEDGlenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTY 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607908 419 GLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07090 387 GLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
12-484 |
1.54e-110 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 336.28 E-value: 1.54e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWSRNTEL-RVRCVRQLRDAMQQHVEELR 89
Cdd:PLN02278 28 LIGGKWTDAYDGkTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAF--PSWSKLTASeRSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGAPrMLTASAQLEGPVGDLSFAADTAesypwKQDLGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQINLA 168
Cdd:PLN02278 106 QLMTLEQGKP-LKEAIGEVAYGASFLEYFAEEA-----KRVYGDIIPSPFPDRRLLVlKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 169 KLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMAD 248
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQ-AGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 249 AAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDP 328
Cdd:PLN02278 259 AAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 329 GTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARpADREVGFYiEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDD 408
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKR-HSLGGTFY-EPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607908 409 AVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-482 |
1.67e-110 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 335.37 E-value: 1.67e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAGtFPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELR 89
Cdd:cd07097 4 YIDGEWVAGGDG-EENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSpEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGAPrmltasaqLEGPVGDLSFAADTAESYP---WKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQIN 166
Cdd:cd07097 81 RLLTREEGKT--------LPEARGEVTRAGQIFRYYAgeaLRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:cd07097 153 AWKIAPALAYGNTVVFKPAELTPASAWALVEILEE-AGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPN 326
Cdd:cd07097 232 AAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 327 DPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGD 406
Cdd:cd07097 312 DEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 407 DDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVN---GGVWYcaDAPFGGYKQSGIG-REMGLLGFEEYLEAK 482
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptAGVDY--HVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
11-482 |
4.26e-110 |
|
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: 334.76 E-value: 4.26e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDstDWSRNT--ELRVRCVRQLRDAMQQHVEE 87
Cdd:cd07144 10 LFINNEFVKSSDGeTIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVtgEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 88 LRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYPwkqdlGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINL 167
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQ-----GKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 168 AKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMA 247
Cdd:cd07144 163 WKLAPALAAGNTVVIKPAENTPLSLLYFANLVKE-AGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 248 DAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVA-IAAATMSSIRPGDPN 326
Cdd:cd07144 242 AAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEkFVEHVKQNYKVGSPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 327 DPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGG-ARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDG 405
Cdd:cd07144 322 DDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGeKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607908 406 DDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07144 402 YEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
25-485 |
3.41e-109 |
|
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: 331.22 E-value: 3.41e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 25 FPTVNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRmLT 103
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTpSERERILLKAAEIMERRADDLIDLLIDEGGSTY-GK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 104 ASAQLEGPVGDLSFAADTAESYpwkqdLGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVL 182
Cdd:cd07150 78 AWFETTFTPELLRAAAGECRRV-----RGETLPSDSPGTVSMSvRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 183 KPAPDTPWCAAALGEIiVEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGG 262
Cdd:cd07150 153 KPSEETPVIGLKIAEI-MEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 263 KSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRD 342
Cdd:cd07150 232 KNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 343 RVQGYLDLAVAEGGRFACGGarpadREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSG 422
Cdd:cd07150 312 RIKRQVEDAVAKGAKLLTGG-----KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607908 423 TVYGADPQRAARIASRLRVGTVNVNGGVWYC-ADAPFGGYKQSGIGREMGLLGFEEYLEAKLIA 485
Cdd:cd07150 387 AILTNDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
11-482 |
9.76e-109 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 331.46 E-value: 9.76e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEEL 88
Cdd:PRK13252 9 LYIDGAYVEATSGeTFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI--WAAMTAMeRSRILRRAVDILRERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAqlegpvgDLSFAADTAESY----PWKQdlGEASPLG----IATRRtlarEAVGVVGAITPWN 160
Cdd:PRK13252 87 AALETLDTGKPIQETSVV-------DIVTGADVLEYYaglaPALE--GEQIPLRggsfVYTRR----EPLGVCAGIGAWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 161 FPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSsHALGALLAKDPRVDMISFTGSTA 240
Cdd:PRK13252 154 YPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTE-AGLPDGVFNVVQGD-GRVGAWLTEHPDIAKVSFTGGVP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 241 TGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSI 320
Cdd:PRK13252 232 TGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 321 RPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADREV--GFYIEPTVIAGLTNDARVAREEIFGPVL 398
Cdd:PRK13252 312 RIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFanGAFVAPTVFTDCTDDMTIVREEIFGPVM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 399 TVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEY 478
Cdd:PRK13252 392 SVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHY 471
|
....
gi 15607908 479 LEAK 482
Cdd:PRK13252 472 TQIK 475
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
11-484 |
3.01e-108 |
|
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: 329.87 E-value: 3.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDG-RAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDsTDWSRNTE--LRVRCVRQLRDAMQQHVEE 87
Cdd:cd07143 9 LFINGEFVDSvHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE-TDWGLKVSgsKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 88 LRELTISEVGAPRMLTASaqlegpvGDLSFAADTAESYP-W-KQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQI 165
Cdd:cd07143 88 LASIEALDNGKTFGTAKR-------VDVQASADTFRYYGgWaDKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 166 NLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAV 245
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPE-AGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 246 MADAAAT-IKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGD 324
Cdd:cd07143 240 MEAAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 325 PNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHD 404
Cdd:cd07143 320 PFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNE--GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 405 GDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07143 398 TEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
11-482 |
2.21e-106 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 325.92 E-value: 2.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDG-RAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAF---DSTDWSRNT-ELRVRCVRQLRDAMQQHV 85
Cdd:PLN02467 10 LFIGGEWREPvLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTgAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 86 EELRELTISEVGAPrMLTASAQLEGPVGDLSFAADTAESYPWKQdlGEASPLGIAT-RRTLAREAVGVVGAITPWNFPHQ 164
Cdd:PLN02467 90 SELAKLETLDCGKP-LDEAAWDMDDVAGCFEYYADLAEALDAKQ--KAPVSLPMETfKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 165 INLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRA 244
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICRE-VGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 245 VMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGD 324
Cdd:PLN02467 246 IMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 325 PNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHD 404
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 405 GDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
11-486 |
6.70e-106 |
|
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: 323.68 E-value: 6.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTEL-RVRCVRQLRDAMQQHVEEL 88
Cdd:cd07142 6 LFINGQFVDAASGkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYeRSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAQLEGPVGDLSFAADtaesypWKQDL-GEASPL-GIATRRTLaREAVGVVGAITPWNFPHQIN 166
Cdd:cd07142 86 AALETWDNGKPYEQARYAEVPLAARLFRYYAG------WADKIhGMTLPAdGPHHVYTL-HEPIGVVGQIIPWNFPLLMF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:cd07142 159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAE-AGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAAT-IKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDP 325
Cdd:cd07142 238 QLAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 326 NDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDG 405
Cdd:cd07142 318 FRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSK--GYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 406 DDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLIA 485
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
.
gi 15607908 486 T 486
Cdd:cd07142 476 M 476
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
28-482 |
4.35e-105 |
|
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: 320.92 E-value: 4.35e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPrmltasa 106
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT--WRATTaKERSSLLRKWYNLMMENKDDLARLITLENGKP------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 qLEGPVGDLSFAADTAESYP--WKQDLGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 183
Cdd:TIGR01780 73 -LKEAKGEILYAASFLEWFAeeAKRVYGDTIPSPQSDKRLIViKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 184 PAPDTPWCAAALGEiIVEHTDFPPGVVNIVTSS-SHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGG 262
Cdd:TIGR01780 152 PAEQTPLSALALAR-LAEQAGIPKGVLNVITGSrAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 263 KSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRD 342
Cdd:TIGR01780 231 NAPFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 343 RVQGYLDLAVAEGGRFACGGARpaDREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSG 422
Cdd:TIGR01780 311 KVEKHIADAVEKGAKVVTGGKR--HELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 423 TVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:TIGR01780 389 YFFSRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-471 |
5.41e-105 |
|
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: 321.44 E-value: 5.41e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWsRNTELRVR--CVRQLRDAMQQHVEELR 89
Cdd:cd07086 2 VIGGEWVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE--W-RKVPAPRRgeIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGAPRMltasaqlEGpVGDLSFAADTA-----ESypwKQDLGEASPLGIATRRTLA-REAVGVVGAITPWNFPH 163
Cdd:cd07086 79 RLVSLEMGKILP-------EG-LGEVQEMIDICdyavgLS---RMLYGLTIPSERPGHRLMEqWNPLGVVGVITAFNFPV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 164 QINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEII---VEHTDFPPGVVNIVTSSShALGALLAKDPRVDMISFTGSTA 240
Cdd:cd07086 148 AVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILaevLEKNGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 241 TGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSI 320
Cdd:cd07086 227 VGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 321 RPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTV 400
Cdd:cd07086 307 RIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYV 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607908 401 IAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARI--ASRLRVGTVNVNGGvwyCADA----PFGGYKQSGIGREMG 471
Cdd:cd07086 387 IKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIP---TSGAeiggAFGGEKETGGGRESG 460
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-485 |
6.40e-105 |
|
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: 320.45 E-value: 6.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 25 FPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSrNTELRVRC--VRQLRDAMQQHVEELRELTISEVGAPrML 102
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MS-NLPAYKRYkiLMKVAELIERRKEELAKLLTIEVGKP-IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 103 TASAQLEGPVGDLSFAADTA-----ESYPwkQDLGEASPLGIATRRtlaREAVGVVGAITPWNFPHQINLAKLGPALAAG 177
Cdd:cd07145 77 QSRVEVERTIRLFKLAAEEAkvlrgETIP--VDAYEYNERRIAFTV---REPIGVVGAITPFNFPANLFAHKIAPAIAVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 178 NTVVLKPAPDTPWCAAALGEIIvEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVF 257
Cdd:cd07145 152 NSVVVKPSSNTPLTAIELAKIL-EEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 258 LELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLIS 337
Cdd:cd07145 231 LELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 338 ARQRDRVQGYLDLAVAEGGRFACGGARPAdrevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSP 417
Cdd:cd07145 311 PEAVERMENLVNDAVEKGGKILYGGKRDE----GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTE 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 418 YGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADA-PFGGYKQSGIGREMGLLGFEEYLEAKLIA 485
Cdd:cd07145 387 YGLQASVFTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
15-484 |
7.29e-105 |
|
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: 320.79 E-value: 7.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 15 GKLSDGRA-GTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAfdSTDWS-RNTELRVRCVRQLRDAMQQHVEELRELT 92
Cdd:cd07151 1 GEWRDGTSeRTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAaTLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 93 ISEVGAPRmLTASAQLEGPVGDLSFAAdtaeSYPWKQDlGEASPLGIATRRT-LAREAVGVVGAITPWNFPHQINLAKLG 171
Cdd:cd07151 79 IRESGSTR-IKANIEWGAAMAITREAA----TFPLRME-GRILPSDVPGKENrVYREPLGVVGVISPWNFPLHLSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 172 PALAAGNTVVLKPAPDTPWCAAALGEIIVEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAA 251
Cdd:cd07151 153 PALALGNAVVLKPASDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 252 TIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTV 331
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 332 CGPLISARQRDRVQGYLDLAVAEGGRFACGGARpadreVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVR 411
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGGEA-----EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607908 412 IANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGG-VWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQpVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-482 |
8.52e-105 |
|
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: 320.83 E-value: 8.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAG-TFPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFDstDWSRNTE-LRVRCVRQLRDAMQQHVEEL 88
Cdd:cd07131 2 YIGGEWVDSASGeTFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFP--EWRKVPApRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAQLEGpVGDLSFAADTAesypwKQDLGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQINL 167
Cdd:cd07131 80 ARLVTREMGKPLAEGRGDVQEA-IDMAQYAAGEG-----RRLFGETVPSELPNKDAMTrRQPIGVVALITPWNFPVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 168 AKLGPALAAGNTVVLKPAPDTPWCAAALGEIiVEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMA 247
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVEL-FAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 248 DAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPND 327
Cdd:cd07131 233 TCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 328 PGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARP--ADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDG 405
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 406 DDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGvwyCADA----PFGGYKQSGIG-REMGLLGFEEYLE 480
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAP---TIGAevhlPFGGVKKSGNGhREAGTTALDAFTE 469
|
..
gi 15607908 481 AK 482
Cdd:cd07131 470 WK 471
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
11-484 |
4.34e-102 |
|
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: 314.01 E-value: 4.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEEL 88
Cdd:cd07117 3 LFINGEWVKGSSGeTIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAeRANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAqlegpvgDLSFAADTAESYP--WKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQIN 166
Cdd:cd07117 81 AMVETLDNGKPIRETRAV-------DIPLAADHFRYFAgvIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:cd07117 154 AWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV--LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPN 326
Cdd:cd07117 232 IAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 327 DPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGAR--PADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHD 404
Cdd:cd07117 312 DPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 405 GDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07117 392 TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
10-482 |
1.58e-101 |
|
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: 312.45 E-value: 1.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 10 ALLIDGKLSDGRAGTFPTV-NPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTELRVRCVRQLRDAMQQHVEEL 88
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDItNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYPwKQDLGEASPLGIATRRT--LAREAVGVVGAITPWNFPHQIN 166
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKIN-GETLAPSIPSMQGERYTafTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSShALGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKE-AGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPN 326
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 327 DPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPaDREvGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGD 406
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEAL-AGE-GYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607908 407 DDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELK 471
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
27-474 |
3.05e-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: 311.22 E-value: 3.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWsRNTELRVR--CVRQLRDAMQQHVEELRELTISEVG-APRmlT 103
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEW-AATPARERgkLLARIADALEARSEELARLLALETGnALR--T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 104 ASaqlegpVGDLSFAADTAESYPW--KQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVV 181
Cdd:cd07108 76 QA------RPEAAVLADLFRYFGGlaGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 182 LKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELG 261
Cdd:cd07108 150 LKAAEDAPLAVLLLAEILAQV--LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 262 GKS-AFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQ 340
Cdd:cd07108 228 GKSpMIVFPDADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 341 RDRVQGYLDLAVAE-GGRFACGGARPADREV--GFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSP 417
Cdd:cd07108 308 FAKVCGYIDLGLSTsGATVLRGGPLPGEGPLadGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSH 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607908 418 YGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLG 474
Cdd:cd07108 388 YGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEG 444
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-467 |
2.12e-99 |
|
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: 308.00 E-value: 2.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRaGTFPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEEL 88
Cdd:cd07124 35 LVIGGKEVRTE-EKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPpEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMltasaqlEGpVGDLSFAADTAESYPWKQDLGEASPLGIAT--RRTLAREAVGVVGAITPWNFPHQIN 166
Cdd:cd07124 112 AAWMVLEVGKNWA-------EA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPgeDNRYVYRPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEE-AGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAAT------IKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSI 320
Cdd:cd07124 263 ERAAKVqpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 321 RPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGgRFACGGARPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTV 400
Cdd:cd07124 343 KVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAV 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607908 401 IAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGvwyCADA-----PFGGYKQSGIG 467
Cdd:cd07124 422 IKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRK---ITGAlvgrqPFGGFKMSGTG 490
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-486 |
4.60e-99 |
|
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: 305.30 E-value: 4.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAfdSTDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMlTASA 106
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA--QRAWAALGvEGRAQRLLRWKRALADHADELAELLHAETGKPRA-DAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 QLEGPVGDLSFAADTAESYPWKQDLGeASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAP 186
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVLAPRKVP-TGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 187 DTPWCAAALGEIIVEhTDFPPGVVNIVTSSShALGALLAkDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAF 266
Cdd:cd07099 157 VTPLVGELLAEAWAA-AGPPQGVLQVVTGDG-ATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 267 VVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQG 346
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 347 YLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYG 426
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGG--GPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607908 427 ADPQRAARIASRLRVGTVNVNGGVWY--CADAPFGGYKQSGIGREMGLLGFEEYLEAKLIAT 486
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDVLLTagIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-482 |
1.99e-98 |
|
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: 300.69 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 52 EAARRAFDstDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRmLTASAQLEGPVGDLSFAADTAESYPWKQD 130
Cdd:cd06534 1 AAARAAFK--AWAALPpAERAAILRKIADLLEERREELAALETLETGKPI-EEALGEVARAIDTFRYAAGLADKLGGPEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 131 LGEASPLGIATRRtlarEAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVV 210
Cdd:cd06534 78 PSPDPGGEAYVRR----EPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQE-AGLPPGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 211 NIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAG 290
Cdd:cd06534 153 NVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 291 QGCAITTRLVVPRARYEEAVAiaaatmssirpgdpndpgtvcgplisarqrdrvqgyldlavaeggRFAcggarpadrev 370
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVE---------------------------------------------KLV----------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 371 gfyiepTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGG- 449
Cdd:cd06534 257 ------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSs 330
|
410 420 430
....*....|....*....|....*....|...
gi 15607908 450 VWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd06534 331 IGVGPEAPFGGVKNSGIGREGGPYGLEEYTRTK 363
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
49-484 |
1.86e-97 |
|
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: 300.53 E-value: 1.86e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 49 RAIEAARRAFdsTDWsRNTEL--RVRCVRQLRDAMQQHVEELRELTISEVGAPRmltasAQLEGPVgDLS-----FAADT 121
Cdd:cd07100 3 AALDRAHAAF--LAW-RKTSFaeRAALLRKLADLLRERKDELARLITLEMGKPI-----AEARAEV-EKCawicrYYAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 122 AESY----PWKQDLGEASplgiatrrtLAREAVGVVGAITPWNFPH-QInlAK-LGPALAAGNTVVLKPAPDTPWCAAAL 195
Cdd:cd07100 74 AEAFladePIETDAGKAY---------VRYEPLGVVLGIMPWNFPFwQV--FRfAAPNLMAGNTVLLKHASNVPGCALAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 196 GEIIVEhTDFPPGVVNIVTSSSHALGALLAkDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLA 275
Cdd:cd07100 143 EELFRE-AGFPEGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 276 AASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEG 355
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 356 GRFACGGARPaDREvGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARI 435
Cdd:cd07100 301 ATLLLGGKRP-DGP-GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERV 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 15607908 436 ASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07100 379 ARRLEAGMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-484 |
2.91e-96 |
|
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: 298.36 E-value: 2.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 25 FPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdwSRNTELRVRCvRQLRDA---MQQHVEELRELTISEVGAPrM 101
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKE---MKSLPAYERA-EILERAaqlLEERREEFARTIALEAGKP-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 102 LTASAQLEGPVGDLSFAADTA-----ESYPwkqdlGEASPLGIATRRTLAREAVGVVGAITPWNFPhqINLA--KLGPAL 174
Cdd:cd07149 76 KDARKEVDRAIETLRLSAEEAkrlagETIP-----FDASPGGEGRIGFTIREPIGVVAAITPFNFP--LNLVahKVGPAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 175 AAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMAdaAATIK 254
Cdd:cd07149 149 AAGNAVVLKPASQTPLSALKLAELLLE-AGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIAR--KAGLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 255 KVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGP 334
Cdd:cd07149 226 KVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 335 LISARQRDRVQGYLDLAVAEGGRFACGGARpadreVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIAN 414
Cdd:cd07149 306 MISEAEAERIEEWVEEAVEGGARLLTGGKR-----DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAN 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607908 415 DSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADA-PFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07149 381 DSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
11-487 |
8.37e-95 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 297.10 E-value: 8.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTEL-RVRCVRQLRDAMQQHVEEL 88
Cdd:PLN02466 60 LLINGQFVDAASGkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYeRSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYpwkqdLGEASPL-GIATRRTLaREAVGVVGAITPWNFPHQINL 167
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKI-----HGLTVPAdGPHHVQTL-HEPIGVAGQIIPWNFPLLMFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 168 AKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMA 247
Cdd:PLN02466 214 WKVGPALACGNTIVLKTAEQTPLSALYAAKLLHE-AGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 248 DAA-ATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPN 326
Cdd:PLN02466 293 LAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPF 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 327 DPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGD 406
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSK--GYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 407 DDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLIAT 486
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 530
|
.
gi 15607908 487 A 487
Cdd:PLN02466 531 P 531
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
11-487 |
3.62e-93 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 291.72 E-value: 3.62e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTEL-RVRCVRQLRDAMQQHVEEL 88
Cdd:PLN02766 23 LFINGEFVDAASGkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFeRGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYPwkqdlGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLA 168
Cdd:PLN02766 103 AALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIH-----GETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 169 KLGPALAAGNTVVLKPAPDTPWCAAALGEIiVEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVM-A 247
Cdd:PLN02766 178 KVAPALAAGCTMVVKPAEQTPLSALFYAHL-AKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMqA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 248 DAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPND 327
Cdd:PLN02766 257 AATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 328 PGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDD 407
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDK--GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 408 DAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLIATA 487
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
1-484 |
7.66e-92 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 288.33 E-value: 7.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 1 MALWGDGISALLIDGKL---------SDGRagTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTELRV 71
Cdd:PRK09847 6 LAYWQDKALSLAIENRLfingeytaaAENE--TFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 72 RCV-RQLRDAMQQHVEELRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESYpwkqdLGEASPLGIATRRTLAREAV 150
Cdd:PRK09847 84 KAVlNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKV-----YGEVATTSSHELAMIVREPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 151 GVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRV 230
Cdd:PRK09847 159 GVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKE-AGLPDGVLNVVTGFGHEAGQALSRHNDI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 231 DMISFTGSTATGRAVMADAA-ATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMH-AGQGCAITTRLVVPRARYEE 308
Cdd:PRK09847 238 DAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYnQGQVCIAGTRLLLEESIADE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 309 AVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGgarpadREVGF--YIEPTVIAGLTNDA 386
Cdd:PRK09847 318 FLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG------RNAGLaaAIGPTIFVDVDPNA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 387 RVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGI 466
Cdd:PRK09847 392 SLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGN 471
|
490
....*....|....*...
gi 15607908 467 GREMGLLGFEEYLEAKLI 484
Cdd:PRK09847 472 GRDKSLHALEKFTELKTI 489
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
10-482 |
1.05e-91 |
|
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: 287.37 E-value: 1.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 10 ALLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVee 87
Cdd:cd07111 23 GHFINGKWVKPENRkSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPgHVRARHLYRIARHIQKHQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 88 lRELTISEvgapRMLTASAQLEGPVGDLSFAADTAESYP-WKQDLGEASPlgiatrrtlAREAVGVVGAITPWNFPHQIN 166
Cdd:cd07111 99 -RLFAVLE----SLDNGKPIRESRDCDIPLVARHFYHHAgWAQLLDTELA---------GWKPVGVVGQIVPWNFPLLML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHaLGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:cd07111 165 AWKICPALAMGNTVVLKPAEYTPLTALLFAEICAE-AGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPN 326
Cdd:cd07111 243 RATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 327 DPGTVCGPLISARQRDRVQGYLDLAVAEGG-RFACGGARPADrevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDG 405
Cdd:cd07111 323 DKAIDMGAIVDPAQLKRIRELVEEGRAEGAdVFQPGADLPSK---GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRT 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607908 406 DDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07111 400 AKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
25-483 |
1.08e-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: 281.06 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 25 FPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTdwsRNTEL--RVRCVRQLRDAMQQHVEELRELTISEVGAPRML 102
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPM---RALPAhrRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 103 tASAQLEGPVGDLSFAADTAEsypwKQDlGEASPLGI----ATRRTLARE-AVGVVGAITPWNFPhqINLA--KLGPALA 175
Cdd:cd07147 78 -ARGEVARAIDTFRIAAEEAT----RIY-GEVLPLDIsargEGRQGLVRRfPIGPVSAITPFNFP--LNLVahKVAPAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 176 AGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSsHALGALLAKDPRVDMISFTGSTATGRAVMADAAAtiKK 255
Cdd:cd07147 150 AGCPFVLKPASRTPLSALILGEVLAE-TGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 256 VFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPL 335
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 336 ISARQRDRVQGYLDLAVAEGGRFACGGARPadrevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIAND 415
Cdd:cd07147 306 ISESEAERVEGWVNEAVDAGAKLLTGGKRD-----GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVND 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 416 SPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADA-PFGGYKQSGIGREMGLLGFEEYLEAKL 483
Cdd:cd07147 381 SKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVDHmPYGGVKDSGIGREGVRYAIEEMTEPRL 449
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-484 |
4.53e-89 |
|
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: 279.70 E-value: 4.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDwSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMlTASAQ 107
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRR-ALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIK-DARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 108 LEGPVGDLSFAADTAesypwKQDLGEASPLGIATRRT-----LAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVL 182
Cdd:cd07094 82 VDRAIDTLRLAAEEA-----ERIRGEEIPLDATQGSDnrlawTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 183 KPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAatIKKVFLELGG 262
Cdd:cd07094 157 KPASKTPLSALELAKILVE-AGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 263 KSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRD 342
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 343 RVQGYLDLAVAEGGRFACGGARPadrevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSG 422
Cdd:cd07094 314 RVERWVEEAVEAGARLLCGGERD-----GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607908 423 TVYGADPQRAARIASRLRVGTVNVNGGVWYCADA-PFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07094 389 GIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
11-484 |
9.96e-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: 277.07 E-value: 9.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSR-NTELRVRCVRQLRDAMQQHVEEL 88
Cdd:cd07140 8 LFINGEFVDAEGGkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKmNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTasaqLEGPVGdlsFAADTAESYP-WKQDL-GEASPLGIA-TRRTLA---REAVGVVGAITPWNFP 162
Cdd:cd07140 88 ATIESLDSGAVYTLA----LKTHVG---MSIQTFRYFAgWCDKIqGKTIPINQArPNRNLTltkREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 163 HQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATG 242
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVK-AGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 243 RAVMADAA-ATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIR 321
Cdd:cd07140 240 KHIMKSCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 322 PGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARpADREvGFYIEPTVIAGLTNDARVAREEIFGPVLTVI 401
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQ-VDRP-GFFFEPTVFTDVEDHMFIAKEESFGPIMIIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 402 A-HDGDDDAV-RIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNggVWYCAD--APFGGYKQSGIGREMGLLGFEE 477
Cdd:cd07140 398 KfDDGDVDGVlQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDvaAPFGGFKQSGFGKDLGEEALNE 475
|
....*..
gi 15607908 478 YLEAKLI 484
Cdd:cd07140 476 YLKTKTV 482
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
12-482 |
2.22e-87 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 276.40 E-value: 2.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELR 89
Cdd:PRK11241 14 LINGEWLDANNGeVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTaKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGAPrmlTASAQlegpvGDLSFAADTAESYP--WKQDLGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQIN 166
Cdd:PRK11241 92 RLMTLEQGKP---LAEAK-----GEISYAASFIEWFAeeGKRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAMI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIiVEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:PRK11241 164 TRKAGPALAAGCTMVLKPASQTPFSALALAEL-AIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPN 326
Cdd:PRK11241 243 EQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 327 DPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGaRPADREvGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGD 406
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGG-KAHELG-GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607908 407 DDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
12-486 |
1.10e-85 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 272.91 E-value: 1.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRaGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAfdSTDWSRNT-ELRVRCVRQLRDAMQQHVEELRE 90
Cdd:PRK09407 22 LTARVDGAAG-PTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPvRERAAVLLRFHDLVLENREELLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 91 LTISEVGAPRmltASAQLEgpVGDLSFAAD----TAESYpwkqdLGE---ASPLGIATRRTLAREAVGVVGAITPWNFPH 163
Cdd:PRK09407 99 LVQLETGKAR---RHAFEE--VLDVALTARyyarRAPKL-----LAPrrrAGALPVLTKTTELRQPKGVVGVISPWNYPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 164 QINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAkdPRVDMISFTGSTATGR 243
Cdd:PRK09407 169 TLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYE-AGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 244 AVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPG 323
Cdd:PRK09407 246 VLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 324 DPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGG-ARPadrEVG--FYiEPTVIAGLTNDARVAREEIFGPVLTV 400
Cdd:PRK09407 326 AGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGkARP---DLGplFY-EPTVLTGVTPDMELAREETFGPVVSV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 401 IAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGG---VWYCADAPFGGYKQSGIGREMGLLGFEE 477
Cdd:PRK09407 402 YPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyaaAWGSVDAPMGGMKDSGLGRRHGAEGLLK 481
|
....*....
gi 15607908 478 YLEAKLIAT 486
Cdd:PRK09407 482 YTESQTIAT 490
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
34-471 |
5.33e-84 |
|
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: 266.08 E-value: 5.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 34 EVLGVAADADAEDMGRAIEAARRAfdSTDW-SRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMlTASAQLEGPV 112
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA--QRAWaATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRP-KAGFEVGAAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 113 GDLSFAADTAeSYPWKQDLGEASP-LGIATRRtlareAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWC 191
Cdd:cd07152 79 GELHEAAGLP-TQPQGEILPSAPGrLSLARRV-----PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 192 AAALGEIIVEHTDFPPGVVNIVTSSSHAlGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDD 271
Cdd:cd07152 153 GGVVIARLFEEAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 272 ADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLA 351
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 352 VAEGGRFACGGARPadrevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQR 431
Cdd:cd07152 312 VAAGARLEAGGTYD-----GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGR 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15607908 432 AARIASRLRVGTVNVNGG-VWYCADAPFGGYKQSGIGREMG 471
Cdd:cd07152 387 AMALADRLRTGMLHINDQtVNDEPHNPFGGMGASGNGSRFG 427
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-482 |
8.25e-84 |
|
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: 266.03 E-value: 8.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMLTASa 106
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPlEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 QLEGPVGDLSFAADTAESYPWKQDLGEASPLgiatRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAP 186
Cdd:cd07102 78 EIRGMLERARYMISIAEEALADIRVPEKDGF----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 187 DTPWCAAALGEIIVEhTDFPPGVVNIVTSSsHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAF 266
Cdd:cd07102 154 QTPLCGERFAAAFAE-AGLPEGVFQVLHLS-HETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 267 VVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQG 346
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 347 YLDLAVAEGGRFACGGAR-PADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVY 425
Cdd:cd07102 312 QIADAIAKGARALIDGALfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607908 426 GADPQRAARIASRLRVGTVNVNggvwyCADA-----PFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMN-----RCDYldpalAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-469 |
5.47e-83 |
|
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: 264.43 E-value: 5.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL--RVRCVRQLRDAMQQHVEELR 89
Cdd:cd07082 5 LINGEWKESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRG--WWPTMPLeeRIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGAPRmltASAQLEgpvgdlsFAA------DTAESYpwKQDLGEASPLGI--ATRRTLA---REAVGVVGAITP 158
Cdd:cd07082 83 NLLMWEIGKTL---KDALKE-------VDRtidyirDTIEEL--KRLDGDSLPGDWfpGTKGKIAqvrREPLGVVLAIGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 159 WNFPhqINLA--KLGPALAAGNTVVLKPAPDTPWCAAALGEIiVEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFT 236
Cdd:cd07082 151 FNYP--LNLTvsKLIPALIMGNTVVFKPATQGVLLGIPLAEA-FHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 237 GSTATGRAVMAdaAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAAT 316
Cdd:cd07082 228 GSTEVGNRLKK--QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 317 MSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGarpaDREVGFYIEPTVIAGLTNDARVAREEIFGP 396
Cdd:cd07082 306 VAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG----GREGGNLIYPTLLDPVTPDMRLAWEEPFGP 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607908 397 VLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGgvwYCADA----PFGGYKQSGIGRE 469
Cdd:cd07082 382 VLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS---KCQRGpdhfPFLGRKDSGIGTQ 455
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
30-486 |
6.22e-83 |
|
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: 263.79 E-value: 6.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 30 PATEEVLGVAADADAEDMGRAIEAARRAfdSTDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRmltASAQL 108
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPfAERAAVFLRFHDLVLERRDELLDLIQLETGKAR---RHAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 109 EgpVGDL----SFAADTAESY--PWKQdlgeASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVL 182
Cdd:cd07101 78 E--VLDVaivaRYYARRAERLlkPRRR----RGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 183 KPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKdpRVDMISFTGSTATGRAVMADAAATIKKVFLELGG 262
Cdd:cd07101 152 KPDSQTALTALWAVELLIE-AGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 263 KSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRD 342
Cdd:cd07101 229 KNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 343 RVQGYLDLAVAEGGRFACGG-ARPadrEVG-FYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGL 420
Cdd:cd07101 309 RVTAHVDDAVAKGATVLAGGrARP---DLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 421 SGTVYGADPQRAARIASRLRVGTVNVNGG---VWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLIAT 486
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNEGyaaAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
25-482 |
2.60e-81 |
|
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: 260.46 E-value: 2.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 25 FPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEELRELTISEVGAPRMLT 103
Cdd:cd07116 18 FDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAeRANILNKIADRMEANLEMLAVAETWDNGKPVRET 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 104 ASAQLEGPVGDLSFAADT--AESypwkqdlGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVV 181
Cdd:cd07116 96 LAADIPLAIDHFRYFAGCirAQE-------GSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 182 LKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELG 261
Cdd:cd07116 169 LKPAEQTPASILVLMELIGDL--LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 262 GKSA--FVVLDDADLAAASAVSAFSACMHA---GQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLI 336
Cdd:cd07116 247 GKSPniFFADVMDADDAFFDKALEGFVMFAlnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 337 SARQRDRVQGYLDLAVAEGGRFACGGARP--ADREVGFYIEPTVIAGlTNDARVAREEIFGPVLTVIAHDGDDDAVRIAN 414
Cdd:cd07116 327 SLEQLEKILSYIDIGKEEGAEVLTGGERNelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIAN 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 415 DSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07116 406 DTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-475 |
5.00e-80 |
|
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: 256.46 E-value: 5.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMltasa 106
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQ--REWAKTSfAERRKVLRSLLKYILENQEEICRVACRDTGKTMV----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 qlegpvgDLSFAA--DTAESYPWKQDLGE--------ASPLGIATRRTLAR-EAVGVVGAITPWNFP-HQInlakLGPAL 174
Cdd:cd07098 74 -------DASLGEilVTCEKIRWTLKHGEkalrpesrPGGLLMFYKRARVEyEPLGVVGAIVSWNYPfHNL----LGPII 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 175 AA---GNTVVLKPAPDTPWCAAALGEII---VEHTDFPPGVVNIVTSSSHAlGALLAKDPRVDMISFTGSTATGRAVMAD 248
Cdd:cd07098 143 AAlfaGNAIVVKVSEQVAWSSGFFLSIIrecLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 249 AAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDP 328
Cdd:cd07098 222 AAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 329 GTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPADRE--VGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGD 406
Cdd:cd07098 302 DVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607908 407 DDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVN--GGVWYCADAPFGGYKQSGIGR---EMGLLGF 475
Cdd:cd07098 382 EEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfGVNYYVQQLPFGGVKGSGFGRfagEEGLRGL 455
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
49-484 |
5.21e-80 |
|
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: 255.58 E-value: 5.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 49 RAIEAARRAFDStdWSR--NTElRVRCVRQLRDAMQQHVEELRELTISEVGAPRmLTASAQLEGPVGDLSFAADTAESYP 126
Cdd:cd07105 4 QAVEAAAAAFPA--WSKtpPSE-RRDILLKAADLLESRRDEFIEAMMEETGATA-AWAGFNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 127 wkqdlGEASPLGIATRRTLA-REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDF 205
Cdd:cd07105 80 -----GGSIPSDKPGTLAMVvKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHE-AGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 206 PPGVVNIVTSS---SHALGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSA 282
Cdd:cd07105 154 PKGVLNVVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 283 FSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDpndpgTVCGPLISARQRDRVQGYLDLAVAEGGRFACGG 362
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 363 aRPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVG 442
Cdd:cd07105 309 -LADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15607908 443 TVNVNGG-VWYCADAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07105 388 AVHINGMtVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
11-485 |
1.43e-78 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 254.09 E-value: 1.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGrAGTFPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFDStdWsRNTELRVRCVRQLRDA--MQQHVEE 87
Cdd:PRK03137 39 LIIGGERITT-EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET--W-KKWSPEDRARILLRAAaiIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 88 LRELTISEVGAPrmlTASAqlegpvgdlsfAADTAES-----YPWKQ--DLGEASPLgiaTRR-----TLAREAVGVVGA 155
Cdd:PRK03137 115 FSAWLVKEAGKP---WAEA-----------DADTAEAidfleYYARQmlKLADGKPV---ESRpgehnRYFYIPLGVGVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 156 ITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIvEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISF 235
Cdd:PRK03137 178 ISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVL-EEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 236 TGSTATGRAVMADAAAT------IKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEA 309
Cdd:PRK03137 257 TGSREVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 310 VAIAAATMSSIRPGDPNDPGTVcGPLISARQRDRVQGYLDLAVAEGgRFACGGARpaDREVGFYIEPTVIAGLTNDARVA 389
Cdd:PRK03137 337 LEKVVELTKELTVGNPEDNAYM-GPVINQASFDKIMSYIEIGKEEG-RLVLGGEG--DDSKGYFIQPTIFADVDPKARIM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 390 REEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGvwyCADA-----PFGGYKQS 464
Cdd:PRK03137 413 QEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRG---CTGAivgyhPFGGFNMS 489
|
490 500
....*....|....*....|....*
gi 15607908 465 GIGREMG----LLGFeeyLEAKLIA 485
Cdd:PRK03137 490 GTDSKAGgpdyLLLF---LQAKTVS 511
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
27-482 |
4.52e-75 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 243.49 E-value: 4.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFDSTdwsRNT--ELRVRCVRQLRDAMQQHVEELRELTISEVGAPrMLTA 104
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDY---RTTtfAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 105 SAQLEGPVGDLSFAADTAESYPWKQDlgeASPLGIATRRTLAR-EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 183
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADEP---ADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 184 PAPDTPWCAAALGEIIvEHTDFPPGVVNIVTSSSHALGALLaKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGK 263
Cdd:PRK09406 158 HASNVPQTALYLADLF-RRAGFPDGCFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 264 SAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDR 343
Cdd:PRK09406 236 DPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 344 VQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGT 423
Cdd:PRK09406 316 VEKQVDDAVAAGATILCGGKRPDGP--GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSN 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 424 VYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:PRK09406 394 AWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
75-484 |
5.63e-75 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 241.56 E-value: 5.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 75 RQLRDAMQQHVEELRELTISEVGAPRMLtasAQLEgpvgdLSFAAD----TAEsypWKQDL-GEAsplgIATRRT----- 144
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQL---AEVE-----VAFTADyidyMAE---WARRYeGEI----IQSDRPgenil 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 145 LAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIiVEHTDFPPGVVNIVTSSSHALGALL 224
Cdd:PRK10090 67 LFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKI-VDEIGLPKGVFNLVLGRGETVGQEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 225 AKDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRA 304
Cdd:PRK10090 146 AGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 305 RYEEAVAIAAATMSSIRPGDPNDPGTV-CGPLISARQRDRVQGYLDLAVAEGGRFACGGARpaDREVGFYIEPTVIAGLT 383
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKA--VEGKGYYYPPTLLLDVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 384 NDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPFGGYKQ 463
Cdd:PRK10090 304 QEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRK 383
|
410 420
....*....|....*....|.
gi 15607908 464 SGIGREMGLLGFEEYLEAKLI 484
Cdd:PRK10090 384 SGIGGADGKHGLHEYLQTQVV 404
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-467 |
3.77e-74 |
|
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: 240.72 E-value: 3.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAFDSTDWSRNTELRVRCVRQLrdamQQHVEELRELTISEVGAPRMLTAsAQ 107
Cdd:cd07146 4 RNPYTGEVVGTVPAGTEEALREALALAASYRSTLTRYQRSAILNKAAALL----EARREEFARLITLESGLCLKDTR-YE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 108 LEGPVGDLSFAADTAesypwKQDLGEASPLGIATRR------TLaREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVV 181
Cdd:cd07146 79 VGRAADVLRFAAAEA-----LRDDGESFSCDLTANGkarkifTL-REPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 182 LKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMAdaAATIKKVFLELG 261
Cdd:cd07146 153 LKPSEKTPLSAIYLADLLYE-AGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAA--TAGYKRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 262 GKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQR 341
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 342 DRVQGYLDLAVAEGGRFACGGARpadreVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLS 421
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQR-----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLS 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15607908 422 GTVYGADPQRAARIASRLRVGTVNVNGGVWYCAD-APFGGYKQSGIG 467
Cdd:cd07146 385 SGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLG 431
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
11-471 |
1.09e-71 |
|
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: 236.30 E-value: 1.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDgRAGTFPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFDStdWsRNTELRVRC--VRQLRDAMQQHVEE 87
Cdd:TIGR01237 35 LVINGERVE-TENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA--W-KKTDPEERAaiLFKAAAIVRRRRHE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 88 LRELTISEVGAPrMLTASAQLEGPVGDLSFAADTAESYpwkqDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINL 167
Cdd:TIGR01237 111 FSALLVKEVGKP-WNEADAEVAEAIDFMEYYARQMIEL----AKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 168 AKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMA 247
Cdd:TIGR01237 186 GMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEE-AGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 248 DAAAT------IKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIR 321
Cdd:TIGR01237 265 RAAKVqpgqkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 322 PGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEgGRFACGGArpADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVI 401
Cdd:TIGR01237 345 VGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAE-GRLVSGGC--GDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFI 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607908 402 AHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGvwyCADA-----PFGGYKQSGIGREMG 471
Cdd:TIGR01237 422 RASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRN---ITGAivgyqPFGGFKMSGTDSKAG 493
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
11-467 |
1.86e-71 |
|
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: 234.72 E-value: 1.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEEL 88
Cdd:cd07085 3 LFINGEWVESKTTeWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLkRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRmltasAQLEGPVGDLSFAADTAESYPwKQDLGEASP---LGIATRRTlaREAVGVVGAITPWNFPHQI 165
Cdd:cd07085 81 ARLITLEHGKTL-----ADARGDVLRGLEVVEFACSIP-HLLKGEYLEnvaRGIDTYSY--RQPLGVVAGITPFNFPAMI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 166 NLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAkDPRVDMISFTGSTATGRAV 245
Cdd:cd07085 153 PLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQE-AGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 246 MADAAATIKKVFLELGGK--------------------SAFVVlddadlaaasavsafsacmhAGQGC-AITTRLVVPRA 304
Cdd:cd07085 231 YERAAANGKRVQALGGAKnhavvmpdadleqtanalvgAAFGA--------------------AGQRCmALSVAVAVGDE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 305 rYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGG--ARPADREVGFYIEPTVIAGL 382
Cdd:cd07085 291 -ADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgVKVPGYENGNFVGPTILDNV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 383 TNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGV-----WYcadaP 457
Cdd:cd07085 370 TPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpvplaFF----S 445
|
490
....*....|
gi 15607908 458 FGGYKQSGIG 467
Cdd:cd07085 446 FGGWKGSFFG 455
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
20-471 |
1.97e-67 |
|
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: 224.01 E-value: 1.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 20 GRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWsRNTELRVR--CVRQLRDAMQQHVEELRELTISEVG 97
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAF--KEW-RDVPAPKRgeIVRQIGDALRKKKEALGKLVSLEMG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 98 APRmltasAQLEGPVGDLSFAADTAesypwkqdLGEASPLG---IATRRTLAR-----EAVGVVGAITPWNFP---HQIN 166
Cdd:cd07130 86 KIL-----PEGLGEVQEMIDICDFA--------VGLSRQLYgltIPSERPGHRmmeqwNPLGVVGVITAFNFPvavWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKlgpALAAGNTVVLKPAPDTPWCAAALGEII---VEHTDFPPGVVNIVTSSShALGALLAKDPRVDMISFTGSTATGR 243
Cdd:cd07130 153 AAI---ALVCGNVVVWKPSPTTPLTAIAVTKIVarvLEKNGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 244 AVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPG 323
Cdd:cd07130 229 QVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 324 DPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARpADREvGFYIEPTVIAGLtNDARVAREEIFGPVLTVIAH 403
Cdd:cd07130 309 DPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKV-IDGP-GNYVEPTIVEGL-SDAPIVKEETFAPILYVLKF 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 404 DGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRL--RVGTVNVN--------GGVwycadapFGGYKQSGIGREMG 471
Cdd:cd07130 386 DTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNigtsgaeiGGA-------FGGEKETGGGRESG 456
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-478 |
5.95e-66 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 219.73 E-value: 5.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 27 TVNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPrMLTAS 105
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGF--RDWRETNiDYRAQKLRDIGKALRARSEEMAQMITREMGKP-INQAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 106 AQLegpvgdlsfaADTAESYPWkqdLGEASPLGIATRRTLA--REAV------GVVGAITPWNFPHQINLAKLGPALAAG 177
Cdd:PRK13968 88 AEV----------AKSANLCDW---YAEHGPAMLKAEPTLVenQQAVieyrplGTILAIMPWNFPLWQVMRGAVPILLAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 178 NTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLaKDPRVDMISFTGSTATGRAVMADAAATIKKVF 257
Cdd:PRK13968 155 NGYLLKHAPNVMGCAQLIAQVFKD-AGIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRAGAAIGAQAGAALKKCV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 258 LELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVpraryEEAVAIA-----AATMSSIRPGDPNDPGTVC 332
Cdd:PRK13968 233 LELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFII-----EEGIASAfterfVAAAAALKMGDPRDEENAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 333 GPLISARQRDRVQGYLDLAVAEGGRFACGGARPADRevGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRI 412
Cdd:PRK13968 308 GPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGA--GNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALEL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 413 ANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGgvwYCADAP---FGGYKQSGIGREMGLLGFEEY 478
Cdd:PRK13968 386 ANDSEFGLSATIFTTDETQARQMAARLECGGVFING---YCASDArvaFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
75-478 |
3.76e-59 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 200.92 E-value: 3.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 75 RQLRDAMQQHVEELRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESypWKQDLGEASPLGIA-TRRTLAREAVGVV 153
Cdd:cd07134 27 KRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKK--WMKPKRVRTPLLLFgTKSKIRYEPKGVC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 154 GAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSSHALGALLAKdpRVDMI 233
Cdd:cd07134 105 LIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA--FDEDEVAVFEGDAEVAQALLEL--PFDHI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 234 SFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIA 313
Cdd:cd07134 181 FFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 314 AATMSSIRPGDPNDPGT--VCGpLISARQRDRVQGYLDLAVAEGGRFACGGARPADREvgfYIEPTVIAGLTNDARVARE 391
Cdd:cd07134 261 KAEIEKFYGKDAARKASpdLAR-IVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR---YIAPTVLTNVTPDMKIMQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 392 EIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADA--PFGGYKQSGIGRE 469
Cdd:cd07134 337 EIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPnlPFGGVNNSGIGSY 416
|
....*....
gi 15607908 470 MGLLGFEEY 478
Cdd:cd07134 417 HGVYGFKAF 425
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
28-471 |
7.07e-59 |
|
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: 202.04 E-value: 7.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNP-ATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRN-TELRVRCVRQLRDAMQQHVEELrELTISEVGAPRMLTAS 105
Cdd:cd07083 37 VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKT--WKDWpQEDRARLLLKAADLLRRRRREL-IATLTYEVGKNWVEAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 106 AQLEGPVGDLSFAADTAESYPWKQDLGEASPlgiATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPA 185
Cdd:cd07083 114 DDVAEAIDFIRYYARAALRLRYPAVEVVPYP---GEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 186 PDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGR------AVMADAAATIKKVFLE 259
Cdd:cd07083 191 EDAVVVGYKVFEIFHE-AGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKkiyeaaARLAPGQTWFKRLYVE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 260 LGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISAR 339
Cdd:cd07083 270 TGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 340 QRDRVQGYLDLAVAEgGRFACGGARPADreVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDD--DAVRIANDSP 417
Cdd:cd07083 350 QEAKVLSYIEHGKNE-GQLVLGGKRLEG--EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTP 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 418 YGLSGTVYGADPQRAARIASRLRVGTVNVN----GGVwyCADAPFGGYKQSGIGREMG 471
Cdd:cd07083 427 YGLTGGVYSRKREHLEEARREFHVGNLYINrkitGAL--VGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
68-482 |
8.66e-59 |
|
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: 200.02 E-value: 8.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 68 ELRVRCVRQLRDAMQQHVEELRElTISE--VGAPRMLTASAQLEGPVGDLSFAADTAESypW-KQDLGEASPLGIATRRT 144
Cdd:cd07133 20 EERRDRLDRLKALLLDNQDALAE-AISAdfGHRSRHETLLAEILPSIAGIKHARKHLKK--WmKPSRRHVGLLFLPAKAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 145 LAREAVGVVGAITPWNFPhqINLAkLGP---ALAAGNTVVLKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSsHALG 221
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYP--LYLA-LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY--FDEDEVAVVTGG-ADVA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 222 ALLAKDPrVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVV 301
Cdd:cd07133 171 AAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 302 PRARYEEAVAIAAATMSSIRPGDPNDPGtvCGPLISARQRDRVQGYLDLAVAEGGR-FACGGArPADREVGFYIEPTVIA 380
Cdd:cd07133 250 PEDKLEEFVAAAKAAVAKMYPTLADNPD--YTSIINERHYARLQGLLEDARAKGARvIELNPA-GEDFAATRKLPPTLVL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 381 GLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCA--DAPF 458
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAqdDLPF 406
|
410 420
....*....|....*....|....
gi 15607908 459 GGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:cd07133 407 GGVGASGMGAYHGKEGFLTFSHAK 430
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
50-477 |
9.42e-57 |
|
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: 194.28 E-value: 9.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 50 AIEAARRAFDSTDwSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESY--PW 127
Cdd:cd07087 3 LVARLRETFLTGK-TRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWmkPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 128 KQDLGEASPLGIATRRtlaREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHtdFPP 207
Cdd:cd07087 82 RVSVPLLLQPAKAYVI---PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY--FDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 208 GVVNIVTSSSHALGALLAKdpRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACM 287
Cdd:cd07087 157 EAVAVVEGGVEVATALLAE--PFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 288 HAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVcGPLISARQRDRVQGYLDlavaeGGRFACGGAR-PA 366
Cdd:cd07087 235 NAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLLD-----DGKVVIGGQVdKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 367 DRevgfYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNV 446
Cdd:cd07087 309 ER----YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCV 384
|
410 420 430
....*....|....*....|....*....|...
gi 15607908 447 NGGVWYCA--DAPFGGYKQSGIGREMGLLGFEE 477
Cdd:cd07087 385 NDVLLHAAipNLPFGGVGNSGMGAYHGKAGFDT 417
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
28-467 |
1.18e-54 |
|
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: 189.55 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 28 VNPATEEVLGVAADADAEDMGRAIEAARRAF-DSTDWSRNTElRVRCVRQLRDAMQQHVEELRELTISEVGAPrMLTASA 106
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNWLPAHE-RIAILERLADLMEERADELALLIAREGGKP-LVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 107 QLEGPVGDLSFAAD-----TAESYPwkQDLGEASplgiATRRTLA-REAVGVVGAITPWNfpHQINLA--KLGPALAAGN 178
Cdd:cd07148 82 EVTRAIDGVELAADelgqlGGREIP--MGLTPAS----AGRIAFTtREPIGVVVAISAFN--HPLNLIvhQVAPAIAAGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 179 TVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSShALGALLAKDPRVDMISFTGSTATGRAVMADAAATiKKVFL 258
Cdd:cd07148 154 PVIVKPALATPLSCLAFVDLLHE-AGLPEGWCQAVPCEN-AVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 259 ELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISA 338
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 339 RQRDRVQGYLDLAVAEGGRFACGGARPADRevgfYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPY 418
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDT----TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15607908 419 GLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCAD-APFGGYKQSGIG 467
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
11-447 |
1.57e-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: 1.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAGTF-PTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNTEL-RVRCVRQLRDAMQQHVEEL 88
Cdd:TIGR01722 3 HWIGGKFAEGASGTYiPVTNPATNEVTTKVAFASVDEVDAAVASARETFLT--WGQTSLAqRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGaprmlTASAQLEGPVGDLSFAADTAESYPwKQDLGEASPlGIATRRTLA--REAVGVVGAITPWNFPHQIN 166
Cdd:TIGR01722 81 AELITAEHG-----KTHSDALGDVARGLEVVEHACGVN-SLLKGETST-QVATRVDVYsiRQPLGVCAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLaKDPRVDMISFTGSTATGRAVM 246
Cdd:TIGR01722 154 LWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSE-AGAPDGVLNVVHGDKEAVDRLL-EHPDVKAVSFVGSTPIGRYIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGC-AITTRLVVPRARyeEAVAIAAATMSSIRPGDP 325
Cdd:TIGR01722 232 TTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCmAISAAVLVGAAD--EWVPEIRERAEKIRIGPG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 326 NDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGA--RPADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAH 403
Cdd:TIGR01722 310 DDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRgyKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15607908 404 DGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVN 447
Cdd:TIGR01722 390 DTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN 433
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
45-478 |
1.01e-53 |
|
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: 186.66 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 45 EDMGRAIEAARRAFDSTDwSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAES 124
Cdd:cd07135 5 DEIDSIHSRLRATFRSGK-TKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 125 ypWKQD--LGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEH 202
Cdd:cd07135 84 --WAKDekVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 203 tdFPPGVVNIVTSSSHALGALLAKdpRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSA 282
Cdd:cd07135 162 --LDPDAFQVVQGGVPETTALLEQ--KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 283 FSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPgTVCGPLISARQRDRVQGYLDlavAEGGRFACGG 362
Cdd:cd07135 238 WGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLD---TTKGKVVIGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 363 AR-PADRevgfYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRV 441
Cdd:cd07135 314 EMdEATR----FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRS 389
|
410 420 430
....*....|....*....|....*....|....*....
gi 15607908 442 GTVNVNGGVWY--CADAPFGGYKQSGIGREMGLLGFEEY 478
Cdd:cd07135 390 GGVVINDTLIHvgVDNAPFGGVGDSGYGAYHGKYGFDTF 428
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
12-471 |
4.23e-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: 184.32 E-value: 4.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAGTfPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELR 89
Cdd:cd07125 36 IINGEETETGEGA-PVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAG--WSATPvEERAEILEKAADLLEANRGELI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGapRMLTasaqlEGpVGDLSFAADTAESYPW---KQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQIN 166
Cdd:cd07125 113 ALAAAEAG--KTLA-----DA-DAEVREAIDFCRYYAAqarELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRA-- 244
Cdd:cd07125 185 TGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHE-AGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLin 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 245 -VMADAAATIKKVFLELGGK--------------------SAFVvlddadlaaasavsafsacmHAGQGCAITTRLVVPR 303
Cdd:cd07125 264 rALAERDGPILPLIAETGGKnamivdstalpeqavkdvvqSAFG--------------------SAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 304 ARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEgGRFACggARPADREVGFYIEPTVIAGLT 383
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIA--PAPLDDGNGYFVAPGIIEIVG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 384 NDarVAREEIFGPVLTVIAHDGD--DDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVN----G---GVwyca 454
Cdd:cd07125 401 IF--DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitGaivGR---- 474
|
490
....*....|....*..
gi 15607908 455 dAPFGGYKQSGIGREMG 471
Cdd:cd07125 475 -QPFGGWGLSGTGPKAG 490
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
46-468 |
7.74e-52 |
|
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: 181.32 E-value: 7.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 46 DMGRAIEAARRAFdsTDWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPR--MLTASAQLEGPVgDLSFAAdta 122
Cdd:cd07095 1 QVDAAVAAARAAF--PGWAALSlEERAAILRRFAELLKANKEELARLISRETGKPLweAQTEVAAMAGKI-DISIKA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 123 esypWKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIvEH 202
Cdd:cd07095 75 ----YHERTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELW-EE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 203 TDFPPGVVNIVTSSSHAlGALLAKDPRVDMISFTGSTATGRAVMADAAATIKKVF-LELGGKSAFVVLDDADLAAASAVS 281
Cdd:cd07095 150 AGLPPGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 282 AFSACMHAGQGCAITTRLVVPRARYEEAVAIA-AATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFAC 360
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGAVGDAFLERlVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 361 GGARPADRevGFYIEPTVIAgLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLR 440
Cdd:cd07095 309 AMERLVAG--TAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420 430
....*....|....*....|....*....|..
gi 15607908 441 VGTVNVN----GGvwyCADAPFGGYKQSGIGR 468
Cdd:cd07095 386 AGIVNWNrpttGA---SSTAPFGGVGLSGNHR 414
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
11-465 |
1.32e-51 |
|
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: 182.22 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWSR-NTELRVRCVRQLRDAMQQHVEELR 89
Cdd:TIGR03240 1 LFIDGKWRAGQGESFASRNPATQEVLWQGAAASADQVEAAVAAARAAF--PAWARlSLEERIAVVQRFAALLEERKEALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGAPRMLTAS--AQLEGPVgDLSFAAdtaesypWKQDLGE-ASPLGIAtRRTLAREAVGVVGAITPWNFPHQIN 166
Cdd:TIGR03240 79 RVIARETGKPLWETRTevASMIGKV-AISIKA-------YHERTGEsENPMPDG-RAVLRHRPHGVVAVFGPYNFPGHLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 167 LAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIvEHTDFPPGVVNIVTSSSHAlGALLAKDPRVDMISFTGSTATGRAVM 246
Cdd:TIGR03240 150 NGHIVPALIAGNTVVFKPSELTPWVAEETVKLW-EKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 247 ADAAATIKKVF-LELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEA-VAIAAATMSSIRPGD 324
Cdd:TIGR03240 228 RQFGGRPEKILaLEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRLLVPDGAQGDAfLARLVEVAERLTVGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 325 PN-DPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARPaDREVGFyIEPTVIaGLTNDARVAREEIFGPVLTVIAH 403
Cdd:TIGR03240 308 WDaEPQPFMGAVISLRAAQRLLAAQAKLLALGGKSLLEMRQL-DPGAAF-LTPGII-DVTGVAELPDEEHFGPLLQVIRY 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607908 404 DGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCAD-APFGGYKQSG 465
Cdd:TIGR03240 385 TDFDEAIAIANNTRFGLSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGASSaAPFGGIGASG 447
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
9-465 |
1.24e-48 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 173.99 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 9 SALLIDGKLSDGRAGTFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFdsTDWSRNT-ELRVRCVRQLRDAMQQHVEE 87
Cdd:PRK09457 1 MTLWINGDWIAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF--PAWARLSfEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 88 LRELTISEVGAPRMLTAS--AQLEGPVgDLSFAADTAESYPWKQDLGEAsplgiatRRTLAREAVGVVGAITPWNFPHQI 165
Cdd:PRK09457 79 LAEVIARETGKPLWEAATevTAMINKI-AISIQAYHERTGEKRSEMADG-------AAVLRHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 166 NLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSShALGALLAKDPRVDMISFTGSTATGRAV 245
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQ-AGLPAGVLNLVQGGR-ETGKALAAHPDIDGLLFTGSANTGYLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 246 MADAAATIKKVF-LELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEA-VAIAAATMSSIRPG 323
Cdd:PRK09457 229 HRQFAGQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDAfLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 324 DPN-DPGTVCGPLISARQRDR-VQGYLDLaVAEGGRfACGGARPADREVGFyIEPTVIaGLTNDARVAREEIFGPVLTVI 401
Cdd:PRK09457 309 RWDaEPQPFMGAVISEQAAQGlVAAQAQL-LALGGK-SLLEMTQLQAGTGL-LTPGII-DVTGVAELPDEEYFGPLLQVV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607908 402 AHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVN----VNGGvwyCADAPFGGYKQSG 465
Cdd:PRK09457 385 RYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNwnkpLTGA---SSAAPFGGVGASG 449
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
147-476 |
7.17e-44 |
|
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: 160.36 E-value: 7.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 147 REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHtdFPPGVVNIVTSSSHALGALLAK 226
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET--FDEEYVAVVEGGVEENQELLDQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 227 dpRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAfvvlddadlaaasavsafsaC-------------------- 286
Cdd:cd07136 176 --KFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSP--------------------Civdedanlklaakrivwgkf 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 287 MHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVcGPLISARQRDRVQGYLDlavaeGGRFACGG-ARP 365
Cdd:cd07136 234 LNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLD-----NGKIVFGGnTDR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 366 ADRevgfYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVN 445
Cdd:cd07136 308 ETL----YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGC 383
|
330 340 350
....*....|....*....|....*....|...
gi 15607908 446 VNGGVWYCADA--PFGGYKQSGIGREMGLLGFE 476
Cdd:cd07136 384 INDTIMHLANPylPFGGVGNSGMGSYHGKYSFD 416
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
19-467 |
2.20e-43 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 164.22 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 19 DGRAGTFPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFDStdWSR-NTELRVRCVRQLRDAMQQHVEELRELTISEV 96
Cdd:PRK11904 558 NGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA--WSRtPVEERAAILERAADLLEANRAELIALCVREA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 97 G-----------------------APRMLTASAQLEGPVGDlsfaadtaesypwkqdlgeasplgiatRRTLAREAVGVV 153
Cdd:PRK11904 636 GktlqdaiaevreavdfcryyaaqARRLFGAPEKLPGPTGE---------------------------SNELRLHGRGVF 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 154 GAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMI 233
Cdd:PRK11904 689 VCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHE-AGIPKDVLQLLPGDGATVGAALTADPRIAGV 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 234 SFTGSTATGRA---VMADAAATIKKVFLELGG--------------------KSAFVVlddadlaaasavsafsacmhAG 290
Cdd:PRK11904 768 AFTGSTETARIinrTLAARDGPIVPLIAETGGqnamivdstalpeqvvddvvTSAFRS--------------------AG 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 291 QGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEgGRFACGGARPADREV 370
Cdd:PRK11904 828 QRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAGTEN 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 371 GFYIEPTVIAglTNDARVAREEIFGPVLTVIAHDGDD-DAV--RIaNDSPYGLSGTVYGADPQRAARIASRLRVGTVNVN 447
Cdd:PRK11904 907 GHFVAPTAFE--IDSISQLEREVFGPILHVIRYKASDlDKVidAI-NATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
490 500
....*....|....*....|....*..
gi 15607908 448 ----G---GVwycadAPFGGYKQSGIG 467
Cdd:PRK11904 984 rnqiGavvGV-----QPFGGQGLSGTG 1005
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
50-476 |
2.20e-42 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 156.23 E-value: 2.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 50 AIEAARRAFdSTDWSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESypWKQ 129
Cdd:cd07132 3 AVRRAREAF-SSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPE--WMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 130 DlgEASPLGIATRRT---LAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHTD-- 204
Cdd:cd07132 80 P--EPVKKNLATLLDdvyIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDke 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 205 -FPpgvvnIVTSSSHALGALLakDPRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAF 283
Cdd:cd07132 158 cYP-----VVLGGVEETTELL--KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 284 SACMHAGQGC-AITTRLVVPRARyEEAVAIAAATMSSIRPGDP-NDPGtvCGPLISARQRDRVQGYLdlavaEGGRFACG 361
Cdd:cd07132 231 GKFINAGQTCiAPDYVLCTPEVQ-EKFVEALKKTLKEFYGEDPkESPD--YGRIINDRHFQRLKKLL-----SGGKVAIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 362 G-ARPADRevgfYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLR 440
Cdd:cd07132 303 GqTDEKER----YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTS 378
|
410 420 430
....*....|....*....|....*....|....*...
gi 15607908 441 VGTVNVNGGVWYCA--DAPFGGYKQSGIGREMGLLGFE 476
Cdd:cd07132 379 SGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFD 416
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
55-482 |
1.13e-41 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 155.19 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 55 RRAFdSTDWSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPRMLTASAQLEGPVGDLSFAADTAESY--PWKQDLG 132
Cdd:PTZ00381 17 KESF-LTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYlkPEKVDTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 133 EASPLGiatRRTLAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHtdFPPGVVNI 212
Cdd:PTZ00381 96 GVFGPG---KSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY--LDPSYVRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 213 VTSSSHALGALLAKdpRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQG 292
Cdd:PTZ00381 171 IEGGVEVTTELLKE--PFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 293 CAITTRLVVPRA---RYEEAVAIAAATMSSIRPGDPNDPGTVcgplISARQRDRVQGYLDlavAEGGRFACGG-ARPADR 368
Cdd:PTZ00381 249 CVAPDYVLVHRSikdKFIEALKEAIKEFFGEDPKKSEDYSRI----VNEFHTKRLAELIK---DHGGKVVYGGeVDIENK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 369 evgfYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNG 448
Cdd:PTZ00381 322 ----YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIND 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 15607908 449 GVWYCADA--PFGGYKQSGIGREMGLLGFEEYLEAK 482
Cdd:PTZ00381 398 CVFHLLNPnlPFGGVGNSGMGAYHGKYGFDTFSHPK 433
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
12-467 |
1.09e-39 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 149.91 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAG-TFPTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWSRnTELRVRCVRQLRDA--MQQHVEEL 88
Cdd:PLN00412 19 YADGEWRTSSSGkSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA--WAK-TPLWKRAELLHKAAaiLKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPRMLTASAQLEGpvGDL-SFAADTAESYPWKQDL--GEASPLGIATRRTLAREA-VGVVGAITPWNFPHQ 164
Cdd:PLN00412 96 AECLVKEIAKPAKDAVTEVVRS--GDLiSYTAEEGVRILGEGKFlvSDSFPGNERNKYCLTSKIpLGVVLAIPPFNYPVN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 165 INLAKLGPALAAGNTVVLKPApdTPWCAAALGEIIVEH-TDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTaTGR 243
Cdd:PLN00412 174 LAVSKIAPALIAGNAVVLKPP--TQGAVAALHMVHCFHlAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 244 AVMADAAATikKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPG 323
Cdd:PLN00412 251 AISKKAGMV--PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 324 DPNDPGTVCgPLISARQRDRVQGYLDLAVAEGGRFAcggaRPADREvGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAH 403
Cdd:PLN00412 329 PPEDDCDIT-PVVSESSANFIEGLVMDAKEKGATFC----QEWKRE-GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607908 404 DGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADA-PFGGYKQSGIG 467
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIG 467
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
20-479 |
1.80e-39 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 149.60 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 20 GRAGTFPTVNPATEEVLGVAADADAEDMG---RAIEAARRAFDSTDWSRNTELrvrcVRQLRDAMQQHVEELRELTISEV 96
Cdd:PLN02315 31 ANGPLVSSVNPANNQPIAEVVEASLEDYEeglRACEEAAKIWMQVPAPKRGEI----VRQIGDALRAKLDYLGRLVSLEM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 97 GapRMLtasAQLEGPVGDLSFAADTAESYPwKQDLGEASPlgiATRRTLAREAV----GVVGAITPWNFPhqinLAKLG- 171
Cdd:PLN02315 107 G--KIL---AEGIGEVQEIIDMCDFAVGLS-RQLNGSIIP---SERPNHMMMEVwnplGIVGVITAFNFP----CAVLGw 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 172 ---PALAAGNTVVLKPAPDTPWCAAALGEII---VEHTDFPPGVVNIVTSSSHaLGALLAKDPRVDMISFTGSTATGRAV 245
Cdd:PLN02315 174 nacIALVCGNCVVWKGAPTTPLITIAMTKLVaevLEKNNLPGAIFTSFCGGAE-IGEAIAKDTRIPLVSFTGSSKVGLMV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 246 MADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDP 325
Cdd:PLN02315 253 QQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 326 NDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGArPADREvGFYIEPTVIAgLTNDARVAREEIFGPVLTVIAHDG 405
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGS-AIESE-GNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 406 DDDAVRIANDSPYGLSGTVYGADPQRAARIASRL--RVGTVNVN--------GGVwycadapFGGYKQSGIGREMGLLGF 475
Cdd:PLN02315 410 LEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVNiptngaeiGGA-------FGGEKATGGGREAGSDSW 482
|
....
gi 15607908 476 EEYL 479
Cdd:PLN02315 483 KQYM 486
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
151-465 |
4.54e-38 |
|
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: 145.81 E-value: 4.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 151 GVVGAITPWNFPhQI--NLAkLGPALAaGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDP 228
Cdd:cd07123 172 GFVYAVSPFNFT-AIggNLA-GAPALM-GNVVLWKPSDTAVLSNYLVYKILEE-AGLPPGVINFVPGDGPVVGDTVLASP 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 229 RVDMISFTGSTATGRAVMADAAA------TIKKVFLELGGK--------------------SAFVvlddadlaaasavsa 282
Cdd:cd07123 248 HLAGLHFTGSTPTFKSLWKQIGEnldryrTYPRIVGETGGKnfhlvhpsadvdslvtatvrGAFE--------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 283 fsacmHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGG-RFACG 361
Cdd:cd07123 313 -----YQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 362 GArpADREVGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDD--DAVRIAND-SPYGLSGTVYGADPQ--RAARIA 436
Cdd:cd07123 388 GK--CDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDfeETLELVDTtSPYALTGAIFAQDRKaiREATDA 465
|
330 340 350
....*....|....*....|....*....|...
gi 15607908 437 SRLRVGTVNVN----GGVwyCADAPFGGYKQSG 465
Cdd:cd07123 466 LRNAAGNFYINdkptGAV--VGQQPFGGARASG 496
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
12-467 |
6.50e-38 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 148.16 E-value: 6.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAgtFPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFdsTDWSR-NTELRVRCVRQLRDAMQQHVEELR 89
Cdd:COG4230 561 LIAGEAASGEA--RPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAF--PAWSAtPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGapRMLTAS-AQLEGPVGDLSFAADTAEsypwkQDLGEASPLgiatrrtlarEAVGVVGAITPWNFPHQINLA 168
Cdd:COG4230 637 ALLVREAG--KTLPDAiAEVREAVDFCRYYAAQAR-----RLFAAPTVL----------RGRGVFVCISPWNFPLAIFTG 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 169 KLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAV--- 245
Cdd:COG4230 700 QVAAALAAGNTVLAKPAEQTPLIAARAVRLLHE-AGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInrt 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 246 MADAAATIKKVFLELGG--------------------KSAFVVlddadlaaasavsafsacmhAGQGCAITTRLVVPRAR 305
Cdd:COG4230 779 LAARDGPIVPLIAETGGqnamivdssalpeqvvddvlASAFDS--------------------AGQRCSALRVLCVQEDI 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 306 YEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEgGRFACGGARPADREVGFYIEPTVIAglTND 385
Cdd:COG4230 839 ADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAE-GRLVHQLPLPEECANGTFVAPTLIE--IDS 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 386 ARVAREEIFGPVLTVIAHDGDD-DAV--RIaNDSPYGLSGTVYGADPQRAARIASRLRVGTVNVN----G---GVwycad 455
Cdd:COG4230 916 ISDLEREVFGPVLHVVRYKADElDKVidAI-NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNrniiGavvGV----- 989
|
490
....*....|..
gi 15607908 456 APFGGYKQSGIG 467
Cdd:COG4230 990 QPFGGEGLSGTG 1001
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
26-471 |
8.93e-38 |
|
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: 144.67 E-value: 8.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 26 PTVNPAT-EEVLGVAADADAEDMGRAIEAARRAFdsTDWSR-NTELRVRCVRQLRDAMQQHVEELRELTISEVGAPrMLT 103
Cdd:TIGR01238 54 PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAF--PTWNAtPAKERAAKLDRLADLLELHMPELMALCVREAGKT-IHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 104 ASAQLEGPVGDLSFAADTAEsypwkQDLGEASplgiatrrtlaREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 183
Cdd:TIGR01238 131 AIAEVREAVDFCRYYAKQVR-----DVLGEFS-----------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 184 PAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAV---MADAAATIKKVFLEL 260
Cdd:TIGR01238 195 PAEQTSLIAYRAVELMQE-AGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqtLAQREDAPVPLIAET 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 261 GGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQ 340
Cdd:TIGR01238 274 GGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 341 RDRVQGYLDlAVAEGGRFACGGARPADREV--GFYIEPTVIAglTNDARVAREEIFGPVLTVIAHDGD--DDAVRIANDS 416
Cdd:TIGR01238 354 KQNLLAHIE-HMSQTQKKIAQLTLDDSRACqhGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKARelDQIVDQINQT 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 417 PYGLSGTVYGADPQRAARIASRLRVGTVNVN----GGVwyCADAPFGGYKQSGIGREMG 471
Cdd:TIGR01238 431 GYGLTMGVHSRIETTYRWIEKHARVGNCYVNrnqvGAV--VGVQPFGGQGLSGTGPKAG 487
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-447 |
1.48e-37 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 145.27 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAGTF-PTVNPATEEVLGVAADADAEDMGRAIEAARRAFDStdWsRNTEL--RVRCVRQLRDAMQQHVEEL 88
Cdd:PLN02419 117 LIGGSFVESQSSSFiDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL--W-RNTPIttRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAprmltasaQLEGPVGDLSFAADTAESYPWKQDL--GEASPL---GIATRRTlaREAVGVVGAITPWNFPH 163
Cdd:PLN02419 194 AMNITTEQGK--------TLKDSHGDIFRGLEVVEHACGMATLqmGEYLPNvsnGVDTYSI--REPLGVCAGICPFNFPA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 164 QINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALlAKDPRVDMISFTGSTATGR 243
Cdd:PLN02419 264 MIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAME-AGLPDGVLNIVHGTNDTVNAI-CDDEDIRAVSFVGSNTAGM 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 244 AVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGC-AITTRLVVPRARYEEAVAIAAATMSSIRP 322
Cdd:PLN02419 342 HIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCmALSTVVFVGDAKSWEDKLVERAKALKVTC 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 323 GdpNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGG---ARPAdREVGFYIEPTVIAGLTNDARVAREEIFGPVLT 399
Cdd:PLN02419 422 G--SEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGrdiVVPG-YEKGNFIGPTILSGVTPDMECYKEEIFGPVLV 498
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15607908 400 VIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVN 447
Cdd:PLN02419 499 CMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
11-467 |
1.74e-37 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 146.93 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 11 LLIDGKLSDGragTFPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAFdsTDWS-RNTELRVRCVRQLRDAMQQHVEEL 88
Cdd:PRK11905 558 LLAGGDVDGG---TRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAF--PEWSaTPAAERAAILERAADLMEAHMPEL 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 89 RELTISEVGAPrMLTASAQLEGPVGDLSFAADTAESYPWKQDlgeasplgiatrrtlaREAVGVVGAITPWNFPHQINLA 168
Cdd:PRK11905 633 FALAVREAGKT-LANAIAEVREAVDFLRYYAAQARRLLNGPG----------------HKPLGPVVCISPWNFPLAIFTG 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 169 KLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAV--- 245
Cdd:PRK11905 696 QIAAALVAGNTVLAKPAEQTPLIAARAVRLLHE-AGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIqrt 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 246 MADAAATIKKVFLELGGK--------------------SAFVVlddadlaaasavsafsacmhAGQGCAITTRLVVprar 305
Cdd:PRK11905 775 LAKRSGPPVPLIAETGGQnamivdssalpeqvvadviaSAFDS--------------------AGQRCSALRVLCL---- 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 306 yEEAVAIAAATM-----SSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEgGRFACGGARPADREVGFYIEPTVIA 380
Cdd:PRK11905 831 -QEDVADRVLTMlkgamDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAA-GRLVHQLPLPAETEKGTFVAPTLIE 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 381 glTNDARVAREEIFGPVLTVIAHDGDD-DAVrIA--NDSPYGLSGTVYGADPQRAARIASRLRVGTVNVN----G---GV 450
Cdd:PRK11905 909 --IDSISDLEREVFGPVLHVVRFKADElDRV-IDdiNATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniiGavvGV 985
|
490
....*....|....*..
gi 15607908 451 wycadAPFGGYKQSGIG 467
Cdd:PRK11905 986 -----QPFGGEGLSGTG 997
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
148-484 |
4.41e-33 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 130.22 E-value: 4.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 148 EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHTDfpPGVVNIVTSSSHALGALLakD 227
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLD--TKAIKVIEGGVPETTALL--E 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 228 PRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKS-AFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARY 306
Cdd:cd07137 176 QKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCpVIVDSTVDLKVAVRRIAGGKWGCNNGQACIAPDYVLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 307 EEAVAIAAATMSSIRPGDPNDPGTVcGPLISARQRDRVQGYLDlavaEGGRFAC---GGARPADRevgFYIEPTVIAGLT 383
Cdd:cd07137 256 PTLIDALKNTLEKFFGENPKESKDL-SRIVNSHHFQRLSRLLD----DPSVADKivhGGERDEKN---LYIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 384 NDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGV--WYCADAPFGGY 461
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVvqYAIDTLPFGGV 407
|
330 340
....*....|....*....|...
gi 15607908 462 KQSGIGREMGLLGFEEYLEAKLI 484
Cdd:cd07137 408 GESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
148-484 |
7.32e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 124.84 E-value: 7.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 148 EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHTDfpPGVVNIVTSSSHALGALLakD 227
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLD--SKAVKVIEGGPAVGEQLL--Q 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 228 PRVDMISFTGSTATGRAVMADAAATIKKVFLELGGK------SAFVVLDDADLAAASAVSAFSACmhAGQGC-AITTRLV 300
Cdd:PLN02203 183 HKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKcpcivdSLSSSRDTKVAVNRIVGGKWGSC--AGQACiAIDYVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 301 vpraryEEAVA-----IAAATMSSIRPGDPNDPGTVCgPLISARQRDRVQGYL-DLAVAeggrfAC---GGARPADRevg 371
Cdd:PLN02203 261 ------EERFApilieLLKSTIKKFFGENPRESKSMA-RILNKKHFQRLSNLLkDPRVA-----ASivhGGSIDEKK--- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 372 FYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGG-V 450
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAiI 405
|
330 340 350
....*....|....*....|....*....|....*
gi 15607908 451 WYCADA-PFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:PLN02203 406 QYACDSlPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
95-473 |
1.27e-30 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 123.50 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 95 EVGAPRMLTAsaQLEGPVGDLSFAADTAESYPWKQDLGEASPLGIATRRTLAREAVGVVGAITPWNFPHQINLAKLGPAL 174
Cdd:cd07084 48 VTGKGWMFAE--NICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGAL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 175 AAGNTVVLKPAPDTPWCAAALGEIIVEHTDFPPGVVNIVTSSSHALGALLAKdPRVDMISFTGSTATGRAVMADAAATik 254
Cdd:cd07084 126 AMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLINGDGKTMQALLLH-PNPKMVLFTGSSRVAEKLALDAKQA-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 255 KVFLELGG-KSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVP-----RARYEEAVAIAAATmssirpgdpndp 328
Cdd:cd07084 203 RIYLELAGfNWKVLGPDAQAVDYVAWQCVQDMTACSGQKCTAQSMLFVPenwskTPLVEKLKALLARR------------ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 329 gTVCGPLISARQRDRVQGYLDLAVAEGGR-FACGGARPADREVGFYIEPTVIAGL--TNDARVAR-----EEIFGPV--L 398
Cdd:cd07084 271 -KLEDLLLGPVQTFTTLAMIAHMENLLGSvLLFSGKELKNHSIPSIYGACVASALfvPIDEILKTyelvtEEIFGPFaiV 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 399 TVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNGGVWYCADAPF----GGYKQSGIGREMGLL 473
Cdd:cd07084 350 VEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNqnhgGGPAADPRGAGIGGP 428
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
13-436 |
5.95e-30 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 122.38 E-value: 5.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 13 IDGKLSDGRAGTFPTVNPATEEVLgVAADADAEDMGRAIEAAR-------RAFDSTDwsrntelRVRCVRQLRDAMQQHV 85
Cdd:cd07128 5 VAGQWHAGTGDGRTLHDAVTGEVV-ARVSSEGLDFAAAVAYARekggpalRALTFHE-------RAAMLKALAKYLMERK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 86 EELRELTISeVGAPRmLTASAQLEGPVGDLSFAADTAESYPWKQDL---GEASPLG-----IATRRTLAREAVGVvgAIT 157
Cdd:cd07128 77 EDLYALSAA-TGATR-RDSWIDIDGGIGTLFAYASLGRRELPNAHFlveGDVEPLSkdgtfVGQHILTPRRGVAV--HIN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 158 PWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHTDFPPGVVNIVTSSShalGALLAKDPRVDMISFTG 237
Cdd:cd07128 153 AFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLPEGALQLICGSV---GDLLDHLGEQDVVAFTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 238 STATGR------------------------AVMA-DA-------AATIKKVFLELGGKsafvvlddadlaaasavsafsa 285
Cdd:cd07128 230 SAATAAklrahpnivarsirfnaeadslnaAILGpDAtpgtpefDLFVKEVAREMTVK---------------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 286 cmhAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDLAVAEGGRFACGGARP 365
Cdd:cd07128 288 ---AGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRF 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607908 366 ----ADREVGFYIEPTVIagLTNDARVARE----EIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIA 436
Cdd:cd07128 365 evvgADAEKGAFFPPTLL--LCDDPDAATAvhdvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
15-436 |
3.52e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 114.42 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 15 GKLSDGRAGTFPTVNPATEEVLgVAADADAEDMGRAIEAARRAFDSTDWSRNTELRVRCVRQLRDAMQQHVEELRELTIS 94
Cdd:PRK11903 11 GRWQAGSGAGTPLFDPVTGEEL-VRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 95 EVGAPRMlTASAQLEGPVGDLSFAADtaesypWKQDLGEASPLGIATRRTLAREAV-----------GVVGAITPWNFPH 163
Cdd:PRK11903 90 NSGTTRN-DSAVDIDGGIFTLGYYAK------LGAALGDARLLRDGEAVQLGKDPAfqgqhvlvptrGVALFINAFNFPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 164 QINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVEHTDFPPGVVNIVTSSShalGALLAKDPRVDMISFTGSTATGR 243
Cdd:PRK11903 163 WGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGILPAGALSVVCGSS---AGLLDHLQPFDVVSFTGSAETAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 244 AVMADAAATIKKVFLELGGKS-------AFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAAT 316
Cdd:PRK11903 240 VLRSHPAVVQRSVRVNVEADSlnsallgPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 317 MSSIRPGDPNDPGTVCGPLISARQRDRVQGYLDL------AVAEGGRFACGGARPAdreVGFYIEPTVIagLTNDARVAR 390
Cdd:PRK11903 320 LAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAAlraqaeVLFDGGGFALVDADPA---VAACVGPTLL--GASDPDAAT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15607908 391 E----EIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIA 436
Cdd:PRK11903 395 AvhdvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
44-484 |
3.79e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.91 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 44 AEDMGRAIEAARRAFDStDWSRNTELRVRCVRQLRDAMQQHVEELRELTISEVGAPrmltasaQLEGPVGDLSFAADTAE 123
Cdd:PLN02174 9 AADASILVTELRRSFDD-GVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKP-------ELESSVYEVSLLRNSIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 124 sYPWKQDLGEASPLGIATRRT-------LAREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALG 196
Cdd:PLN02174 81 -LALKQLKNWMAPEKAKTSLTtfpasaeIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 197 EIIVEHTDfpPGVVNIVTSSSHALGALLAKdpRVDMISFTGSTATGRAVMADAAATIKKVFLELGGKSAFVVLDDADLAA 276
Cdd:PLN02174 160 KLLEQYLD--SSAVRVVEGAVTETTALLEQ--KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 277 ASAVSAFSA--CmHAGQGCA-----ITTRLVVPRARyeEAVAIAAATMSSIRPGDPNDPGTVcgplISARQRDRVQGYLD 349
Cdd:PLN02174 236 TVRRIIAGKwgC-NNGQACIspdyiLTTKEYAPKVI--DAMKKELETFYGKNPMESKDMSRI----VNSTHFDRLSKLLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 350 LAVAEgGRFACGGARpaDREvGFYIEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVYGADP 429
Cdd:PLN02174 309 EKEVS-DKIVYGGEK--DRE-NLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNK 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607908 430 QRAARIASRLRVGTVNVNGGVWYCA--DAPFGGYKQSGIGREMGLLGFEEYLEAKLI 484
Cdd:PLN02174 385 KLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
12-467 |
1.67e-25 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 110.83 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 12 LIDGKLSDGRAGtfPTVNPA-TEEVLGVAADADAEDMGRAIEAARRAfdSTDW-SRNTELRVRCVRQLRDAMQQHVEELR 89
Cdd:PRK11809 650 MLEDPVAAGEMS--PVINPAdPRDIVGYVREATPAEVEQALESAVNA--APIWfATPPAERAAILERAADLMEAQMQTLM 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 90 ELTISEVGAPrMLTASAQLEGPVGDLSFAADTAEsypwkQDLGEAsplgiaTRRTLareavGVVGAITPWNFPHQINLAK 169
Cdd:PRK11809 726 GLLVREAGKT-FSNAIAEVREAVDFLRYYAGQVR-----DDFDND------THRPL-----GPVVCISPWNFPLAIFTGQ 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 170 LGPALAAGNTVVLKPAPDTPWCAAALGEIIVEhTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGR------ 243
Cdd:PRK11809 789 VAAALAAGNSVLAKPAEQTPLIAAQAVRILLE-AGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARllqrnl 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 244 AVMADAAATIKKVFLELGGKSAFVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPRARYEEAVAIAAATMSSIRPG 323
Cdd:PRK11809 868 AGRLDPQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMG 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 324 DPNDPGTVCGPLISARQRDRVQGYLDlAVAEGGRFACGGARPADREV--GFYIEPTVIAgLTNDARVAReEIFGPVLTVI 401
Cdd:PRK11809 948 NPDRLSTDIGPVIDAEAKANIERHIQ-AMRAKGRPVFQAARENSEDWqsGTFVPPTLIE-LDSFDELKR-EVFGPVLHVV 1024
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607908 402 --AHDGDDDAVRIANDSPYGLSGTVYGADPQRAARIASRLRVGTVNVNG-------GVwycadAPFGGYKQSGIG 467
Cdd:PRK11809 1025 ryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnmvgavvGV-----QPFGGEGLSGTG 1094
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
49-448 |
2.18e-21 |
|
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: 96.46 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 49 RAIEAARRAFDS-TDWSRNTelRVRCVRQLRDAMQQHVEELRELTISEVGAPRmltasAQLEG----PVGDLSFAADTAE 123
Cdd:cd07129 3 AAAAAAAAAFESyRALSPAR--RAAFLEAIADEIEALGDELVARAHAETGLPE-----ARLQGelgrTTGQLRLFADLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 124 SYPWKQ---D--LGEASPLGIA-TRRTLAreAVGVVGAITPWNFPHQINLAklG----PALAAGNTVVLKPAPDTPWCAA 193
Cdd:cd07129 76 EGSWLDariDpaDPDRQPLPRPdLRRMLV--PLGPVAVFGASNFPLAFSVA--GgdtaSALAAGCPVVVKAHPAHPGTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 194 ALGEII---VEHTDFPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMADAAA--TIKKVFLELGGKS---A 265
Cdd:cd07129 152 LVARAIraaLRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNpvfI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 266 FVVLDDADLAAASAVSAFSACMHAGQGCAITTRLVVPR-ARYEEAVAIAAATMSSIrpgdpnDPGTVCGPLISARQRDRV 344
Cdd:cd07129 232 LPGALAERGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAgPAGDAFIAALAEALAAA------PAQTMLTPGIAEAYRQGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 345 QGYLDLAVAEggRFACGGARPADREVGFYIEPTVIAGLTNDArVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTV 424
Cdd:cd07129 306 EALAAAPGVR--VLAGGAAAEGGNQAAPTLFKVDAAAFLADP-ALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATI 382
|
410 420
....*....|....*....|....*...
gi 15607908 425 YGA--DPQRAARIASRL--RVGTVNVNG 448
Cdd:cd07129 383 HGEedDLALARELLPVLerKAGRLLFNG 410
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
127-465 |
1.88e-14 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 75.59 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 127 WKQDLGEASPLGIATRRTLAREAVG-VVGAITpwnFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEI---IVEH 202
Cdd:cd07127 173 WEKPQGKHDPLAMEKTFTVVPRGVAlVIGCST---FPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQVareVLAE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 203 TDFPPGVVNIVTSS-SHALGALLAKDPRVDMISFTGSTATGRAVmaDAAATIKKVFLELGGKSAFVVLDDADLAAASAVS 281
Cdd:cd07127 250 AGFDPNLVTLAADTpEEPIAQTLATRPEVRIIDFTGSNAFGDWL--EANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 282 AFSACMHAGQGCAITTRLVVPRA--RYEEAV----AIAAATMSSIRpGDPNDPGTVCGpLISARQRDRVQGYLDLAVAEG 355
Cdd:cd07127 328 AFSLSLYSGQMCTTPQNIYVPRDgiQTDDGRksfdEVAADLAAAID-GLLADPARAAA-LLGAIQSPDTLARIAEARQLG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 356 GRFACGGARP----ADREVGfyiEPTVIAGLTNDARVAREEIFGPVLTVIAHDGDDDAVRIANDSPY---GLSGTVYGAD 428
Cdd:cd07127 406 EVLLASEAVAhpefPDARVR---TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTD 482
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15607908 429 PQRAARIAS-RLRVG---TVNVNGGVWYCADAPFGGYKQSG 465
Cdd:cd07127 483 PEVVERVQEaALDAGvalSINLTGGVFVNQSAAFSDFHGTG 523
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
29-246 |
2.94e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 52.60 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 29 NPATEEVLGVAADADAedmgrAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRM------ 101
Cdd:PRK15398 25 PPAAVGEMGVFASVDD-----AVAAAKVAQQR--YQQKSlAMRQRIIDAIREALLPHAEELAELAVEETGMGRVedkiak 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 102 LTASAQLEGPVGDLSFAAdtaesypWKQDLG----EASPlgiatrrtlareaVGVVGAITPWNFP------HQINLaklg 171
Cdd:PRK15398 98 NVAAAEKTPGVEDLTTEA-------LTGDNGltliEYAP-------------FGVIGAVTPSTNPtetiinNAISM---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 172 paLAAGNTVVLKPAPD----TPWCAAALGEIIVEHTdfppGVVNIVTS----SSHALGALLAkDPRVDMISFTGSTATGR 243
Cdd:PRK15398 154 --LAAGNSVVFSPHPGakkvSLRAIELLNEAIVAAG----GPENLVVTvaepTIETAQRLMK-HPGIALLVVTGGPAVVK 226
|
...
gi 15607908 244 AVM 246
Cdd:PRK15398 227 AAM 229
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
45-247 |
3.85e-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: 49.16 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 45 EDMGRAIEAARRAFDStdWSRNT-ELRVRCVRQLRDAMQQHVEELRELTISEVGAPRM------LTASAQLEGPVGDLSF 117
Cdd:cd07121 4 ATVDDAVAAAKAAQKQ--YRKCTlADREKIIEAIREALLSNAEELAEMAVEETGMGRVedkiakNHLAAEKTPGTEDLTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 118 AAdtaesypWKQD----LGEASPlgiatrrtlareaVGVVGAITPWNFP------HQINLaklgpaLAAGNTVVLKPAPD 187
Cdd:cd07121 82 TA-------WSGDngltLVEYAP-------------FGVIGAITPSTNPtetiinNSISM------LAAGNAVVFNPHPG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607908 188 TPWCAA----ALGEIIVEHTDfPPGVVNIVTSSSHALGALLAKDPRVDMISFTGSTATGRAVMA 247
Cdd:cd07121 136 AKKVSAyaveLINKAIAEAGG-PDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALS 198
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
148-250 |
4.88e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 39.40 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 148 EAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEII----VEHtDFPPGVVNIVTSSSHALGAL 223
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAA-GAPEGLIQWIEEPSIELTQE 172
|
90 100
....*....|....*....|....*..
gi 15607908 224 LAKDPRVDMIsftgsTATGRAVMADAA 250
Cdd:cd07122 173 LMKHPDVDLI-----LATGGPGMVKAA 194
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
151-262 |
7.50e-03 |
|
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: 38.63 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607908 151 GVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAALGEIIVeHTDFPPGVVNIVTSSSHALGALLAK-DPR 229
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLH-LCGMPATDVDLIHSDGPTMNKILLEaNPR 222
|
90 100 110
....*....|....*....|....*....|...
gi 15607908 230 vdMISFTGSTATGRAVmadAAATIKKVFLELGG 262
Cdd:cd07126 223 --MTLFTGSSKVAERL---ALELHGKVKLEDAG 250
|
|
| |
