|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
3-463 |
0e+00 |
|
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: 719.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:cd07139 10 PSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSRTMQSGLPREHIDNFIEVARAFPFSAVRQSRN-GNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVV 161
Cdd:cd07139 90 MPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGgGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 162 LKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGK 241
Cdd:cd07139 170 LKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 242 SAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSR 321
Cdd:cd07139 250 SAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRER 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 322 VEGYMASGVAEGAAVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGA 401
Cdd:cd07139 330 VEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGS 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 402 VFTGDLDHGLSIARRIRTGTVELNGSLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGL 463
Cdd:cd07139 410 VWTADVERGLAVARRIRTGTVGVNGFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
2-461 |
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: 616.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:cd07138 9 APAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADELAQAITLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GCPISLSRTMQSGLPREHIDNFIEVARAFPFsavrQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVV 161
Cdd:cd07138 87 GAPITLARAAQVGLGIGHLRAAADALKDFEF----EERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 162 LKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGG 240
Cdd:cd07138 163 LKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDgPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 241 KSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRS 320
Cdd:cd07138 243 KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 321 RVEGYMASGVAEGAAVVTGG-GRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLS 399
Cdd:cd07138 323 RVQGYIQKGIEEGARLVAGGpGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 400 GAVFTGDLDHGLSIARRIRTGTVELNGSLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07138 403 GYVWSADPERARAVARRLRAGQVHINGAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
11-463 |
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: 570.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSrTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRT 90
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 MQSGLPREHIDNFIEVARAFPFSAVRQSRN-----GNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPA 165
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPAlrggpGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 166 PETPLDSYLLAEMLQDAGLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAA 244
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTgSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 245 VILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEG 324
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 325 YMASGVAEGAAVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFT 404
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 405 GDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGL 463
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGgGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
3-461 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 566.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFdsGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:COG1012 17 AASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERREELAALLTLETG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSRT-MQSGLprEHIDNFIEVARAFPFSAVRQSRNG-NALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTV 160
Cdd:COG1012 95 KPLAEARGeVDRAA--DFLRYYAGEARRLYGETIPSDAPGtRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 161 VLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELG 239
Cdd:COG1012 173 VLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 240 GKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQR 319
Cdd:COG1012 253 GKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 320 SRVEGYMASGVAEGAAVVTGGGRPQGfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLS 399
Cdd:COG1012 333 ERVLAYIEDAVAEGAELLTGGRRPDG-EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLA 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567559872 400 GAVFTGDLDHGLSIARRIRTGTVELNGSLVG--LNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:COG1012 412 ASVFTRDLARARRVARRLEAGMVWINDGTTGavPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
3-461 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 544.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSRTmQSGLPREHIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVL 162
Cdd:pfam00171 81 KPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 163 KPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGK 241
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 242 SAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSR 321
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 322 VEGYMASGVAEGAAVVTGGGRpqGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGA 401
Cdd:pfam00171 320 VLKYVEDAKEEGAKLLTGGEA--GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 402 VFTGDLDHGLSIARRIRTGTVELNGSLVG--LNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGdaDGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
11-461 |
1.82e-166 |
|
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: 477.04 E-value: 1.82e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRT 90
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 MQSGLPrEHIDNFIEVARAFpFSAVRQSRNGNALV--VHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPET 168
Cdd:cd07114 81 QVRYLA-EWYRYYAGLADKI-EGAVIPVDKGDYLNftRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 169 PLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVIL 247
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 248 DDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMA 327
Cdd:cd07114 239 DDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 328 SGVAEGAAVVTGGGRPQG--FDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTG 405
Cdd:cd07114 319 RAREEGARVLTGGERPSGadLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 406 DLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07114 399 DLARAHRVARAIEAGTVWVNTyRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
1-461 |
4.20e-166 |
|
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: 477.09 E-value: 4.20e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 1 MSSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQ 80
Cdd:cd07091 13 VDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDELAALESLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 81 MGCPISLSRTMqsglpreHIDNFIEVARAFPFSA-------VRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPA 153
Cdd:cd07091 93 NGKPLEESAKG-------DVALSIKCLRYYAGWAdkiqgktIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 154 LLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGN-DI 231
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 232 RRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIG 311
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 312 PMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFA 391
Cdd:cd07091 326 PQVSKAQFDKILSYIESGKKEGATLLTGGERHG--SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 392 NDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
32-461 |
8.66e-165 |
|
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: 472.08 E-value: 8.66e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 32 DKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRtMQSGLPREHIDNFIEVARAFP 111
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 112 FSAVRQSRNGN-ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVN 190
Cdd:cd07078 78 GEVIPSPDPGElAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 191 IVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQ 269
Cdd:cd07078 158 VVTGDgDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 270 VCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGfDHG 349
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEG-GKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 350 YFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLV 429
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....
gi 2567559872 430 GL--NAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07078 397 GAepSAPFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
6-461 |
6.65e-164 |
|
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: 470.93 E-value: 6.65e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 6 NDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPI 85
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 86 SLSRTMQSGlprehidnfiEVARAFPFSAVRQ----------SRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALL 155
Cdd:cd07112 81 SDALAVDVP----------SAANTFRWYAEAIdkvygevaptGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 156 AGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCG-NDIRR 233
Cdd:cd07112 151 AGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPgFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 234 VTLELGGKSAAVILDDA-DLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGP 312
Cdd:cd07112 231 VWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 313 MVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFAN 392
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 393 DSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCfDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
11-461 |
1.08e-161 |
|
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: 465.12 E-value: 1.08e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRT 90
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 MQsgLPR--EHIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPET 168
Cdd:cd07093 79 RD--IPRaaANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 169 PLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVIL 247
Cdd:cd07093 157 PLTAWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 248 DDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMA 327
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 328 SGVAEGAAVVTGGGRPQ--GFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTG 405
Cdd:cd07093 317 LARAEGATILTGGGRPElpDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 406 DLDHGLSIARRIRTGTVELNGSLV-GLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVrDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
11-461 |
1.66e-156 |
|
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: 451.50 E-value: 1.66e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRT 90
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 mqsglprehidnfiEVARA---FPFSA---------VRQSRNGNA--LVVHEPVGVVAAVIPWNAPqLVTII-KLAPALL 155
Cdd:cd07103 79 --------------EVDYAasfLEWFAeearriygrTIPSPAPGKriLVIKQPVGVVAAITPWNFP-AAMITrKIAPALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 156 AGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAER-EVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRV 234
Cdd:cd07103 144 AGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPaEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 235 TLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMV 314
Cdd:cd07103 224 SLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 315 SARQRSRVEGYMASGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDS 394
Cdd:cd07103 304 NERAVEKVEALVEDAVAKGAKVLTGGKRLG--LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559872 395 EYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGL-NAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07103 382 PYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDaEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
11-461 |
3.37e-155 |
|
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: 448.13 E-value: 3.37e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRT 90
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 mqsglpreHIDNFIEVARAF-----PFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPA 165
Cdd:cd07106 79 --------EVGGAVAWLRYTasldlPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 166 PETPLDSYLLAEMLQDAgLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAV 245
Cdd:cd07106 151 PFTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 246 ILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGY 325
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 326 MASGVAEGAAVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTG 405
Cdd:cd07106 310 VEDAKAKGAKVLAGGEPLDG--PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 406 DLDHGLSIARRIRTGTVELNGSL-VGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07106 388 DLERAEAVARRLEAGTVWINTHGaLDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
2-461 |
5.98e-155 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 448.68 E-value: 5.98e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:cd07119 8 EAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GCPISLSRTmqsglpreHIDNFIEVARAFPFSAVRQSRNGN-------ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPAL 154
Cdd:cd07119 88 GKTLRESEI--------DIDDVANCFRYYAGLATKETGEVYdvpphviSRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 155 LAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIV--PAErEVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIR 232
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVtgSGA-TVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 233 RVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGP 312
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 313 MVSARQRSRVEGYMASGVAEGAAVVTGGGRPQG--FDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEF 390
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdeLAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 391 ANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGLN-APLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAeAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
12-461 |
6.70e-144 |
|
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: 419.82 E-value: 6.70e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 12 VSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTm 91
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 92 qsglpreHIDNFIEVARaFPFSAVRQ----SRN--GN---ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVL 162
Cdd:cd07118 81 -------EIEGAADLWR-YAASLARTlhgdSYNnlGDdmlGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 163 KPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGK 241
Cdd:cd07118 153 KPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYgATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 242 SAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSR 321
Cdd:cd07118 233 NPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 322 VEGYMASGVAEGAAVVTGGGRPQGFDhGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGA 401
Cdd:cd07118 313 ITDYVDAGRAEGATLLLGGERLASAA-GLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 402 VFTGDLDHGLSIARRIRTGTVELNGSLVGL-NAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07118 392 VWSKDIDTALTVARRIRAGTVWVNTFLDGSpELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
2-461 |
9.95e-144 |
|
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: 420.22 E-value: 9.95e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSG-PWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQ 80
Cdd:cd07141 17 DSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIERDRAYLASLETLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 81 MGCPISLSRTMQsglprehIDNFIEVARAFPFSAVR-QSR----NGN--ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPA 153
Cdd:cd07141 97 NGKPFSKSYLVD-------LPGAIKVLRYYAGWADKiHGKtipmDGDffTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 154 LLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVS-EYLVTHPGVDKVAFTGSTAAGRRIAALCGN-DI 231
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAgAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsNL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 232 RRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIG 311
Cdd:cd07141 250 KRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 312 PMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFA 391
Cdd:cd07141 330 PQIDEEQFKKILELIESGKKEGAKLECGGKRHG--DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERA 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 392 NDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07141 408 NNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCyNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
3-461 |
2.23e-143 |
|
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: 419.50 E-value: 2.23e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:cd07144 19 SSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSrtmqsglPREHIDNFIEVARAFPFSA-------VRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALL 155
Cdd:cd07144 98 KPYHSN-------ALGDLDEIIAVIRYYAGWAdkiqgktIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 156 AGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPA-EREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRV 234
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 235 TLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERF-DSLIQSMPVGDPGDTATQIGPM 313
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFvEHVKQNYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 314 VSARQRSRVEGYMASGVAEGAAVVTGG-GRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFAN 392
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVYGGeKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKAN 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 393 DSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVG-LNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07144 411 DTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSdVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
11-461 |
2.35e-142 |
|
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: 415.60 E-value: 2.35e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSR- 89
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 90 ---------TMQSGLPrEHIDNFIEVARAFPFSAVRqsrngnALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTV 160
Cdd:cd07110 79 dvddvagcfEYYADLA-EQLDAKAERAVPLPSEDFK------ARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 161 VLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELG 239
Cdd:cd07110 152 VLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTgDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 240 GKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQR 319
Cdd:cd07110 232 GKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 320 SRVEGYMASGVAEGAAVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLS 399
Cdd:cd07110 312 EKVLSFIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2567559872 400 GAVFTGDLDHGLSIARRIRTGTVELNGS-LVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07110 392 AAVISRDAERCDRVAEALEAGIVWINCSqPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
1-461 |
2.60e-141 |
|
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: 413.58 E-value: 2.60e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 1 MSSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQ 80
Cdd:cd07088 7 VPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELAKLIVEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 81 MGCPISLSRtMQSGLPREHIDNFIEVARAFPFSAVRQSRNG-NALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCT 159
Cdd:cd07088 85 QGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNeNIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 160 VVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLEL 238
Cdd:cd07088 164 IVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRgSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 239 GGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQ 318
Cdd:cd07088 244 GGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 319 RSRVEGYMASGVAEGAAVVTGGGRPQGfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGL 398
Cdd:cd07088 324 LDKVEEMVERAVEAGATLLTGGKRPEG-EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 399 SGAVFTGDLDHGLSIARRIRTGTVELN----GSLVGLNAplgGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07088 403 TSYIYTENLNTAMRATNELEFGETYINrenfEAMQGFHA---GWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
3-461 |
2.63e-140 |
|
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: 411.35 E-value: 2.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:cd07559 12 PSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELLAVAETLDNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSRTMQSGLPREHIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVL 162
Cdd:cd07559 90 KPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 163 KPAPETPLDSYLLAEMLQDAgLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGK 241
Cdd:cd07559 170 KPASQTPLSILVLMELIGDL-LPKGVVNVVTgFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 242 SAAVILDDA-----DLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSA 316
Cdd:cd07559 249 SPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 317 RQRSRVEGYMASGVAEGAAVVTGGGRPQ--GFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDS 394
Cdd:cd07559 329 DQLEKILSYVDIGKEEGAEVLTGGERLTlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDT 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559872 395 EYGLSGAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07559 409 EYGLGGGVWTRDINRALRVARGIQTGRVWVNCyHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
3-461 |
1.66e-139 |
|
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: 409.43 E-value: 1.66e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSP-YTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:cd07131 10 SASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFPE--WRKVPAPRRAEYLFRAAELLKKRKEELARLVTREM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GCPISLSRtmqsGLPREHID----NFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAG 157
Cdd:cd07131 88 GKPLAEGR----GDVQEAIDmaqyAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 158 CTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAERE-VSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTL 236
Cdd:cd07131 164 NTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEeVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 237 ELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSA 316
Cdd:cd07131 244 EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 317 RQRSRVEGYMASGVAEGAAVVTGGGRPQG--FDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDS 394
Cdd:cd07131 324 AQLEKVLNYNEIGKEEGATLLLGGERLTGggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDT 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 395 EYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGLNA--PLGGFKSSGLG-RESGPEGLAAYTEIKSI 461
Cdd:cd07131 404 EYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhlPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
11-462 |
7.33e-139 |
|
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: 407.08 E-value: 7.33e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRT 90
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 -MQSGLprEHIDNFIEVARAFPFSAVrQSRNGN-ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPET 168
Cdd:cd07090 79 dIDSSA--DCLEYYAGLAPTLSGEHV-PLPGGSfAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 169 PLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILD 248
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 249 DADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMAS 328
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 329 GVAEGAAVVTGGGRPQ---GFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTG 405
Cdd:cd07090 316 AKQEGAKVLCGGERVVpedGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559872 406 DLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIG 462
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTyNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
11-461 |
1.52e-138 |
|
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: 406.05 E-value: 1.52e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDsgPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRT 90
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 MQsgLPREhIDNFIE---VARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPE 167
Cdd:cd07115 79 LD--VPRA-ADTFRYyagWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 168 TPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVI 246
Cdd:cd07115 156 TPLSALRIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 247 LDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYM 326
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 327 ASGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGD 406
Cdd:cd07115 316 DVGREEGARLLTGGKRPG--ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 407 LDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07115 394 LGRAHRVAAALKAGTVWINTyNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
11-463 |
1.59e-138 |
|
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: 405.85 E-value: 1.59e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRt 90
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 mqsglprehiDNFIEVARAFPFSA----------VRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTV 160
Cdd:cd07109 79 ----------ADVEAAARYFEYYGgaadklhgetIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 161 VLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELG 239
Cdd:cd07109 149 VVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 240 GKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGdPGDTATQIGPMVSARQR 319
Cdd:cd07109 229 GKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 320 SRVEGYMASGVAEGAAVVTGGGRPQGFDH-GYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGL 398
Cdd:cd07109 308 DRVEGFVARARARGARIVAGGRIAEGAPAgGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGL 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 399 SGAVFTGDLDHGLSIARRIRTGTVELN--GSLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGL 463
Cdd:cd07109 388 VAGVWTRDGDRALRVARRLRAGQVFVNnyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
3-461 |
6.01e-138 |
|
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: 405.30 E-value: 6.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:cd07117 12 GSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKELLAMVETLDNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSRTMQSGLPREHIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVL 162
Cdd:cd07117 90 KPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 163 KPAPETPLDSYLLAEMLQDAgLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGK 241
Cdd:cd07117 170 KPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 242 SAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSR 321
Cdd:cd07117 249 SANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 322 VEGYMASGVAEGAAVVTGGGR--PQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLS 399
Cdd:cd07117 329 ILSYVDIAKEEGAKILTGGHRltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2567559872 400 GAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07117 409 GGVFTKDINRALRVARAVETGRVWVNTyNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
11-461 |
2.68e-137 |
|
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: 402.48 E-value: 2.68e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRt 90
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 mQSGLPREhIDN---FIEVARAFP-FSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAP 166
Cdd:cd07092 78 -DDELPGA-VDNfrfFAGAARTLEgPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 167 ETPLDSYLLAEMLQDaGLPEGVVNIVPAERE-VSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAV 245
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 246 ILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGY 325
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 326 MAsGVAEGAAVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTG 405
Cdd:cd07092 315 VE-RAPAHARVLTGGRRAEG--PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 406 DLDHGLSIARRIRTGTVELNGSLVGLN-APLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAeMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
30-461 |
4.67e-136 |
|
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: 398.83 E-value: 4.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 30 DVDKAVSAARQAFdsGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPIslsrtMQSGLPREHIDNFIEVARA 109
Cdd:cd07104 1 DVDRAYAAAAAAQ--KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTR-----PKAAFEVGAAIAILREAAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 110 FPFSA----VRQSRNGN-ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDS-YLLAEMLQDAG 183
Cdd:cd07104 74 LPRRPegeiLPSDVPGKeSMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 184 LPEGVVNIVPAER-EVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIG 262
Cdd:cd07104 154 LPKGVLNVVPGGGsEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 263 SFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGR 342
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 343 pqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTV 422
Cdd:cd07104 314 -----EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2567559872 423 ELNGSLV--GLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07104 389 HINDQTVndEPHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
8-465 |
4.30e-134 |
|
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: 395.67 E-value: 4.30e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 8 TIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSlEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISL 87
Cdd:TIGR04284 16 TFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDETDWSRDT-ALRVRCLRQLRDALRAHVEELRELTIAEVGAPRML 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 88 SRTMQSGLPREHIDNFIEVARAFPFS-----AVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVL 162
Cdd:TIGR04284 95 TAGAQLEGPVDDLGFAADLAESYAWTtdlgvASPMGIPTRRTLRREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 163 KPAPETPLDSYLLAEML-QDAGLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGG 240
Cdd:TIGR04284 175 KPAPDTPWCAAVLGELIaEHTDFPPGVVNIVTsSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAATLKKVFLELGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 241 KSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRS 320
Cdd:TIGR04284 255 KSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCGPVISARQRD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 321 RVEGYMASGVAEGAAVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSG 400
Cdd:TIGR04284 335 RVQSYLDLAVAEGGRFACGGGRPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSG 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 401 AVFTGDLDHGLSIARRIRTGTVELNGSL-VGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGLPS 465
Cdd:TIGR04284 415 TVFGADPERAAAVAARVRTGTVNVNGGVwYSADAPFGGYKQSGIGREMGVAGFEEYLETKLIATAA 480
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
3-461 |
8.58e-134 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 394.66 E-value: 8.58e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:PRK13473 13 AGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENADEFARLESLNCG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLsrTMQSGLPREhIDNFievarAFPFSAVRQ---SRNGNALVVH------EPVGVVAAVIPWNAPQLVTIIKLAPA 153
Cdd:PRK13473 91 KPLHL--ALNDEIPAI-VDVF-----RFFAGAARClegKAAGEYLEGHtsmirrDPVGVVASIAPWNYPLMMAAWKLAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 154 LLAGCTVVLKPAPETPLDSYLLAEMLQDAgLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIR 232
Cdd:PRK13473 163 LAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRgATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 233 RVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGP 312
Cdd:PRK13473 242 RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 313 MVSARQRSRVEGYMASGVAEGAA-VVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFA 391
Cdd:PRK13473 322 LISAAHRDRVAGFVERAKALGHIrVVTGGEAPDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 392 NDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGLN-APLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSeMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
5-461 |
3.33e-133 |
|
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: 393.15 E-value: 3.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 5 SNDTIEVVSPY-TEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGC 83
Cdd:cd07097 12 GGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEELARLLTREEGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 84 PISLSRTmqsglprehidnfiEVARA---FPFSA---------VRQSRNGNALV--VHEPVGVVAAVIPWNAPQLVTIIK 149
Cdd:cd07097 90 TLPEARG--------------EVTRAgqiFRYYAgealrlsgeTLPSTRPGVEVetTREPLGVVGLITPWNFPIAIPAWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 150 LAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCG 228
Cdd:cd07097 156 IAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSgSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 229 NDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTAT 308
Cdd:cd07097 236 ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 309 QIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAV 388
Cdd:cd07097 316 DIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 389 EFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGL--NAPLGGFKSSGLG-RESGPEGLAAYTEIKSI 461
Cdd:cd07097 396 AIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVdyHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-461 |
5.03e-132 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 390.40 E-value: 5.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 1 MSSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQR-LSLAFDKNaDLLASLVTE 79
Cdd:PRK13252 16 VEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI--WAAMTAMERSRILRRaVDILRERN-DELAALETL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 80 QMGCPISLSRT--MQSGlpREHIDNFIEVARAFpfSAVRQSRNGNALV--VHEPVGVVAAVIPWNAPQLVTIIKLAPALL 155
Cdd:PRK13252 93 DTGKPIQETSVvdIVTG--ADVLEYYAGLAPAL--EGEQIPLRGGSFVytRREPLGVCAGIGAWNYPIQIACWKSAPALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 156 AGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVT 235
Cdd:PRK13252 169 AGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 236 LELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVS 315
Cdd:PRK13252 249 MELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 316 ARQRSRVEGYMASGVAEGAAVVTGGGR--PQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFAND 393
Cdd:PRK13252 329 FAHRDKVLGYIEKGKAEGARLLCGGERltEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARAND 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2567559872 394 SEYGLSGAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:PRK13252 409 TEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-461 |
1.30e-131 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 389.86 E-value: 1.30e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 8 TIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAF---DSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCP 84
Cdd:PLN02467 24 RIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 85 ISlsrtmqsglprEHIDNFIEVARAFPFSAVR----QSRNGNAL----------VVHEPVGVVAAVIPWNAPQLVTIIKL 150
Cdd:PLN02467 104 LD-----------EAAWDMDDVAGCFEYYADLaealDAKQKAPVslpmetfkgyVLKEPLGVVGLITPWNYPLLMATWKV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 151 APALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGN 229
Cdd:PLN02467 173 APALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTgLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 230 DIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQ 309
Cdd:PLN02467 253 MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 310 IGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVE 389
Cdd:PLN02467 333 LGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2567559872 390 FANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGL-NAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:PLN02467 413 LANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFcQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
2-461 |
2.07e-130 |
|
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: 386.11 E-value: 2.07e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDsGPWSRT-SLEDRIEVLQRLSLAFDKNADLLASLVTEQ 80
Cdd:cd07143 17 DSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE-TDWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 81 MGCPISlsrTMQSGlprehidNFIEVARAFPFSA----------VRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKL 150
Cdd:cd07143 96 NGKTFG---TAKRV-------DVQASADTFRYYGgwadkihgqvIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 151 APALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRI-AALCG 228
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYgRTCGNAISSHMDIDKVAFTGSTLVGRKVmEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 229 NDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTAT 308
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 309 QIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRpQGfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAV 388
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGGKR-HG-NEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567559872 389 EFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELN-GSLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07143 404 KRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
4-462 |
3.68e-130 |
|
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: 385.12 E-value: 3.68e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 4 TSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAfdSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGc 83
Cdd:cd07151 7 TSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 84 pislSRTMQSGLPREHIDNFIEVARAFPF--------SAVRQSRNgnaLVVHEPVGVVAAVIPWNAPQLVTIIKLAPALL 155
Cdd:cd07151 84 ----STRIKANIEWGAAMAITREAATFPLrmegrilpSDVPGKEN---RVYREPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 156 AGCTVVLKPAPETPLDS-YLLAEMLQDAGLPEGVVNIV-PAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRR 233
Cdd:cd07151 157 LGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVvGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 234 VTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPM 313
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 314 VSARQRSRVEGYMASGVAEGAAVVTGGGRpqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFAND 393
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEA-----EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 394 SEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVG--LNAPLGGFKSSGLGRESGPEGLAAYTEIKSIG 462
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdePHVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
10-461 |
9.84e-130 |
|
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: 383.22 E-value: 9.84e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 10 EVVSPYTEQVLAAVPSATKADVDKAVSAARQAFdsGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPIsLSR 89
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTY-GKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 90 TMQSGLPREHIDNFIEVARAFPFSAVRQSRNGN-ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPET 168
Cdd:cd07150 79 WFETTFTPELLRAAAGECRRVRGETLPSDSPGTvSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 169 PLDSYLLAEMLQDAGLPEGVVNIVPAER-EVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVIL 247
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFNVVTGGGaEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 248 DDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMA 327
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 328 SGVAEGAAVVTGGGRpqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDL 407
Cdd:cd07150 319 DAVAKGAKLLTGGKY-----DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 408 DHGLSIARRIRTGTVELNGSLV--GLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07150 394 QRAFKLAERLESGMVHINDPTIldEAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
9-461 |
1.13e-129 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 383.10 E-value: 1.13e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 9 IEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGpwSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLS 88
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM--KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 89 RtmqsglprehidnfIEVARA------------------FPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKL 150
Cdd:cd07149 79 R--------------KEVDRAietlrlsaeeakrlagetIPFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 151 APALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAERE-VSEYLVTHPGVDKVAFTGSTAAGRRIAALCGn 229
Cdd:cd07149 145 GPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAG- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 230 dIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQ 309
Cdd:cd07149 224 -LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 310 IGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRpqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVE 389
Cdd:cd07149 303 VGPMISEAEAERIEEWVEEAVEGGARLLTGGKR-----DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIA 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567559872 390 FANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELN-GSLVGLNA-PLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07149 378 MANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdSSTFRVDHmPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
3-461 |
1.25e-128 |
|
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: 381.46 E-value: 1.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:cd07142 15 AASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSRTMQSGLPREHIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVL 162
Cdd:cd07142 95 KPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 163 KPAPETPLDSYLLAEMLQDAGLPEGVVNIVPA-EREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGN-DIRRVTLELGG 240
Cdd:cd07142 175 KPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 241 KSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRS 320
Cdd:cd07142 255 KSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 321 RVEGYMASGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSG 400
Cdd:cd07142 335 KILSYIEHGKEEGATLITGGDRIG--SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAA 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 401 AVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07142 413 GVFSKNIDTANTLSRALKAGTVWVNCyDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
31-461 |
1.55e-127 |
|
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: 376.80 E-value: 1.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 31 VDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTmqsglprehidnfiEV---A 107
Cdd:cd07100 1 IEAALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA--------------EVekcA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 108 RAFPFSA----------VRQSRNGNALVVHEPVGVVAAVIPWNAP--QLVTIikLAPALLAGCTVVLKPAPETPLDSYLL 175
Cdd:cd07100 65 WICRYYAenaeafladePIETDAGKAYVRYEPLGVVLGIMPWNFPfwQVFRF--AAPNLMAGNTVLLKHASNVPGCALAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 176 AEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAA 255
Cdd:cd07100 143 EELFREAGFPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 256 VESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMASGVAEGAA 335
Cdd:cd07100 223 VKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 336 VVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIAR 415
Cdd:cd07100 303 LLLGGKRPDG--PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2567559872 416 RIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07100 381 RLEAGMVFINGmVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
11-464 |
1.66e-126 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 375.17 E-value: 1.66e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSR- 89
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 90 --TMQSGLprehIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPE 167
Cdd:cd07107 79 dvMVAAAL----LDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 168 TPLDSYLLAEMLQDAgLPEGVVNIVPAEREVS-EYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVI 246
Cdd:cd07107 155 APLSALRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 247 LDDADLDAAVESLRIG-SFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGY 325
Cdd:cd07107 234 FPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 326 MASGVAEGAAVVTGGGRPQG--FDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVF 403
Cdd:cd07107 314 IDSAKREGARLVTGGGRPEGpaLEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIW 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 404 TGDLDHGLSIARRIRTGTVELNGSLVG-LNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGLP 464
Cdd:cd07107 394 TNDISQAHRTARRVEAGYVWINGSSRHfLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
11-461 |
3.67e-124 |
|
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: 369.38 E-value: 3.67e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFdsGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPIslsRT 90
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNAL---RT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 MQSGLPREHIDNFIEvarafpFSAVRQSRNGNAL---------VVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVV 161
Cdd:cd07108 76 QARPEAAVLADLFRY------FGGLAGELKGETLpfgpdvltyTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 162 LKPAPETPLDSYLLAEMLQDAgLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGG 240
Cdd:cd07108 150 LKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYgEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 241 KSAAVILDDADLDAAVESLRIGS-FRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQR 319
Cdd:cd07108 229 KSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 320 SRVEGYMASGVAE-GAAVVTGGGRPQG--FDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEY 396
Cdd:cd07108 309 AKVCGYIDLGLSTsGATVLRGGPLPGEgpLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 397 GLSGAVFTGDLDHGLSIARRIRTGTVELN-GSLVGLNAPLGGFKSSGLGRESGPEG-LAAYTEIKSI 461
Cdd:cd07108 389 GLAAYVWTRDLGRALRAAHALEAGWVQVNqGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
6-455 |
6.05e-124 |
|
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: 369.80 E-value: 6.05e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 6 NDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPI 85
Cdd:cd07111 36 RKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 86 SLSRTMQSGLprehidnfieVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPA 165
Cdd:cd07111 114 RESRDCDIPL----------VARHFYHHAGWAQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 166 PETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAV 245
Cdd:cd07111 184 EYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 246 ILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGY 325
Cdd:cd07111 264 VFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIREL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 326 MASGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTG 405
Cdd:cd07111 344 VEEGRAEGADVFQPGADLP--SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSE 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 406 DLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAY 455
Cdd:cd07111 422 NLSLALEVALSLKAGVVWINGhNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
2-461 |
2.38e-123 |
|
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: 367.92 E-value: 2.38e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEdRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:cd07113 10 AGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAE-RGRILLRLADLIEQHGEELAQLETLCS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GCPISLSRTMQSGLPREHIDNFI---------EVARAFPfsavrqSRNG---NALVVHEPVGVVAAVIPWNAPQLVTIIK 149
Cdd:cd07113 89 GKSIHLSRAFEVGQSANFLRYFAgwatkingeTLAPSIP------SMQGeryTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 150 LAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGN 229
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 230 DIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQ 309
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 310 IGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVE 389
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAG--EGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQ 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2567559872 390 FANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07113 401 LINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMhTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
3-464 |
2.45e-123 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 368.76 E-value: 2.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:PLN02766 32 AASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSRTMQSGLPREHIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVL 162
Cdd:PLN02766 112 KLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 163 KPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVS-EYLVTHPGVDKVAFTGSTAAGRRI-AALCGNDIRRVTLELGG 240
Cdd:PLN02766 192 KPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAgAAIASHMDVDKVSFTGSTEVGRKImQAAATSNLKQVSLELGG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 241 KSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRS 320
Cdd:PLN02766 272 KSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 321 RVEGYMASGVAEGAAVVTgGGRPQGfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSG 400
Cdd:PLN02766 352 KILSYIEHGKREGATLLT-GGKPCG-DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAA 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2567559872 401 AVFTGDLDHGLSIARRIRTGTVELNGSLV-GLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGLP 464
Cdd:PLN02766 430 GIVTKDLDVANTVSRSIRAGTIWVNCYFAfDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
9-463 |
4.73e-123 |
|
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: 366.67 E-value: 4.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 9 IEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLS 88
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 89 RtmqsglprehidnfIEVARA------------------FPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKL 150
Cdd:cd07145 79 R--------------VEVERTirlfklaaeeakvlrgetIPVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 151 APALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGN 229
Cdd:cd07145 145 APAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYgSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 230 DIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQ 309
Cdd:cd07145 225 TGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 310 IGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQgfdhGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVE 389
Cdd:cd07145 305 LGPLISPEAVERMENLVNDAVEKGGKILYGGKRDE----GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVE 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 390 FANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGS--LVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGL 463
Cdd:cd07145 381 IANSTEYGLQASVFTNDINRALKVARELEAGGVVINDStrFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
12-463 |
1.11e-121 |
|
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: 362.82 E-value: 1.11e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 12 VSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSlEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTM 91
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 92 QSGLPREhIDNFIEVARAFPfSAVRQSRNGN-ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPL 170
Cdd:cd07120 81 ISGAISE-LRYYAGLARTEA-GRMIEPEPGSfSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 171 DSYLLAEMLQDA-GLPEGVVNIVPAER-EVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILD 248
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGsEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 249 DADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMAS 328
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 329 GVAEGAAVVTGGGRPQ-GFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDL 407
Cdd:cd07120 319 AIAAGAEVVLRGGPVTeGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 408 DHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGL 463
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDwNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
37-461 |
1.87e-120 |
|
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: 356.54 E-value: 1.87e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 37 AARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRtMQSGLPREHIDNFIEVARAFP-FSAV 115
Cdd:cd06534 2 AARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGgPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 116 RQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVP-A 194
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPgG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 195 EREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLK 274
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 275 TRIIVSKSRERELLERFDsliqsmpvgdpgdtatqigpmvsarqrsrvegymasgvaegaavvtgggrpqgfdhgyfvep 354
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 355 TVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVG--LN 432
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvgPE 336
|
410 420
....*....|....*....|....*....
gi 2567559872 433 APLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
1-463 |
7.17e-120 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 359.77 E-value: 7.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 1 MSSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQ 80
Cdd:PLN02278 34 TDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRWYDLIIANKEDLAQLMTLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 81 MGCPISLSRTMQSGlPREHIDNFIEVA-RAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCT 159
Cdd:PLN02278 112 QGKPLKEAIGEVAY-GASFLEYFAEEAkRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 160 VVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLEL 238
Cdd:PLN02278 191 VVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDaPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLEL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 239 GGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQ 318
Cdd:PLN02278 271 GGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 319 RSRVEGYMASGVAEGAAVVTGGGRpqGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGL 398
Cdd:PLN02278 351 VQKVESHVQDAVSKGAKVLLGGKR--HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGL 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 399 SGAVFTGDLDHGLSIARRIRTGTVELNGSLVGLN-APLGGFKSSGLGRESGPEGLAAYTEIKSIGL 463
Cdd:PLN02278 429 AAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEvAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
3-461 |
2.65e-119 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 359.19 E-value: 2.65e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAfdSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTeqmg 82
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQ---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 cpislsrtMQSGLPREHIdnFIEV----------ARAFPfSAVRQSRNGNAL-------VVHEPVGVVAAVIPWNAPQLV 145
Cdd:PRK09407 102 --------LETGKARRHA--FEEVldvaltaryyARRAP-KLLAPRRRAGALpvltkttELRQPKGVVGVISPWNYPLTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 146 TIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHpgVDKVAFTGSTAAGRRIA 224
Cdd:PRK09407 171 AVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPgPVVGTALVDN--ADYLMFTGSTATGRVLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 225 ALCGndiRR---VTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVG 301
Cdd:PRK09407 249 EQAG---RRligFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 302 DPGDTATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGG-GRPqgfDHG-YFVEPTVFSGVTPSMTIAREEIFGPVISVL 379
Cdd:PRK09407 326 AGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGkARP---DLGpLFYEPTVLTGVTPDMELAREETFGPVVSVY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 380 ACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVG----LNAPLGGFKSSGLGRESGPEGLAAY 455
Cdd:PRK09407 403 PVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgsVDAPMGGMKDSGLGRRHGAEGLLKY 482
|
....*.
gi 2567559872 456 TEIKSI 461
Cdd:PRK09407 483 TESQTI 488
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
12-463 |
2.97e-118 |
|
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: 353.86 E-value: 2.97e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 12 VSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTM 91
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 92 QSGLPrEHIDNFIEVA-RAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPL 170
Cdd:cd07102 79 IRGML-ERARYMISIAeEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 171 DSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDA 250
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 251 DLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMASGV 330
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 331 AEGAAVVTGGGR-PQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDH 409
Cdd:cd07102 318 AKGARALIDGALfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2567559872 410 GLSIARRIRTGTVELN-GSLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGL 463
Cdd:cd07102 398 AEALGEQLETGTVFMNrCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
30-461 |
4.38e-118 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 353.04 E-value: 4.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 30 DVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCP-------ISLSRTMqsglprehIDN 102
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATaawagfnVDLAAGM--------LRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 103 FIEVARAFPFSAVRQSRNG-NALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQD 181
Cdd:cd07105 71 AASLITQIIGGSIPSDKPGtLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 182 AGLPEGVVNIVPAERE----VSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVE 257
Cdd:cd07105 151 AGLPKGVLNVVTHSPEdapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 258 SLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDpgdtaTQIGPMVSARQRSRVEGYMASGVAEGAAVV 337
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 338 TGGGRPQGFDhGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRI 417
Cdd:cd07105 306 VGGLADESPS-GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRI 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2567559872 418 RTGTVELNGSLVGLNA--PLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07105 385 ESGAVHINGMTVHDEPtlPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
7-461 |
5.42e-118 |
|
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: 354.18 E-value: 5.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 7 DTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPIS 86
Cdd:cd07086 13 ETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE--WRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 87 LSRtmqsGLPREHID--NFievarafpfsAVRQSRNGNALVVH------------EPVGVVAAVIPWNAPQLVTIIKLAP 152
Cdd:cd07086 91 EGL----GEVQEMIDicDY----------AVGLSRMLYGLTIPserpghrlmeqwNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 153 ALLAGCTVVLKPAPETPLDSY----LLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCG 228
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIavtkILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 229 NDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTAT 308
Cdd:cd07086 237 RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 309 QIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAV 388
Cdd:cd07086 317 LVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 389 EFANDSEYGLSGAVFTGDldhgLSIARRIR------TGTVELNGSLVG--LNAPLGGFKSSGLGRESGPEGLAAYTEIKS 460
Cdd:cd07086 397 AINNDVPQGLSSSIFTED----LREAFRWLgpkgsdCGIVNVNIPTSGaeIGGAFGGEKETGGGRESGSDAWKQYMRRST 472
|
.
gi 2567559872 461 I 461
Cdd:cd07086 473 C 473
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
12-461 |
4.06e-117 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 351.14 E-value: 4.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 12 VSPYTEQVLAAVPSATKADVDKAVSAARQAfdSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTm 91
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA--QRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 92 QSGLPREHIDNFIEVA------RAFPFSAVrqSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPA 165
Cdd:cd07099 78 EVLLALEAIDWAARNAprvlapRKVPTGLL--MPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 166 PETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHpGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAV 245
Cdd:cd07099 156 EVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 246 ILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGY 325
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 326 MASGVAEGAAVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTG 405
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNG--GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2567559872 406 DLDHGLSIARRIRTGTVELNGSLVGL---NAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINDVLLTAgipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
13-462 |
8.14e-117 |
|
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: 350.46 E-value: 8.14e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 13 SPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTeqmgcpislsrtMQ 92
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQ------------LE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 93 SGLPREH----IDNFIEVARAFPFSAVR---QSRNGNAL-------VVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGC 158
Cdd:cd07101 68 TGKARRHafeeVLDVAIVARYYARRAERllkPRRRRGAIpvltrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 159 TVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHpgVDKVAFTGSTAAGRRIAALCGNDIRRVTLE 237
Cdd:cd07101 148 AVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPgSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 238 LGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSAR 317
Cdd:cd07101 226 LGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 318 QRSRVEGYMASGVAEGAAVVTGG-GRPqgfDHG-YFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSE 395
Cdd:cd07101 306 QLDRVTAHVDDAVAKGATVLAGGrARP---DLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTD 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 396 YGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLV----GLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIG 462
Cdd:cd07101 383 YGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAaawaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-461 |
4.53e-116 |
|
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: 350.37 E-value: 4.53e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 5 SNDTIEVVSPY-TEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLS-LAFDKNADLLASLVTEqmg 82
Cdd:cd07124 44 TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAaLLRRRRFELAAWMVLE--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 cpISLSRTMQSGLPREHIDnFIEV-------ARAFPFSAVRQSRNGNalvVHEPVGVVAAVIPWNAPQLVTIIKLAPALL 155
Cdd:cd07124 119 --VGKNWAEADADVAEAID-FLEYyaremlrLRGFPVEMVPGEDNRY---VYRPLGVGAVISPWNFPLAILAGMTTAALV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 156 AGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGND---- 230
Cdd:cd07124 193 TGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPgEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpgq 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 231 --IRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTAT 308
Cdd:cd07124 273 kwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 309 QIGPMVSARQRSRVEGYMASGVAEGAaVVTGGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAV 388
Cdd:cd07124 353 YMGPVIDKGARDRIRRYIEIGKSEGR-LLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEAL 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2567559872 389 EFANDSEYGLSGAVFTGDLDHgLSIARR-IRTGTVELN----GSLVGLNaPLGGFKSSGLG-RESGPEGLAAYTEIKSI 461
Cdd:cd07124 432 EIANDTEYGLTGGVFSRSPEH-LERARReFEVGNLYANrkitGALVGRQ-PFGGFKMSGTGsKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
18-457 |
1.75e-112 |
|
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: 338.88 E-value: 1.75e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 18 QVLAAVPSATKADVDKAVSAARQAfdSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGcpislSRTMQSGLPR 97
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-----SIRPKAGFEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 98 EHIDNFIEVARA---------FPFSAVRQSrngnaLVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPET 168
Cdd:cd07152 75 GAAIGELHEAAGlptqpqgeiLPSAPGRLS-----LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 169 PLDS-YLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVIL 247
Cdd:cd07152 150 PVSGgVVIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 248 DDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMA 327
Cdd:cd07152 230 DDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 328 SGVAEGAAVVTGGGRpqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDL 407
Cdd:cd07152 310 DSVAAGARLEAGGTY-----DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2567559872 408 DHGLSIARRIRTGTVELNGSLV--GLNAPLGGFKSSGLG-RESGPEGLAAYTE 457
Cdd:cd07152 385 GRAMALADRLRTGMLHINDQTVndEPHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
11-459 |
1.49e-110 |
|
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: 334.40 E-value: 1.49e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRt 90
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT--WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 MQSGLPREHIDNFIEVARAFPFSAVRQSRNGN-ALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETP 169
Cdd:TIGR01780 78 GEILYAASFLEWFAEEAKRVYGDTIPSPQSDKrLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 170 LDSYLLAEMLQDAGLPEGVVNIVPAER--EVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVIL 247
Cdd:TIGR01780 158 LSALALARLAEQAGIPKGVLNVITGSRakEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 248 DDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMA 327
Cdd:TIGR01780 238 DDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 328 SGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDL 407
Cdd:TIGR01780 318 DAVEKGAKVVTGGKRHE--LGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2567559872 408 DHGLSIARRIRTGTVELNGSLVG-LNAPLGGFKSSGLGRESGPEGLAAYTEIK 459
Cdd:TIGR01780 396 SRIWRVAEALEYGMVGINTGLISnVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-464 |
1.64e-110 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 337.16 E-value: 1.64e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMG 82
Cdd:PLN02466 69 AASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 CPISLSRTMQsgLPRehidnfieVARAFPFSA----------VRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAP 152
Cdd:PLN02466 149 KPYEQSAKAE--LPM--------FARLFRYYAgwadkihgltVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 153 ALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIvpaereVSEY-------LVTHPGVDKVAFTGSTAAGRRIAA 225
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNV------VSGFgptagaaLASHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 226 LCGN-DIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPG 304
Cdd:PLN02466 293 LAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPF 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 305 DTATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESE 384
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG--SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 385 DQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVgLNA--PLGGFKSSGLGRESGPEGLAAYTEIKSIG 462
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDV-FDAaiPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
..
gi 2567559872 463 LP 464
Cdd:PLN02466 530 TP 531
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
2-461 |
1.34e-109 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 333.40 E-value: 1.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:PRK09847 30 AAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GCPISLS-RTMQSGLPR------EHIDN-FIEVARAfpfsavrqSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPA 153
Cdd:PRK09847 110 GKPIRHSlRDDIPGAARairwyaEAIDKvYGEVATT--------SSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 154 LLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPA-EREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCG-NDI 231
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 232 RRVTLELGGKSAAVILDDA-DLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQI 310
Cdd:PRK09847 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 311 GPMVSARQRSRVEGYMASGVAEGAAVVTggGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEF 390
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKGQLLLD--GRNAG--LAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQL 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 391 ANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVG-LNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:PRK09847 418 ANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGdMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
2-461 |
1.04e-107 |
|
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: 327.94 E-value: 1.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:cd07085 11 ESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDELARLITLEH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GCPIS-----LSRTMQSglprehidnfIEVARAFPF----SAVRQSRNG-NALVVHEPVGVVAAVIPWNAPQLVTIIKLA 151
Cdd:cd07085 89 GKTLAdargdVLRGLEV----------VEFACSIPHllkgEYLENVARGiDTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 152 PALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDI 231
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 232 RRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVC-SLKTRIIVSKSRErELLERFDSLIQSMPVGDPGDTATQI 310
Cdd:cd07085 239 KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCmALSVAVAVGDEAD-EWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 311 GPMVSARQRSRVEGYMASGVAEGAAVVTGG--GRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAV 388
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGrgVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 389 EFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNgslVGLNAPL-----GGFKSSGLGRES--GPEGLAAYTEIKSI 461
Cdd:cd07085 398 AIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLaffsfGGWKGSFFGDLHfyGKDGVRFYTQTKTV 474
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
9-463 |
9.63e-107 |
|
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: 324.58 E-value: 9.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 9 IEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDsgPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLS 88
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 89 RtmqsglprehidnfIEVARA---FPFSAVRQSRNGN---------------ALVVHEPVGVVAAVIPWNAPQLVTIIKL 150
Cdd:cd07147 79 R--------------GEVARAidtFRIAAEEATRIYGevlpldisargegrqGLVRRFPIGPVSAITPFNFPLNLVAHKV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 151 APALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNd 230
Cdd:cd07147 145 APAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 231 iRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQI 310
Cdd:cd07147 224 -KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 311 GPMVSARQRSRVEGYMASGVAEGAAVVTGGGRpqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEF 390
Cdd:cd07147 303 GPMISESEAERVEGWVNEAVDAGAKLLTGGKR-----DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAA 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2567559872 391 ANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNG--SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSIGL 463
Cdd:cd07147 378 VNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDvpTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
5-461 |
1.73e-105 |
|
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: 321.83 E-value: 1.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 5 SNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFdSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCP 84
Cdd:cd07082 14 SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 85 ISLS-----RTMqsglprEHIDNFIEVAR-----AFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPAL 154
Cdd:cd07082 93 LKDAlkevdRTI------DYIRDTIEELKrldgdSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 155 LAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGndIRR 233
Cdd:cd07082 167 IMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 234 VTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPM 313
Cdd:cd07082 245 LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 314 VSARQRSRVEGYMASGVAEGAAVVTGGGRpqgfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFAND 393
Cdd:cd07082 325 IDPKSADFVEGLIDDAVAKGATVLNGGGR----EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2567559872 394 SEYGLSGAVFTGDLDHGLSIARRIRTGTVELN-------GSLvglnaPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07082 401 SNYGLQASIFTKDINKARKLADALEVGTVNINskcqrgpDHF-----PFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
9-461 |
6.58e-104 |
|
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: 317.45 E-value: 6.58e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 9 IEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLS 88
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 89 RtMQSGLPREHIDNFIEVAR-----AFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLK 163
Cdd:cd07094 79 R-VEVDRAIDTLRLAAEEAErirgeEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 164 PAPETPLDSYLLAEMLQDAGLPEGVVNIVPAER-EVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGndIRRVTLELGGKS 242
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEReVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 243 AAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRV 322
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 323 EGYMASGVAEGAAVVTGGGRpqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAV 402
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGER-----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 403 FTGDLDHGLSIARRIRTGTVELNGS--LVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVNDSsaFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-461 |
8.85e-104 |
|
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: 318.29 E-value: 8.85e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 1 MSSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQ 80
Cdd:cd07140 15 VDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 81 MGCPISLSRtmqsglpREHIDNFIEVARAF------------PFSAVRQSRNgNALVVHEPVGVVAAVIPWNAPQLVTII 148
Cdd:cd07140 95 SGAVYTLAL-------KTHVGMSIQTFRYFagwcdkiqgktiPINQARPNRN-LTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 149 KLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALC 227
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPgSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 228 G-NDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDT 306
Cdd:cd07140 247 AvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 307 ATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQgfDHGYFVEPTVFSGVTPSMTIAREEIFGPV--ISVLACESE 384
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVD--RPGFFFEPTVFTDVEDHMFIAKEESFGPImiISKFDDGDV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559872 385 DQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTyNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
9-463 |
8.91e-104 |
|
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: 316.99 E-value: 8.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 9 IEVVSPYTEQVLAAVPSATKADVDKAVSAARqafdsGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGcpISLS 88
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALAA-----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESG--LCLK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 89 RTMqsglpREhIDNFIEVARA--------------FPFSAVRQSRNGnaLVVHEPVGVVAAVIPWNAPQLVTIIKLAPAL 154
Cdd:cd07146 74 DTR-----YE-VGRAADVLRFaaaealrddgesfsCDLTANGKARKI--FTLREPLGVVLAITPFNHPLNQVAHKIAPAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 155 LAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIV-PAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGndIRR 233
Cdd:cd07146 146 AANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVtGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 234 VTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPM 313
Cdd:cd07146 224 QLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 314 VSARQRSRVEGYMASGVAEGAAVVTGGGRpqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFAND 393
Cdd:cd07146 304 IDEEAAIQIENRVEEAIAQGARVLLGNQR-----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNS 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567559872 394 SEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGsLVGL---NAPLGGFKSSGLG-RESGPEGLAAYTEIKSIGL 463
Cdd:cd07146 379 TAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFrseLSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-461 |
7.06e-102 |
|
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: 312.85 E-value: 7.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 10 EVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISlsR 89
Cdd:cd07116 19 DNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVR--E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 90 TMQSGLPR--EHIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPE 167
Cdd:cd07116 95 TLAADIPLaiDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 168 TPLDSYLLAEMLQDAgLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVI 246
Cdd:cd07116 175 TPASILVLMELIGDL-LPPGVVNVVNgFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 247 L------DDADLDAAVESLRIGSFrNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRS 320
Cdd:cd07116 254 FadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 321 RVEGYMASGVAEGAAVVTGGGR---PQGFDHGYFVEPTVFSGvtPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYG 397
Cdd:cd07116 333 KILSYIDIGKEEGAEVLTGGERnelGGLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYG 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2567559872 398 LSGAVFTGDLDHGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07116 411 LGAGVWTRDGNTAYRMGRGIQAGRVWTNCyHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
4-461 |
6.47e-98 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 303.78 E-value: 6.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 4 TSNDTIEVVSPY-TEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLS-LAFDKNADLLASLVTEqm 81
Cdd:PRK03137 47 TTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAaIIRRRKHEFSAWLVKE-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 gcpislsrtmqSGLP--------REHIDnFIEV-ARafpfSAVR-------QSRNG--NALVvHEPVGVVAAVIPWNAPQ 143
Cdd:PRK03137 123 -----------AGKPwaeadadtAEAID-FLEYyAR----QMLKladgkpvESRPGehNRYF-YIPLGVGVVISPWNFPF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 144 LVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRR 222
Cdd:PRK03137 186 AIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSgSEVGDYLVDHPKTRFITFTGSREVGLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 223 I---AALCG---NDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQ 296
Cdd:PRK03137 266 IyerAAKVQpgqIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 297 SMPVGDPGDtATQIGPMVSARQRSRVEGYMASGVAEGAaVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVI 376
Cdd:PRK03137 346 ELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEGR-LVLGGEGDDS--KGYFIQPTIFADVDPKARIMQEEIFGPVV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 377 SVLACESEDQAVEFANDSEYGLSGAVFTGDLDHgLSIARR-IRTGTVELN----GSLVGLNaPLGGFKSSGL-GRESGPE 450
Cdd:PRK03137 422 AFIKAKDFDHALEIANNTEYGLTGAVISNNREH-LEKARReFHVGNLYFNrgctGAIVGYH-PFGGFNMSGTdSKAGGPD 499
|
490
....*....|.
gi 2567559872 451 GLAAYTEIKSI 461
Cdd:PRK03137 500 YLLLFLQAKTV 510
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
14-461 |
2.33e-96 |
|
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: 298.44 E-value: 2.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 14 PYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLA---------SLVTEQMG-- 82
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQRE--WAKTSFAERRKVLRSLLKYILENQEEICrvacrdtgkTMVDASLGei 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 ---CPiSLSRTMQSG----LPREHIDNFIEVARAfpfsavrqsrngnALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALL 155
Cdd:cd07098 81 lvtCE-KIRWTLKHGekalRPESRPGGLLMFYKR-------------ARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 156 AGCTVVLKPAPETPLDSY----LLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDI 231
Cdd:cd07098 147 AGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 232 RRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIG 311
Cdd:cd07098 227 TPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 312 PMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGFDH--GYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVE 389
Cdd:cd07098 307 AMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYpqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2567559872 390 FANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELN---GSLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07098 387 IANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
59-455 |
4.72e-95 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 293.18 E-value: 4.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 59 LQRLSLAFDKNADLLASLVTEQMGCPISLSRTmQSGLPREHIDNFIEVARAFPFSAVRQSR-NGNALVVHEPVGVVAAVI 137
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDYMAEWARRYEGEIIQSDRpGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 138 PWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGS 216
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRgETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 217 TAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQ 296
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 297 SMPVGDPGD-TATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPV 375
Cdd:PRK10090 240 AVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEG--KGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 376 ISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELN----GSLVGLNAplgGFKSSGLGRESGPEG 451
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINrenfEAMQGFHA---GWRKSGIGGADGKHG 394
|
....
gi 2567559872 452 LAAY 455
Cdd:PRK10090 395 LHEY 398
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
5-459 |
1.00e-92 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 289.50 E-value: 1.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 5 SNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCP 84
Cdd:PRK11241 24 NGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 85 ISLSRTmQSGLPREHIDNFIEVA-RAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLK 163
Cdd:PRK11241 102 LAEAKG-EISYAASFIEWFAEEGkRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 164 PAPETPLDSYLLAEMLQDAGLPEGVVNIVPAER-EVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKS 242
Cdd:PRK11241 181 PASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 243 AAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRV 322
Cdd:PRK11241 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 323 EGYMASGVAEGAAVVTgGGRPQGFDhGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAV 402
Cdd:PRK11241 341 EEHIADALEKGARVVC-GGKAHELG-GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2567559872 403 FTGDLDHGLSIARRIRTGTVELNGSLVGLN-APLGGFKSSGLGRESGPEGLAAYTEIK 459
Cdd:PRK11241 419 YARDLSRVFRVGEALEYGIVGINTGIISNEvAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
9-461 |
7.03e-89 |
|
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: 280.60 E-value: 7.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 9 IEVVSPY-TEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISL 87
Cdd:TIGR01237 48 IVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA--WKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 88 SRTMQS---GLPREHIDNFIEVARAFPFSAVRQSRNGnalVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKP 164
Cdd:TIGR01237 126 ADAEVAeaiDFMEYYARQMIELAKGKPVNSREGETNQ---YVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 165 APETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRI---AALCG---NDIRRVTLE 237
Cdd:TIGR01237 203 AEAAPVIAAKFVEILEEAGLPKGVVQFVPGSgSEVGDYLVDHPKTSLITFTGSREVGTRIferAAKVQpgqKHLKRVIAE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 238 LGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSAR 317
Cdd:TIGR01237 283 MGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 318 QRSRVEGYMASGVAEGAAVVTGGGRPQgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYG 397
Cdd:TIGR01237 363 SFNKIMEYIEIGKAEGRLVSGGCGDDS---KGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYG 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2567559872 398 LSGAVFTGDLDHGLSIARRIRTGTVELN----GSLVGLNaPLGGFKSSGLGRES-GPEGLAAYTEIKSI 461
Cdd:TIGR01237 440 LTGGVISNNRDHINRAKAEFEVGNLYFNrnitGAIVGYQ-PFGGFKMSGTDSKAgGPDYLALFMQAKTV 507
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
12-461 |
1.03e-87 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 275.97 E-value: 1.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 12 VSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSR-- 89
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 90 -TMQSGLprehIDNFIEVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPET 168
Cdd:PRK13968 90 vAKSANL----CDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 169 PLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILD 248
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 249 DADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMAS 328
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 329 GVAEGAAVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLD 408
Cdd:PRK13968 326 TLAEGARLLLGGEKIAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2567559872 409 HGLSIARRIRTGTVELNG-SLVGLNAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:PRK13968 404 QARQMAARLECGGVFINGyCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
9-461 |
3.88e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 266.60 E-value: 3.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 9 IEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLS 88
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 89 RTMQSGLPR------EHIDNFI--EVARAfpfSAVRQSRngnALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTV 160
Cdd:PRK09406 81 KAEALKCAKgfryyaEHAEALLadEPADA---AAVGASR---AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 161 VLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGG 240
Cdd:PRK09406 155 LLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 241 KSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRS 320
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 321 RVEGYMASGVAEGAAVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSG 400
Cdd:PRK09406 315 EVEKQVDDAVAAGATILCGGKRPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 401 AVFTGDLDHGLSIARRIRTGTVELNGSLVGLNA-PLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINGMTVSYPElPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
30-448 |
6.29e-77 |
|
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: 246.80 E-value: 6.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 30 DVDKAVSAARQAFDsgPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTMQSGLPREhIDNFIEVARA 109
Cdd:cd07095 1 QVDAAVAAARAAFP--GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGK-IDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 110 FPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVV 189
Cdd:cd07095 78 RTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 190 NIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIA-ALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSG 268
Cdd:cd07095 158 NLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHrQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 269 QVCSLKTRIIVSKSRE-RELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQgfD 347
Cdd:cd07095 238 QRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV--A 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 348 HGYFVEPTVFSgVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGS 427
Cdd:cd07095 316 GTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRP 394
|
410 420
....*....|....*....|...
gi 2567559872 428 LVGLN--APLGGFKSSGLGRESG 448
Cdd:cd07095 395 TTGASstAPFGGVGLSGNHRPSA 417
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
9-444 |
1.99e-75 |
|
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: 243.87 E-value: 1.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 9 IEVVSPYTEQVLAAVPSATKADVDKAVSAARQAF-DSGPWsrTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPIsl 87
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 88 srtmqsglprehIDNFIEVARAF------------------PFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIK 149
Cdd:cd07148 77 ------------VDAKVEVTRAIdgvelaadelgqlggreiPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 150 LAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGN 229
Cdd:cd07148 145 VAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 230 DIrRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQ 309
Cdd:cd07148 225 GT-RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 310 IGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQgfDHGYfvEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVE 389
Cdd:cd07148 304 VGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLS--DTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2567559872 390 FANDSEYGLSGAVFTGDLDHGLSIARRirtgtveLNGSLVGLN---------APLGGFKSSGLG 444
Cdd:cd07148 380 QANSLPVAFQAAVFTKDLDVALKAVRR-------LDATAVMVNdhtafrvdwMPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
6-464 |
9.67e-73 |
|
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: 238.63 E-value: 9.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 6 NDTIEVVSP-YTEQVLAAVPSATKADVDKAVSAARQAFdsGPWSRTSLEDRIEVLQRLSLAFDKN-ADLLASLVTEQmgc 83
Cdd:cd07125 45 GEGAPVIDPaDHERTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANrGELIALAAAEA--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 84 pislSRTMQSGLP--REHIDnFievARAFPFSAVRQSRNG---------NALVVHePVGVVAAVIPWNAPQLVTIIKLAP 152
Cdd:cd07125 120 ----GKTLADADAevREAID-F---CRYYAAQARELFSDPelpgptgelNGLELH-GRGVFVCISPWNFPLAIFTGQIAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 153 ALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRIA-ALCGND 230
Cdd:cd07125 191 ALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPgDGEEIGEALVAHPRIDGVIFTGSTETAKLINrALAERD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 231 IRRVTL--ELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSlKTRIIVSksrERELLERFDSLIQ----SMPVGDPG 304
Cdd:cd07125 271 GPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCS-ALRLLYL---QEEIAERFIEMLKgamaSLKVGDPW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 305 DTATQIGPMVSARQRSRVEGYMASGVAEGAAVVTgggRPQGFDHGYFVEPTVFSGVTPSmTIaREEIFGPVISVLACESE 384
Cdd:cd07125 347 DLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAP---APLDDGNGYFVAPGIIEIVGIF-DL-TTEVFGPILHVIRFKAE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 385 --DQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELN----GSLVGLNaPLGGFKSSGLGRESG-PEGLAAYTE 457
Cdd:cd07125 422 dlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitGAIVGRQ-PFGGWGLSGTGPKAGgPNYLLRFGN 500
|
....*..
gi 2567559872 458 IKSIGLP 464
Cdd:cd07125 501 EKTVSLN 507
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
12-461 |
6.27e-70 |
|
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: 230.93 E-value: 6.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 12 VSPY-TEQVLAAVPSATKADVDKAVSAARQAFdsGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGcpislsRT 90
Cdd:cd07083 37 VSPFaPSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVG------KN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 91 MQSGLP--REHIDNFIEVARAfpfsAVRQSRNGNALV---------VHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCT 159
Cdd:cd07083 109 WVEAIDdvAEAIDFIRYYARA----ALRLRYPAVEVVpypgednesFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 160 VVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGND------IR 232
Cdd:cd07083 185 VIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVgEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLapgqtwFK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 233 RVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGP 312
Cdd:cd07083 265 RLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 313 MVSARQRSRVEGYMASGVAEGaAVVTGGGRPQGfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESED--QAVEF 390
Cdd:cd07083 345 VIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEG--EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEV 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 391 ANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELN----GSLVGLNaPLGGFKSSGLG-RESGPEGLAAYTEIKSI 461
Cdd:cd07083 422 ANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkitGALVGVQ-PFGGFKLSGTNaKTGGPHYLRRFLEMKAV 496
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
5-455 |
6.70e-70 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 229.79 E-value: 6.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 5 SNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGcp 84
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 85 islsRTMQSGLP--REHID--NFievarafpfsAVRQSRNGNALVVH------------EPVGVVA---------AVIPW 139
Cdd:cd07130 86 ----KILPEGLGevQEMIDicDF----------AVGLSRQLYGLTIPserpghrmmeqwNPLGVVGvitafnfpvAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 140 NApqlvtiiklAPALLAGCTVVLKPAPETPLDSY----LLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTG 215
Cdd:cd07130 152 NA---------AIALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 216 STAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLI 295
Cdd:cd07130 223 STAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 296 QSMPVGDPGDTATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGfdHGYFVEPTVFSGvTPSMTIAREEIFGPV 375
Cdd:cd07130 303 KQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDG--PGNYVEPTIVEG-LSDAPIVKEETFAPI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 376 ISVLACESEDQAVEFANDSEYGLSGAVFTGDL------------DHGlsIArRIRTGTvelNGSLVGlnAPLGGFKSSGL 443
Cdd:cd07130 380 LYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLrnafrwlgpkgsDCG--IV-NVNIGT---SGAEIG--GAFGGEKETGG 451
|
490
....*....|..
gi 2567559872 444 GRESGPEGLAAY 455
Cdd:cd07130 452 GRESGSDAWKQY 463
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
8-447 |
2.63e-68 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 225.99 E-value: 2.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 8 TIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISL 87
Cdd:PRK09457 16 AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 88 SRTmqsglprehidnfiEVA----------RAFpfsAVR--QSRN----GNALVVHEPVGVVAAVIPWNAPQLVTIIKLA 151
Cdd:PRK09457 94 AAT--------------EVTaminkiaisiQAY---HERtgEKRSemadGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 152 PALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRI-AALCGND 230
Cdd:PRK09457 157 PALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLhRQFAGQP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 231 IRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRE-RELLERFDSLIQSMPVGDP-GDTAT 308
Cdd:PRK09457 237 EKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWdAEPQP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 309 QIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGfDHGyFVEPTVFSgVTPSMTIAREEIFGPVISVLACESEDQAV 388
Cdd:PRK09457 317 FMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQA-GTG-LLTPGIID-VTGVAELPDEEYFGPLLQVVRYDDFDEAI 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 389 EFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGLN--APLGGFKSSGLGRES 447
Cdd:PRK09457 394 RLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASsaAPFGGVGASGNHRPS 454
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-465 |
2.87e-66 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 221.17 E-value: 2.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:PLN00412 26 TSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA--WAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GCPI--SLSRTMQSGlprEHIDNFIE------------VARAFPFSavrqSRNGNALVVHEPVGVVAAVIPWNAPQLVTI 147
Cdd:PLN00412 104 AKPAkdAVTEVVRSG---DLISYTAEegvrilgegkflVSDSFPGN----ERNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 148 IKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAaGRRIAAL 226
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMHPGVNCISFTGGDT-GIAISKK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 227 CGndIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDT 306
Cdd:PLN00412 256 AG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 307 AtQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRpqgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQ 386
Cdd:PLN00412 334 C-DITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-----EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 387 AVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLV-GLNA-PLGGFKSSGLGRESGPEGLAAYTEIKS--IG 462
Cdd:PLN00412 408 GIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPArGPDHfPFQGLKDSGIGSQGITNSINMMTKVKStvIN 487
|
...
gi 2567559872 463 LPS 465
Cdd:PLN00412 488 LPK 490
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
34-461 |
5.37e-66 |
|
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: 218.16 E-value: 5.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 34 AVSAARQAFDSGpwsRT-SLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTMQSGLPREHIDNFIE----VAR 108
Cdd:cd07087 3 LVARLRETFLTG---KTrSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKhlkkWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 109 AFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAgLPEGV 188
Cdd:cd07087 80 PRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 189 VNIVPAEREVSEYLVTHPgVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSG 268
Cdd:cd07087 159 VAVVEGGVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 269 QVCSLKTRIIVSKSRERELLERFDSLIQSMpVGDPGDTATQIGPMVSARQRSRVEGYMasgvaEGAAVVTGGGRPQGfdh 348
Cdd:cd07087 238 QTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQVDKE--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 349 GYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSL 428
Cdd:cd07087 309 ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVL 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 2567559872 429 VGL---NAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07087 389 LHAaipNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
39-451 |
1.16e-62 |
|
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: 209.65 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 39 RQAFDSGPWSrtSLEDRIEVLQRLSLAFDKNADLLA--------------SLVTEQMGCPISLSRTmqsglpREHIDNFI 104
Cdd:cd07133 8 KAAFLANPPP--SLEERRDRLDRLKALLLDNQDALAeaisadfghrsrheTLLAEILPSIAGIKHA------RKHLKKWM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 105 EVAR---AFPFsavrqsRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQD 181
Cdd:cd07133 80 KPSRrhvGLLF------LPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 182 AgLPEGVVNIVPAEREVSEYLVTHPgVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRI 261
Cdd:cd07133 154 Y-FDEDEVAVVTGGADVAAAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 262 GSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSM---PVGDPGDTAtqigpMVSARQRSRVEGYMASGVAEGAAVVT 338
Cdd:cd07133 232 GKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPDYTS-----IINERHYARLQGLLEDARAKGARVIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 339 GGGRPQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIR 418
Cdd:cd07133 307 LNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTH 386
|
410 420 430
....*....|....*....|....*....|....*.
gi 2567559872 419 TGTVELNGSLVGL---NAPLGGFKSSGLGRESGPEG 451
Cdd:cd07133 387 SGGVTINDTLLHVaqdDLPFGGVGASGMGAYHGKEG 422
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
47-461 |
5.53e-62 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 207.85 E-value: 5.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 47 WSRTSLEDRIEVLQRLSLAFDKNADLLAS-------------LVTEQMGCPISLSRTMQsglpreHIDNFIEVARAFPFS 113
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAalaadfrkpaaevDLTEILPVLSEINHAIK------HLKKWMKPKRVRTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 114 AVRQSRngnALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAgLPEGVVNIVP 193
Cdd:cd07134 88 LLFGTK---SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 194 AEREVSEYLVTHPgVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSL 273
Cdd:cd07134 164 GDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 274 KTRIIVSKSRERELLERFDSLIQSMPVGDPGDTAT-QIGPMVSARQRSRVEGYMASGVAEGAAVVTGGgrpQGFDHGYFV 352
Cdd:cd07134 243 PDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG---QFDAAQRYI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 353 EPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGL- 431
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFl 399
|
410 420 430
....*....|....*....|....*....|..
gi 2567559872 432 --NAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07134 400 npNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
1-461 |
2.06e-61 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 210.76 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 1 MSSTSNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQ 80
Cdd:PLN02419 123 VESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL--WRNTPITTRQRVMLKFQELIRKNMDKLAMNITTE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 81 MGCPISLSR-TMQSGLprEHIDNFIEVARAFPFSAVRQSRNG-NALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGC 158
Cdd:PLN02419 201 QGKTLKDSHgDIFRGL--EVVEHACGMATLQMGEYLPNVSNGvDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGN 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 159 TVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLEL 238
Cdd:PLN02419 279 TFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNM 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 239 GGKSAAVILDDADLDAAVESLRIGSFRNSGQVC-SLKTRIIV--SKSRERELLERFDSLiqSMPVGDPGDtaTQIGPMVS 315
Cdd:PLN02419 359 GAKNHGLVLPDANIDATLNALLAAGFGAAGQRCmALSTVVFVgdAKSWEDKLVERAKAL--KVTCGSEPD--ADLGPVIS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 316 ARQRSRVEGYMASGVAEGAAVVTGGGR--PQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFAND 393
Cdd:PLN02419 435 KQAKERICRLIQSGVDDGAKLLLDGRDivVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINK 514
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2567559872 394 SEYGLSGAVFTgdldhglSIARRIRTGTVELNGSLVGLNAPL---------GGFKSSGLGRES--GPEGLAAYTEIKSI 461
Cdd:PLN02419 515 NKYGNGAAIFT-------SSGAAARKFQMDIEAGQIGINVPIpvplpffsfTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
29-461 |
6.67e-60 |
|
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: 202.45 E-value: 6.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 29 ADVDKAVSAARQAFDSGpwSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTMQSGLPREHIDNFIEVAR 108
Cdd:cd07135 5 DEIDSIHSRLRATFRSG--KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 109 AF------PFSAVRQSrNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDA 182
Cdd:cd07135 83 KWakdekvKDGPLAFM-FGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 183 gLPEGVVNIVPAEREVSEYLVTHpGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIG 262
Cdd:cd07135 162 -LDPDAFQVVQGGVPETTALLEQ-KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 263 SFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPgDTATQIGPMVSARQRSRVEGYMASgvaEGAAVVTGGGR 342
Cdd:cd07135 240 KFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 343 PQGfdhGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGD---LDHglsIARRIRT 419
Cdd:cd07135 316 DEA---TRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDkseIDH---ILTRTRS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2567559872 420 GTVELNGSL--VGL-NAPLGGFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07135 390 GGVVINDTLihVGVdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
5-442 |
1.95e-57 |
|
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: 198.19 E-value: 1.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 5 SNDTIEVVSPYT-EQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVlqrlslaFDKNADLLASLVTEQMgc 83
Cdd:cd07123 44 TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKE--WARMPFEDRAAI-------FLKAADLLSGKYRYEL-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 84 pisLSRTM--QSGLPRE-HIDNFIEVARAFPFSAV-------RQSRNGNA----LVVHEPV-GVVAAVIPWNAPQLVTII 148
Cdd:cd07123 113 ---NAATMlgQGKNVWQaEIDAACELIDFLRFNVKyaeelyaQQPLSSPAgvwnRLEYRPLeGFVYAVSPFNFTAIGGNL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 149 KLAPALLaGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIAALC 227
Cdd:cd07123 190 AGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDgPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 228 GNDIR------RVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVG 301
Cdd:cd07123 269 GENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 302 DPGDTATQIGPMVSARQRSRVEGYMASGVAEGAAVVTGGGRPQGfDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLAC 381
Cdd:cd07123 349 DPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDD-SVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVY 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 382 ESED--QAVEFAND-SEYGLSGAVFTGDLDHGLSIARRIR--TGTVELN----GSLVGlNAPLGGFKSSG 442
Cdd:cd07123 428 PDSDfeETLELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNFYINdkptGAVVG-QQPFGGARASG 496
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
4-461 |
1.99e-57 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 198.47 E-value: 1.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 4 TSNDTIEVVSPYTEQ-VLAAVPSATKADVDKAVSAARQAfdSGPWSRTSLEDRIEVlqrlslaFDKNADLLASLVTEQMg 82
Cdd:TIGR01236 43 DSNERIPQVNPHNHQaVLAKATNATEEDAMKAVEAALDA--KKDWSNLPFYDRAAI-------FLKAADLLSGPYRYEI- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 83 cpisLSRTM--QSGLPRE-HIDNFIEVARAFPFSA-------VRQSRNGNAL---VVHEPV-GVVAAVIPWNAPQLVTII 148
Cdd:TIGR01236 113 ----LAATMlgQSKTVYQaEIDAVAELIDFFRFNVkyarelyAQQPISAPGEwnrTEYRPLeGFVYAISPFNFTAIAGNL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 149 KLAPALLaGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAER-EVSEYLVTHPGVDKVAFTGSTAAGRRIAALC 227
Cdd:TIGR01236 189 AGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGvQVSDQVLADPDLAGIHFTGSTNTFKHLWKKV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 228 GNDIR------RVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVG 301
Cdd:TIGR01236 268 AQNLDryhnfpRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 302 DPGDTATQIGPMVSARQRSRVEGYM--ASGVAEGAAVVTGGGrpqgFD--HGYFVEPTVFSGVTPSMTIAREEIFGPVIS 377
Cdd:TIGR01236 348 DPDDFRGFMGAVIDEQSFDKIVKYIedAKKDPEALTILYGGK----YDdsQGYFVEPTVVESKDPDHPLMSEEIFGPVLT 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 378 VLACESE--DQAVEFA-NDSEYGLSGAVFTGDLDHGLSIARRIR--TGTVELN----GSLVGlNAPLGGFKSSGLGRESG 448
Cdd:TIGR01236 424 VYVYPDDkyKEILDLVdSTSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINdkctGAVVG-QQPFGGARMSGTNDKAG 502
|
490
....*....|....
gi 2567559872 449 -PEGLAAYTEIKSI 461
Cdd:TIGR01236 503 gPNNLLRWTSPRSI 516
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
3-444 |
1.35e-49 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 182.32 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPY-TEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:PRK11904 558 NGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAELIALCVREA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GcpislsRTMQSGLP--REHIDnF-----IEVARAFpfsAVRQSRNG-----NALVVHePVGVVAAVIPWNAPQLVTIIK 149
Cdd:PRK11904 636 G------KTLQDAIAevREAVD-FcryyaAQARRLF---GAPEKLPGptgesNELRLH-GRGVFVCISPWNFPLAIFLGQ 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 150 LAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIA-ALC 227
Cdd:PRK11904 705 VAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDgATVGAALTADPRIAGVAFTGSTETARIINrTLA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 228 GNDIRRVTL--ELGGKSaAVILDDADL-----DAAVESlrigSFRNSGQVCS-LktRIIVSksrERELLERFDSLIQ-SM 298
Cdd:PRK11904 785 ARDGPIVPLiaETGGQN-AMIVDSTALpeqvvDDVVTS----AFRSAGQRCSaL--RVLFV---QEDIADRVIEMLKgAM 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 299 P---VGDPGDTATQIGPMVSARQRSRVEGYMASGVAEgAAVVTGGGRPQGFDHGYFVEPTVFSgvTPSMTIAREEIFGPV 375
Cdd:PRK11904 855 AelkVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAGTENGHFVAPTAFE--IDSISQLEREVFGPI 931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2567559872 376 ISVLACESE--DQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELN----GSLVGLNaPLGGFKSSGLG 444
Cdd:PRK11904 932 LHVIRYKASdlDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNrnqiGAVVGVQ-PFGGQGLSGTG 1005
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
125-461 |
3.36e-48 |
|
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: 171.53 E-value: 3.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 125 VVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAgLPEGVVNIVPAEREVSEYLVT 204
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 205 HPgVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRE 284
Cdd:cd07136 175 QK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 285 RELLERFDSLIQSMPVGDPGDTATqIGPMVSARQRSRVEGYMasgvaEGAAVVTGGgrpQGFDHGYFVEPTVFSGVTPSM 364
Cdd:cd07136 254 EKFIKELKEEIKKFYGEDPLESPD-YGRIINEKHFDRLAGLL-----DNGKIVFGG---NTDRETLYIEPTILDNVTWDD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 365 TIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGL---NAPLGGFKSS 441
Cdd:cd07136 325 PVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLanpYLPFGGVGNS 404
|
330 340
....*....|....*....|
gi 2567559872 442 GLGRESGPEGLAAYTEIKSI 461
Cdd:cd07136 405 GMGSYHGKYSFDTFSHKKSI 424
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
26-444 |
4.37e-47 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 169.82 E-value: 4.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 26 ATKADVDKAVSAARQAFDSGPwSRtSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTMQSGLPREHIDNFI- 104
Cdd:PTZ00381 4 DNPEIIPPIVKKLKESFLTGK-TR-PLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 105 ---EVARAFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLqD 181
Cdd:PTZ00381 82 hldEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-T 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 182 AGLPEGVVNIVPAEREVSEYLVTHPgVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRI 261
Cdd:PTZ00381 161 KYLDPSYVRVIEGGVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 262 GSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMpVGDPGDTATQIGPMVSARQRSRVEGYMASgvaEGAAVVTGGg 341
Cdd:PTZ00381 240 GKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGG- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 342 rpqGFD-HGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTG 420
Cdd:PTZ00381 315 ---EVDiENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSG 391
|
410 420
....*....|....*....|....*..
gi 2567559872 421 TVELNGSLVGL---NAPLGGFKSSGLG 444
Cdd:PTZ00381 392 AVVINDCVFHLlnpNLPFGGVGNSGMG 418
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
3-444 |
4.25e-44 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 166.27 E-value: 4.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 3 STSNDTIEVVSPY-TEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQM 81
Cdd:COG4230 566 AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELMALLVREA 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 82 GcpislsRTMQSGLP--REHIDnFievARafpFSAVRQSRNGNALVVHEPVGVVAAVIPWNAP------QLvtiiklAPA 153
Cdd:COG4230 644 G------KTLPDAIAevREAVD-F---CR---YYAAQARRLFAAPTVLRGRGVFVCISPWNFPlaiftgQV------AAA 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 154 LLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRIA-ALCGNDI 231
Cdd:COG4230 705 LAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDgETVGAALVADPRIAGVAFTGSTETARLINrTLAARDG 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 232 RRVTL--ELGGK------SAA----VILDdadldaAVESlrigSFRNSGQVCS-LktRII-VSKSRERELLERFDSLIQS 297
Cdd:COG4230 785 PIVPLiaETGGQnamivdSSAlpeqVVDD------VLAS----AFDSAGQRCSaL--RVLcVQEDIADRVLEMLKGAMAE 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 298 MPVGDPGDTATQIGPMVSARQRSRVEGYMASGVAEGaAVVTGGGRPQGFDHGYFVEPTVFSgvTPSMTIAREEIFGPVIS 377
Cdd:COG4230 853 LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVHQLPLPEECANGTFVAPTLIE--IDSISDLEREVFGPVLH 929
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 378 VLACESE--DQAVEFANDSEYGLSGAVFT---GDLDHglsIARRIRTGTVELN----GSLVGLNaPLGGFKSSGLG 444
Cdd:COG4230 930 VVRYKADelDKVIDAINATGYGLTLGVHSridETIDR---VAARARVGNVYVNrniiGAVVGVQ-PFGGEGLSGTG 1001
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
33-473 |
1.70e-42 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 156.23 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 33 KAVSAARQAFDSGpwsRT-SLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTMQSGLPREHIDNFIE------ 105
Cdd:cd07132 2 EAVRRAREAFSSG---KTrPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISnlpewm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 106 ----VARAFPfsavrqsrngNAL----VVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAE 177
Cdd:cd07132 79 kpepVKKNLA----------TLLddvyIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 178 MLqdaglpegvvnivPAEREVSEYLVTHPGV-----------DKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVI 246
Cdd:cd07132 149 LI-------------PKYLDKECYPVVLGGVeettellkqrfDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 247 LDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTAtQIGPMVSARQRSRVEGYM 326
Cdd:cd07132 216 DKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 327 asgvaEGAAVVTGGgrpQGFDHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGD 406
Cdd:cd07132 295 -----SGGKVAIGG---QTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 407 LDHGLSIARRIRTGTVELNGSLVGL---NAPLGGFKSSGLGRESGPEGLAAYTEIKSIGLPSVLAEKLIS 473
Cdd:cd07132 367 KKVINKILSNTSSGGVCVNDTIMHYtldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNS 436
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
8-455 |
8.07e-42 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 155.76 E-value: 8.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 8 TIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGcpisl 87
Cdd:PLN02315 35 LVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMG----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 88 sRTMQSGLP--REHID--NF-IEVARAFPFSAVRQSRNGNALV-VHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVV 161
Cdd:PLN02315 108 -KILAEGIGevQEIIDmcDFaVGLSRQLNGSIIPSERPNHMMMeVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 162 LKPAPETPLDSY----LLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLE 237
Cdd:PLN02315 187 WKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 238 LGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSAR 317
Cdd:PLN02315 267 LSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 318 QRSRVEGYMASGVAEGAAVVTGGGRPQGfdHGYFVEPTVFSgVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYG 397
Cdd:PLN02315 347 SKKNFEKGIEIIKSQGGKILTGGSAIES--EGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQG 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 398 LSGAVFTGDLD--------HGLSIArrIRTGTVELNGSLVGlnAPLGGFKSSGLGRESGPEGLAAY 455
Cdd:PLN02315 424 LSSSIFTRNPEtifkwigpLGSDCG--IVNVNIPTNGAEIG--GAFGGEKATGGGREAGSDSWKQY 485
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
2-444 |
7.94e-41 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 156.56 E-value: 7.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 2 SSTSNDTIEVVSPY-TEQVLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQ 80
Cdd:PRK11905 562 GDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPELFALAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 81 MGcpislsRTMQSGLP--REHIDnFIEvarafpFSAVrQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGC 158
Cdd:PRK11905 640 AG------KTLANAIAevREAVD-FLR------YYAA-QARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGN 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 159 TVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAE-REVSEYLVTHPGVDKVAFTGSTAAGRRI----AALCGNDIRR 233
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDgRTVGAALVADPRIAGVMFTGSTEVARLIqrtlAKRSGPPVPL 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 234 VTlELGGKSaAVILDDADL-----DAAVESlrigSFRNSGQVCS-LktRII-VSKSRERELLERFDSLIQSMPVGDPGDT 306
Cdd:PRK11905 786 IA-ETGGQN-AMIVDSSALpeqvvADVIAS----AFDSAGQRCSaL--RVLcLQEDVADRVLTMLKGAMDELRIGDPWRL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 307 ATQIGPMVSARQRSRVEGYMASGVAEGaAVVTGGGRPQGFDHGYFVEPTVFSgvTPSMTIAREEIFGPVISVLACESE-- 384
Cdd:PRK11905 858 STDVGPVIDAEAQANIEAHIEAMRAAG-RLVHQLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADel 934
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2567559872 385 DQAVEFANDSEYGLSGAVFT---GDLDHglsIARRIRTGTVELN----GSLVGLNaPLGGFKSSGLG 444
Cdd:PRK11905 935 DRVIDDINATGYGLTFGLHSridETIAH---VTSRIRAGNIYVNrniiGAVVGVQ-PFGGEGLSGTG 997
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
11-459 |
3.36e-40 |
|
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: 151.22 E-value: 3.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 11 VVSPYTEQ-VLAAVPSATKADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLslafdknADLLASLVTEQMG-CPISLS 88
Cdd:TIGR01238 55 VTNPADRRdIVGQVFHANLAHVQAAIDSAQQAFPT--WNATPAKERAAKLDRL-------ADLLELHMPELMAlCVREAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 89 RTMQSGLP--REHIDnfievaraFPFSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAP 166
Cdd:TIGR01238 126 KTIHNAIAevREAVD--------FCRYYAKQVRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 167 ETPLDSYLLAEMLQDAGLPEGVVNIVP-AEREVSEYLVTHPGVDKVAFTGSTAAGRRI-AALCGNDIRRVTL--ELGGKS 242
Cdd:TIGR01238 198 QTSLIAYRAVELMQEAGFPAGTIQLLPgRGADVGAALTSDPRIAGVAFTGSTEVAQLInQTLAQREDAPVPLiaETGGQN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 243 AAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRV 322
Cdd:TIGR01238 278 AMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 323 EGYM--ASGVAEGAAVVTGGGRPQgFDHGYFVEPTVFSgvTPSMTIAREEIFGPVISVLACESE--DQAVEFANDSEYGL 398
Cdd:TIGR01238 358 LAHIehMSQTQKKIAQLTLDDSRA-CQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKARelDQIVDQINQTGYGL 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2567559872 399 SGAVFTGDLDHGLSIARRIRTGTVELN----GSLVGLNaPLGGFKSSGLG-RESGPEGLAAYTEIK 459
Cdd:TIGR01238 435 TMGVHSRIETTYRWIEKHARVGNCYVNrnqvGAVVGVQ-PFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
122-461 |
6.35e-36 |
|
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: 137.93 E-value: 6.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 122 NALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQdAGLPEGVVNIVPAEREVSEY 201
Cdd:cd07137 94 KAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIP-EYLDTKAIKVIEGGVPETTA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 202 LVTHPGvDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSF-RNSGQVCSLKTRIIVS 280
Cdd:cd07137 173 LLEQKW-DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 281 KSRERELLERFDSLIQSMPVGDPGDTAtQIGPMVSARQRSRVEGYMA-SGVAegAAVVTGGGRPqgfDHGYFVEPTVFSG 359
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDdPSVA--DKIVHGGERD---EKNLYIEPTILLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 360 VTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLVGLNA---PLG 436
Cdd:cd07137 326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIdtlPFG 405
|
330 340
....*....|....*....|....*
gi 2567559872 437 GFKSSGLGRESGPEGLAAYTEIKSI 461
Cdd:cd07137 406 GVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
23-448 |
5.19e-33 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 133.18 E-value: 5.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 23 VPSATKADVDKAVSAARQAfdsGP-WSRTSLEDRIEVLQRLslafdknadllASLVTEQMGCPISLsrtmqsgLPRE--- 98
Cdd:PRK11809 676 VREATPAEVEQALESAVNA---APiWFATPPAERAAILERA-----------ADLMEAQMQTLMGL-------LVREagk 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 99 HIDNFI-EVARAFPFsaVR----QSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSY 173
Cdd:PRK11809 735 TFSNAIaEVREAVDF--LRyyagQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 174 LLAEMLQDAGLPEGVVNIVPAERE-VSEYLVTHPGVDKVAFTGSTAAG----RRIAALCGNDIRRVTL--ELGGKSaAVI 246
Cdd:PRK11809 813 QAVRILLEAGVPAGVVQLLPGRGEtVGAALVADARVRGVMFTGSTEVArllqRNLAGRLDPQGRPIPLiaETGGQN-AMI 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 247 LDDADLDAAVESLRIGS-FRNSGQVCS-LKTRIIVSKSREReLLERFDSLIQSMPVGDPGDTATQIGPMVSARQRSRVEG 324
Cdd:PRK11809 892 VDSSALTEQVVADVLASaFDSAGQRCSaLRVLCLQDDVADR-TLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIER 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 325 YMASGVAEGAAVV-TGGGRPQGFDHGYFVEPTVFSgvTPSMTIAREEIFGPVISVLACESE--DQAVEFANDSEYGLSGA 401
Cdd:PRK11809 971 HIQAMRAKGRPVFqAARENSEDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVRYNRNqlDELIEQINASGYGLTLG 1048
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2567559872 402 VFTgDLDHglSIAR---RIRTGTVELN----GSLVGLNaPLGGFKSSGLGRESG 448
Cdd:PRK11809 1049 VHT-RIDE--TIAQvtgSAHVGNLYVNrnmvGAVVGVQ-PFGGEGLSGTGPKAG 1098
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
121-469 |
1.10e-28 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 118.29 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 121 GNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQdAGLPEGVVNIVPAEREVSE 200
Cdd:PLN02203 100 ATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEGGPAVGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 201 YLVTHPGvDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAVI--LDDA-DLDAAVESLRIGSFRN-SGQVCSLKTR 276
Cdd:PLN02203 179 QLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 277 IIVSKSRERELLERFDSLIQSMPVGDPGDTATqIGPMVSARQRSRVEGYMA-SGVAegAAVVTGGgrpqGFD-HGYFVEP 354
Cdd:PLN02203 258 VLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKdPRVA--ASIVHGG----SIDeKKLFIEP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 355 TVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHGLSIARRIRTGTVELNGSLV--GLN 432
Cdd:PLN02203 331 TILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIqyACD 410
|
330 340 350
....*....|....*....|....*....|....*...
gi 2567559872 433 A-PLGGFKSSGLGRESGPEGLAAYTEIKSIGLPSVLAE 469
Cdd:PLN02203 411 SlPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE 448
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
149-452 |
5.88e-27 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 113.52 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 149 KLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAG-LPEGVVNIVPAEreVSEYLVTHPGVDKVAFTGSTAAGRRI---A 224
Cdd:cd07128 164 KFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS--VGDLLDHLGEQDVVAFTGSAATAAKLrahP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 225 ALCGNDIRrVTLELGGKSAAVILDDADLDAAVESLRIGSFRN-----SGQVCSLKTRIIVSKSRERELLERFDSLIQSMP 299
Cdd:cd07128 242 NIVARSIR-FNAEADSLNAAILGPDATPGTPEFDLFVKEVARemtvkAGQKCTAIRRAFVPEARVDAVIEALKARLAKVV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 300 VGDPGDTATQIGPMVSARQRSRVEGYMASgVAEGAAVVTGGG---RPQGFDH--GYFVEPTVFSGVTPSMTIAREEI--F 372
Cdd:cd07128 321 VGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPdrfEVVGADAekGAFFPPTLLLCDDPDAATAVHDVeaF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 373 GPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDHglsiARRIRTGTVELNGSLVGLNA-----------PLGGFKSS 441
Cdd:cd07128 400 GPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAF----ARELVLGAAPYHGRLLVLNRdsakestghgsPLPQLVHG 475
|
330
....*....|.
gi 2567559872 442 GLGRESGPEGL 452
Cdd:cd07128 476 GPGRAGGGEEL 486
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
20-472 |
8.24e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 109.75 E-value: 8.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 20 LAAVPSATKADVDKAVSAARQAFDSGpwSRTSLEDRIEVLQRLSLAFDKN-----ADLLASLVTEQMGC---PISLSRTm 91
Cdd:PLN02174 1 MAAKKMFGAADASILVTELRRSFDDG--VTRGYEWRVTQLKKLMIICDNHepeivAALRDDLGKPELESsvyEVSLLRN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 92 QSGLPREHIDNFIEVARA------FPFSAVrqsrngnalVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPA 165
Cdd:PLN02174 78 SIKLALKQLKNWMAPEKAktslttFPASAE---------IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 166 PETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLvtHPGVDKVAFTGSTAAGRRIAALCGNDIRRVTLELGGKSAAV 245
Cdd:PLN02174 149 ELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 246 ILDDADLDAAVESLRIGSFR-NSGQVCSLKTRIIVSKSRERELLERFDSLIQSMPVGDPGDTaTQIGPMVSARQRSRVEG 324
Cdd:PLN02174 227 VDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMES-KDMSRIVNSTHFDRLSK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 325 YMASGVAEGaAVVTGGGRPQgfdHGYFVEPTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGLSGAVFT 404
Cdd:PLN02174 306 LLDEKEVSD-KIVYGGEKDR---ENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFT 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2567559872 405 GDLDHGLSIARRIRTGTVELNGSLVGL---NAPLGGFKSSGLGRESGPEGLAAYTEIKSIGLPSVLAEKLI 472
Cdd:PLN02174 382 HNKKLKERFAATVSAGGIVVNDIAVHLalhTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSAV 452
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
129-455 |
9.25e-25 |
|
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: 106.17 E-value: 9.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 129 PVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAG-LPEGVVNIVPAEREVSEYLVTHPG 207
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTMQALLLHPN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 208 VDKVAFTGSTAAGRRIAALCGNDirRVTLELGGKSAAVILDDAD-----LDAAVESLRIGsfrnSGQVCSLKTRIIVSKS 282
Cdd:cd07084 180 PKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQavdyvAWQCVQDMTAC----SGQKCTAQSMLFVPEN 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 283 RE-RELLERFDSLIQSMPVGDpgdtatqigPMVSARQRSRVEGYMASGVAEGAAVVTGGGR-PQGFDHGYFVEPTVFSGV 360
Cdd:cd07084 254 WSkTPLVEKLKALLARRKLED---------LLLGPVQTFTTLAMIAHMENLLGSVLLFSGKeLKNHSIPSIYGACVASAL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 361 -TPSMTIAR------EEIFGPVISVLACEsEDQAVEFANDSEYG---LSGAVFTGDLDH-GLSIARRIRTGTVELNGSLV 429
Cdd:cd07084 325 fVPIDEILKtyelvtEEIFGPFAIVVEYK-KDQLALVLELLERMhgsLTAAIYSNDPIFlQELIGNLWVAGRTYAILRGR 403
|
330 340 350
....*....|....*....|....*....|.
gi 2567559872 430 GLNAPL----GGFKSSGLGRESG-PEGLAAY 455
Cdd:cd07084 404 TGVAPNqnhgGGPAADPRGAGIGgPEAIKLV 434
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
31-426 |
4.43e-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: 95.30 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 31 VDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPIS-----LSRT-----MQSGLPREH- 99
Cdd:cd07129 1 VDAAAAAAAAAFES--YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEArlqgeLGRTtgqlrLFADLVREGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 100 -----IDNFIEVARAFPFSAVRQsrngnalvVHEPVGVVAAVIPWNAPqlvtiikLA---------PALLAGCTVVLKPA 165
Cdd:cd07129 79 wldarIDPADPDRQPLPRPDLRR--------MLVPLGPVAVFGASNFP-------LAfsvaggdtaSALAAGCPVVVKAH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 166 PETPLDSYLLAEMLQDA----GLPEGVVN-IVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRIAALCgnDIRR----VTL 236
Cdd:cd07129 144 PAHPGTSELVARAIRAAlratGLPAGVFSlLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA--AARPepipFYA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 237 ELGGKSAAVILDDAdLDAAVESLR---IGSFR-NSGQVCSLKTRIIVSKSrerELLERFDSLIQSMPVGDPGdtatqiGP 312
Cdd:cd07129 222 ELGSVNPVFILPGA-LAERGEAIAqgfVGSLTlGAGQFCTNPGLVLVPAG---PAGDAFIAALAEALAAAPA------QT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 313 MVSARQRsrvEGYmASGVAE-----GAAVVTGGGRPQGfdhGYFVEPTVFSgVTPSMTIA----REEIFGPVISVLACES 383
Cdd:cd07129 292 MLTPGIA---EAY-RQGVEAlaaapGVRVLAGGAAAEG---GNQAAPTLFK-VDAAAFLAdpalQEEVFGPASLVVRYDD 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2567559872 384 EDQAVEFANDSEYGLSGAVF--TGDLDHGLSIARRI--RTGTVELNG 426
Cdd:cd07129 364 AAELLAVAEALEGQLTATIHgeEDDLALARELLPVLerKAGRLLFNG 410
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
149-409 |
5.06e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 95.54 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 149 KLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAG-LPEGVVNIVPAErevSEYLVTH-PGVDKVAFTGSTAAGRRIAAL 226
Cdd:PRK11903 168 KAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGS---SAGLLDHlQPFDVVSFTGSAETAAVLRSH 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 227 cGNDIR---RVTLELGGKSAAVILDDADLDAAVESLRIGSF-----RNSGQVCSLKTRIIVSKSRERELLERFDSLIQSM 298
Cdd:PRK11903 245 -PAVVQrsvRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVvremtVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKT 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 299 PVGDPGDTATQIGPMVSARQRSRVEGYMAsGVAEGAAVVTGGGRPQGFDH----GYFVEPTVF--SGVTPSMTIAREEIF 372
Cdd:PRK11903 324 TVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDAdpavAACVGPTLLgaSDPDAATAVHDVEVF 402
|
250 260 270
....*....|....*....|....*....|....*..
gi 2567559872 373 GPVISVLACESEDQAVEFANDSEYGLSGAVFTGDLDH 409
Cdd:PRK11903 403 GPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAF 439
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
120-291 |
7.56e-13 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 69.94 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 120 NGNALVVHEPVGVVAAVIPWNAPQLVtIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDA---GLPEGVVNIVP-AE 195
Cdd:cd07077 91 NGETYVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPhPS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 196 REVSEYLVTHPGVDKVAFTGSTAAGRriAALCGNDIRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNsGQVCSLKT 275
Cdd:cd07077 170 DELAEELLSHPKIDLIVATGGRDAVD--AAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQ 246
|
170
....*....|....*.
gi 2567559872 276 RIIVSKSRERELLERF 291
Cdd:cd07077 247 NLYVVDDVLDPLYEEF 262
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
12-406 |
8.52e-13 |
|
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: 70.20 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 12 VSPYTEQVLAAVPsatKADVDKAVSAARQAFDSgpWSRTSLEDRI----EVLQRLSlafdKNADLLASLVTEQMGcpISL 87
Cdd:cd07127 70 VSPYGVELGVTYP---QCDPDALLAAARAAMPG--WRDAGARARAgvclEILQRLN----ARSFEMAHAVMHTTG--QAF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 88 SRTMQSGLPREHiDNFIEvarAFPFSAVRQSRNGNALVVHEPVGV----------------VAAVI------PWNA-PQL 144
Cdd:cd07127 139 MMAFQAGGPHAQ-DRGLE---AVAYAWREMSRIPPTAEWEKPQGKhdplamektftvvprgVALVIgcstfpTWNGyPGL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 145 VTiiklapALLAGCTVVLKPAPETPLDSYLLA----EMLQDAGLPEGVVNIV--PAEREVSEYLVTHPGVDKVAFTGSTA 218
Cdd:cd07127 215 FA------SLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFDPNLVTLAadTPEEPIAQTLATRPEVRIIDFTGSNA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 219 AGRRIAALCGNdiRRVTLELGGKSAAVILDDADLDAAVESLRIGSFRNSGQVCSLKTRIIVSKS--RERELLERFDSLIQ 296
Cdd:cd07127 289 FGDWLEANARQ--AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiQTDDGRKSFDEVAA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 297 SMP------VGDPGDTATQIGPMVSARQRSRVEGymASGVAEGAAVVTGGGRPQgFDHGYFVEPTVFSGVTPSMTIAREE 370
Cdd:cd07127 367 DLAaaidglLADPARAAALLGAIQSPDTLARIAE--ARQLGEVLLASEAVAHPE-FPDARVRTPLLLKLDASDEAAYAEE 443
|
410 420 430
....*....|....*....|....*....|....*....
gi 2567559872 371 IFGPVISVLACESEDQAVEFANDS--EYG-LSGAVFTGD 406
Cdd:cd07127 444 RFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTD 482
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
128-291 |
6.17e-12 |
|
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: 67.13 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 128 EPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDA----GLPEGVVNIVP-AEREVSEYL 202
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEePSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 203 VTHPGVDKVAFTGSTAAGRRiAALCGNDIrrvtleLG---GKSAAVILDDADLDAAVESLRIG-SFRNsGQVCSLKTRII 278
Cdd:cd07122 174 MKHPDVDLILATGGPGMVKA-AYSSGKPA------IGvgpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVI 245
|
170
....*....|...
gi 2567559872 279 VSKSRERELLERF 291
Cdd:cd07122 246 VDDEIYDEVRAEL 258
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
31-291 |
9.25e-12 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 66.91 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 31 VDKAVSAARQAfdSGPWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGCPISLSRTMQSGLPREHIDNfIEVARAF 110
Cdd:cd07081 1 LDDAVAAAKVA--QQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYN-VYKDEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 111 PfSAVRQSRNGNALVVHEPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDA----GLPE 186
Cdd:cd07081 78 C-GVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 187 G-VVNIVPAEREVSEYLVTHPGVDKVAFTGSTA--------AGRRIAALCGNdirrvtlelggkSAAVILDDADLDAAVE 257
Cdd:cd07081 157 NlIGWIDNPSIELAQRLMKFPGIGLLLATGGPAvvkaayssGKPAIGVGAGN------------TPVVIDETADIKRAVQ 224
|
250 260 270
....*....|....*....|....*....|....
gi 2567559872 258 SLRIGSFRNSGQVCSLKTRIIVSKSRERELLERF 291
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLF 258
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| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
29-431 |
8.31e-09 |
|
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: 57.63 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 29 ADVDKAVSAARQAFDSgpWSRTSLEDRIEVLQRLSLAFDKNADLLASLVTEQMGcpislsrtMqsGLPREHIDNFIEVAR 108
Cdd:cd07121 4 ATVDDAVAAAKAAQKQ--YRKCTLADREKIIEAIREALLSNAEELAEMAVEETG--------M--GRVEDKIAKNHLAAE 71
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 109 AFP-----FSAVRQSRNGNALVVHEPVGVVAAVIPWNAPqLVTIIKLAPALLA-GCTVVLKPAPETPLDSYLLAEMLQDA 182
Cdd:cd07121 72 KTPgtedlTTTAWSGDNGLTLVEYAPFGVIGAITPSTNP-TETIINNSISMLAaGNAVVFNPHPGAKKVSAYAVELINKA 150
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 183 -----GLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTA-------AGRR-IAALCGNdirrvtlelggksAAVILDD 249
Cdd:cd07121 151 iaeagGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAvvkaalsSGKKaIGAGAGN-------------PPVVVDE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 250 -ADLDAAVESLRIG-SFRNSgQVCSLKTRIIVSKSRERELLERFDS----LIQSMPVGDPGDTATQIGPMVSArQRSRVe 323
Cdd:cd07121 218 tADIEKAARDIVQGaSFDNN-LPCIAEKEVIAVDSVADYLIAAMQRngayVLNDEQAEQLLEVVLLTNKGATP-NKKWV- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 324 GYMASGVAEGAAVVTGGGRpqgfdhgyfvePTVFSGVTPSMTIAREEIFGPVISVLACESEDQAVEFANDSEYGL--SGA 401
Cdd:cd07121 295 GKDASKILKAAGIEVPADI-----------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAI 363
|
410 420 430
....*....|....*....|....*....|.
gi 2567559872 402 VFTGDLDHGLSIARRIRTGTVELNG-SLVGL 431
Cdd:cd07121 364 IHSKNVENLTKMARAMQTTIFVKNGpSYAGL 394
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| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
128-425 |
2.75e-08 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 56.35 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 128 EPVGVVAAVIPWNAPQLVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDA----GLPEGVVNIVPAE-REVSEYL 202
Cdd:PRK13805 107 EPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAavaaGAPKDIIQWIEEPsVELTNAL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 203 VTHPGVDKVAFTGSTAAGRriAAL-CGNDirrvtlELG---GKSAAVILDDADLDAAVESLrIGS--FRNsGQVCSLKTR 276
Cdd:PRK13805 187 MNHPGIALILATGGPGMVK--AAYsSGKP------ALGvgaGNVPAYIDKTADIKRAVNDI-LLSktFDN-GMICASEQA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 277 IIVSKSRERELLERFdsliqsmpvgdpgdtATQIGPMVSARQRSRVEGYM--ASGVAEGAAVVtggGRP-------QGFD 347
Cdd:PRK13805 257 VIVDDEIYDEVKEEF---------------ASHGAYFLNKKELKKLEKFIfgKENGALNADIV---GQSaykiaemAGFK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 348 hgyfVEPTV------FSGVTPSMTIAREEIFgPVISVLACESEDQAVEFA----NDSEYGLSGAVFTGDLDHGLSIARRI 417
Cdd:PRK13805 319 ----VPEDTkiliaeVKGVGESEPLSHEKLS-PVLAMYKAKDFEDAVEKAeklvEFGGLGHTAVIYTNDDELIKEFGLRM 393
|
....*...
gi 2567559872 418 RTGTVELN 425
Cdd:PRK13805 394 KACRILVN 401
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| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
5-406 |
6.67e-05 |
|
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: 45.18 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 5 SNDTIEVVSPYTEQVLAAVPSATKADVDKAVSAARQAFDSGpwsrtsLEDRIEVLQRLSLAFDknadlLASLVTEQMGCP 84
Cdd:cd07126 10 ASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSG------LHNPLKNPERYLLYGD-----VSHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 85 IS---LSRTMQSGLPREHIDNFIEV------------------ARAFPFSAVRQSRNGNALvvHEPVGVVAAVIPWNAPQ 143
Cdd:cd07126 79 EVedfFARLIQRVAPKSDAQALGEVvvtrkflenfagdqvrflARSFNVPGDHQGQQSSGY--RWPYGPVAIITPFNFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 144 LVTIIKLAPALLAGCTVVLKPAPETPLDSYLLAEMLQDAGLPEGVVNIVPAEREVSEYLVTHPGVDKVAFTGSTAAGRRI 223
Cdd:cd07126 157 EIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 224 AalcgndirrvtLELGGKsaaVILDDADLDAAVESLRIG------------SFRNSGQVCSLKTRIIVSKS-RERELLER 290
Cdd:cd07126 237 A-----------LELHGK---VKLEDAGFDWKILGPDVSdvdyvawqcdqdAYACSGQKCSAQSILFAHENwVQAGILDK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567559872 291 FDSLIQSMPVGDpgdtaTQIGPMVSARQRsRVEGYMASGVAEGAAVVTGGGRPQGfDHGY-----FVEPT-VFsgvTPSM 364
Cdd:cd07126 303 LKALAEQRKLED-----LTIGPVLTWTTE-RILDHVDKLLAIPGAKVLFGGKPLT-NHSIpsiygAYEPTaVF---VPLE 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2567559872 365 TIARE--------EIFGP--VISVLACESEDQAVEFANDSEYGLSGAVFTGD 406
Cdd:cd07126 373 EIAIEenfelvttEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSND 424
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