|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
32-492 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 791.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 32 GETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPI 111
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 112 ANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPA 191
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 192 EQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSNIKRIGLELGGKSP 271
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 272 QVVLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRV 351
Cdd:cd07112 241 NIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 352 LGYIDAGRADGARPVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAV 431
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77389950 432 WTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVW 492
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTW 461
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
21-495 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 592.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:COG1012 9 FIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPA--WAATPPAERAAILLRAADLLEERREELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYnGDVVSAAACIAWYAEAIDKVYGEVAATAY-DMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPA 179
Cdd:COG1012 87 ALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDApGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 180 LATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNI 259
Cdd:COG1012 166 LAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE-NL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 260 KRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRM 339
Cdd:COG1012 245 KRVTLELGGKNPAIV-LDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 340 GSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMAT 419
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGE-GGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77389950 420 ANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNC-FDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWFAH 495
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDgTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
17-491 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 569.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 17 PNRPFIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILANR 96
Cdd:cd07091 3 PTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 97 EELALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKL 176
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 177 GPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQ 256
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 257 SNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTA 336
Cdd:cd07091 243 SNLKKVTLELGGKSPNIV-FDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 337 TRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEA 416
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSK--GYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77389950 417 MATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
26-491 |
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: 557.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 26 YVDSlSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETL 105
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 106 NVGKPIANAYnGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNS 185
Cdd:pfam00171 78 ENGKPLAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 186 VILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLE 265
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 266 LGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSE 345
Cdd:pfam00171 236 LGGKNPLIV-LEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 346 EQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVY 425
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDN--GYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77389950 426 GLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSL-AVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-494 |
0e+00 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 541.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 7 WHARAKAVALPNRPFIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILL 86
Cdd:PRK09847 9 WQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 87 RFSELILANREELALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWN 166
Cdd:PRK09847 89 KLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 167 YPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEV 246
Cdd:PRK09847 169 FPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 247 GKYFMQYSGQSNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKV 326
Cdd:PRK09847 249 GKQLLKDAGDSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 327 FAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGArpVIGGGRVKTETGgfYIEPTIFEGVRNDMKIAQEEIFGPVLS 406
Cdd:PRK09847 329 WQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQ--LLLDGRNAGLAA--AIGPTIFVDVDPNASLSREEIFGPVLV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 407 AIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYT 486
Cdd:PRK09847 405 VTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFT 484
|
....*...
gi 77389950 487 DLKAVWFA 494
Cdd:PRK09847 485 ELKTIWIS 492
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
40-494 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 528.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNGDV 119
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTAL 199
Cdd:cd07115 82 PRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 200 KFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSgQSNIKRIGLELGGKSPQVVlADCD 279
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGA-AGNLKRVSLELGGKSANIV-FADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 280 DLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGR 359
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 360 ADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNA 439
Cdd:cd07115 320 EEGARLLTGGKRPGAR--GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 77389950 440 HRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWFA 494
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
21-491 |
4.03e-179 |
|
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: 511.12 E-value: 4.03e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAG-VWSRMAPADRRRILLRFSELILANREEL 99
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 100 ALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPA 179
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 180 LATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSNI 259
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 260 KRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRM 339
Cdd:cd07141 250 KRVTLELGGKSPNIV-FADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 340 GSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMAT 419
Cdd:cd07141 329 GPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDK--GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77389950 420 ANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
21-492 |
2.08e-177 |
|
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: 506.85 E-value: 2.08e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYnGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:cd07119 81 RLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQySGQSNIK 260
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMR-AAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 261 RIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMG 340
Cdd:cd07119 239 KVALELGGKNPNIV-FADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 341 SMVSEEQMDRVLGYIDAGRADGARPVIGGGRvKTETG---GFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAM 417
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKR-PTGDElakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77389950 418 ATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVW 492
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
38-493 |
2.65e-174 |
|
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: 497.84 E-value: 2.65e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIAnAYNG 117
Cdd:cd07114 2 INPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIR-ETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYAEAIDKVYGEVAATAY-DMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPF 196
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 197 TALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLA 276
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 277 DCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYID 356
Cdd:cd07114 240 DADLDAAVNGVVAGIFA-AAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 357 AGRADGARPVIGGGRVKTE--TGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTG 434
Cdd:cd07114 319 RAREEGARVLTGGERPSGAdlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 77389950 435 SVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWF 493
Cdd:cd07114 399 DLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
38-491 |
5.98e-173 |
|
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: 494.39 E-value: 5.98e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNG 117
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFT 197
Cdd:cd07093 80 DIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 198 ALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGqSNIKRIGLELGGKSPQVVlAD 277
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPNIV-FA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 278 CDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDA 357
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 358 GRADGARPVIGGGRVKT--ETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGS 435
Cdd:cd07093 318 ARAEGATILTGGGRPELpdLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 436 VKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
16-491 |
3.79e-172 |
|
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: 493.16 E-value: 3.79e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 16 LPNRPFIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILAN 95
Cdd:cd07142 2 KHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 96 REELALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWK 175
Cdd:cd07142 82 ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 176 LGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSG 255
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 256 QSNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDT 335
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIV-CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 336 ATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDE 415
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSK--GYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 416 AMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
58-493 |
1.30e-169 |
|
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: 485.17 E-value: 1.30e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 58 DVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYnGDVVSAAACIAWYAEAIDKVY 137
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 138 GEVAATAY-DMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLN 216
Cdd:cd07078 78 GEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 217 VVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANT 296
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIV-FDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 297 GQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEt 376
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGG- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 377 GGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCF 456
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 77389950 457 DRG-SLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWF 493
Cdd:cd07078 395 SVGaEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-491 |
3.28e-167 |
|
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: 479.81 E-value: 3.28e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAGvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNgDV 119
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA-DV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTAL 199
Cdd:cd07109 82 EAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 200 KFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVlADCD 279
Cdd:cd07109 162 RLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIV-FADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 280 DLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATrMGSMVSEEQMDRVLGYIDAGR 359
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 360 ADGARPVIGGGRVKTET-GGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKN 438
Cdd:cd07109 319 ARGARIVAGGRIAEGAPaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 77389950 439 AHRAAKSLRAGVVWVNC-FDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07109 399 ALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
21-489 |
4.96e-165 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 475.30 E-value: 4.96e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELaIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIK 260
Cdd:cd07559 162 AAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 261 RIGLELGGKSPQV----VLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTA 336
Cdd:cd07559 240 PVTLELGGKSPNIffddAMDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 337 TRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTE--TGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFD 414
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGglDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77389950 415 EAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLK 489
Cdd:cd07559 400 EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
21-491 |
1.10e-164 |
|
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: 474.59 E-value: 1.10e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEaGVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE-SWWSKVTGEERGELLDKLADLVEKNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:cd07144 90 AIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIK 260
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ-NLK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 261 RIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAK-VFAPGDPLDTATRM 339
Cdd:cd07144 249 AVTLECGGKSPALV-FEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 340 GSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETG-GFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMA 418
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77389950 419 TANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
21-491 |
3.63e-163 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 471.23 E-value: 3.63e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSNIK 260
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 261 RIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMG 340
Cdd:PLN02766 264 QVSLELGGKSPLLI-FDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 341 SMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATA 420
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDK--GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77389950 421 NDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:PLN02766 421 NNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
21-491 |
2.57e-160 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 462.81 E-value: 2.57e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKV-YGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPA 179
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 180 LATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGlGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNI 259
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE-RL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 260 KRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRM 339
Cdd:cd07139 240 ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLM-NNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 340 GSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMAT 419
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77389950 420 ANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFdRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-491 |
4.23e-159 |
|
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: 460.07 E-value: 4.23e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 12 KAVALPNRPFIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSEL 91
Cdd:cd07143 1 GKYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 92 ILANREELALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSM 171
Cdd:cd07143 81 MERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 172 AAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFM 251
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 252 QYSGQSNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGD 331
Cdd:cd07143 241 EAAAKSNLKKVTLELGGKSPNIV-FDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 332 PLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVK 411
Cdd:cd07143 320 PFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNE--GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 412 GFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07143 398 TEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
21-491 |
1.17e-158 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 461.20 E-value: 1.17e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:PLN02466 61 LINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:PLN02466 141 ALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPAL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSNIK 260
Cdd:PLN02466 221 ACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 261 RIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMG 340
Cdd:PLN02466 301 PVTLELGGKSPFIV-CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 341 SMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATA 420
Cdd:PLN02466 380 PQIDSEQFEKILRYIKSGVESGATLECGGDRFGSK--GYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRA 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77389950 421 NDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:PLN02466 458 NNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
40-491 |
1.47e-158 |
|
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: 457.95 E-value: 1.47e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNGDV 119
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEVAAT-AYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTA 198
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 199 LKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADC 278
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 279 DDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAG 358
Cdd:cd07118 242 DLDAAADAVVFGVYF-NAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 359 RADGARPVIGGGRVKTETGgFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKN 438
Cdd:cd07118 321 RAEGATLLLGGERLASAAG-LFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 77389950 439 AHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
21-491 |
1.09e-153 |
|
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: 445.79 E-value: 1.09e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07138 2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDkvygevaatAYDMT-----TLVMREPLGIVAAVVPWNYPMSMAAWK 175
Cdd:cd07138 80 QAITLEMGAPITLARAAQVGLGIGHLRAAADALK---------DFEFEerrgnSLVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 176 LGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSG 255
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 256 QSnIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDT 335
Cdd:cd07138 231 DT-VKRVALELGGKSANII-LDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 336 ATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGG-GRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFD 414
Cdd:cd07138 309 ATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77389950 415 EAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNcFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
38-491 |
8.39e-152 |
|
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: 440.59 E-value: 8.39e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNG 117
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-RV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYAEAIDKVYGE---VAATAYDMTTlvmREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQS 194
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSGEhvpLPGGSFAYTR---REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 195 PFTALKFGELAIEAGMPPGVLNVVPGLGHiAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGqSNIKRIGLELGGKSPQVV 274
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 275 LADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGY 354
Cdd:cd07090 234 FDDADLENAVNGAMMANFL-SQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 355 IDAGRADGARPVIGGGRVKTE---TGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAV 431
Cdd:cd07090 313 IESAKQEGAKVLCGGERVVPEdglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 432 WTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
19-491 |
3.75e-151 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 440.09 E-value: 3.75e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 19 RPFIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEagVWSRMAPADRRRILLRFSELILANREE 98
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 99 LALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGE---VAATAYDMTtlvMREPLGIVAAVVPWNYPMSMAAWK 175
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEqipLRGGSFVYT---RREPLGVCAGIGAWNYPIQIACWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 176 LGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIaGKALGLHMDVDCVGFTGSTEVGKYFMQYSG 255
Cdd:PRK13252 163 SAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 256 QSnIKRIGLELGGKSPQVVladcDDLDAAAAGIAAGIFAN---TGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDP 332
Cdd:PRK13252 242 AS-LKEVTMELGGKSPLIV----FDDADLDRAADIAMLANfysSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 333 LDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTE--TGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPV 410
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 411 KGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKA 490
Cdd:PRK13252 397 DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
.
gi 77389950 491 V 491
Cdd:PRK13252 477 V 477
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-491 |
9.65e-149 |
|
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: 432.63 E-value: 9.65e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYnGDV 119
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEVA-ATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTA 198
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIpSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 199 LKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGqSNIKRIGLELGGKSP------- 271
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPfivfdda 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 272 ---QVVladcddldaaaAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQM 348
Cdd:cd07103 240 dldKAV-----------DGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 349 DRVLGYIDAGRADGARPVIGGGRVktETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLA 428
Cdd:cd07103 309 EKVEALVEDAVAKGAKVLTGGKRL--GLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77389950 429 GAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07103 387 AYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
16-495 |
1.13e-148 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 433.57 E-value: 1.13e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 16 LPNRPFIDGQYVDSlSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILAN 95
Cdd:PRK13473 1 MQTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 96 REELALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEvAATAY--DMTTLVMREPLGIVAAVVPWNYPMSMAA 173
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGK-AAGEYleGHTSMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 174 WKLGPALATGNSVILKPAEQSPFTALKFGELAIEAgMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQy 253
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 254 SGQSNIKRIGLELGGKSPqVVLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPL 333
Cdd:PRK13473 235 AAADSVKRTHLELGGKAP-VIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 334 DTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVkTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGF 413
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEA-PDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 414 DEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNcfDRGSLA--VPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVN--THFMLVseMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
....
gi 77389950 492 WFAH 495
Cdd:PRK13473 471 MVKH 474
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
38-491 |
3.64e-148 |
|
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: 431.67 E-value: 3.64e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSrMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNG 117
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYAEAIDKVYGEVAATAYD-----MTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAE 192
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPAlrggpGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 193 QSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQ 272
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 273 VVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVL 352
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMH-NAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 353 GYIDAGRADGARPVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVW 432
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 77389950 433 TGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
21-495 |
4.90e-148 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 432.31 E-value: 4.90e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKR--WAELKAAERKRYLHKIADLIEQHADEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAyNGDVVSAAACIAWYAE-AIDKVYGEVAATAyDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPA 179
Cdd:TIGR02299 82 VLECLDCGQPLRQT-RQQVIRAAENFRFFADkCEEAMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 180 LATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQySGQSNI 259
Cdd:TIGR02299 160 LAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMR-NGADTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 260 KRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANtGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRM 339
Cdd:TIGR02299 239 KRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFN-GERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 340 GSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETG-----GFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFD 414
Cdd:TIGR02299 318 GPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTFRGedlgrGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 415 EAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWFA 494
Cdd:TIGR02299 398 EAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVALA 477
|
.
gi 77389950 495 H 495
Cdd:TIGR02299 478 L 478
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
21-489 |
2.05e-147 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 430.00 E-value: 2.05e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFeaGVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGqSNIK 260
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 261 RIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMG 340
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDADLESAVDGAMLGNFF-SAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 341 SMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTET--GGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMA 418
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGlqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77389950 419 TANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLK 489
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
21-492 |
1.15e-142 |
|
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: 418.01 E-value: 1.15e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELaIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGkYFMQYSGQSNIK 260
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVG-RDVAIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 261 RIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMG 340
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILF-NQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 341 SMVSEEQMDRVLGYIDAGRADGARPVIGGGRVkTETG---GFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAM 417
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTGGHRL-TENGldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77389950 418 ATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVW 492
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIY 472
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
40-492 |
4.91e-142 |
|
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: 415.62 E-value: 4.91e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIAnAYNGDV 119
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGE---VAATAYDMTTlvmREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPF 196
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGEtipVGGRNLHYTL---REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 197 TALKFGELAIEAgMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSnIKRIGLELGGKSPQVVLA 276
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 277 DCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYID 356
Cdd:cd07107 236 DADPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 357 AGRADGARPVIGGGRVKTET--GGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTG 434
Cdd:cd07107 316 SAKREGARLVTGGGRPEGPAleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 77389950 435 SVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVW 492
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
19-491 |
3.85e-141 |
|
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: 413.95 E-value: 3.85e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 19 RPFIDGQYVDSlsGETFACIYPGDGR-PLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANRE 97
Cdd:cd07097 2 RNYIDGEWVAG--GDGEENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 98 ELALLETLNVGKPIANAyNGDVVSAAACIAWYAEAIDKVYGEVAATAY-DMTTLVMREPLGIVAAVVPWNYPMSMAAWKL 176
Cdd:cd07097 78 ELARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPSTRpGVEVETTREPLGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 177 GPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGq 256
Cdd:cd07097 157 APALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 257 SNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTA 336
Cdd:cd07097 236 ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFF-STGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 337 TRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEA 416
Cdd:cd07097 315 VDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77389950 417 MATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRG-SLAVPFGGFKQSGFG-RDKSLHAMDKYTDLKAV 491
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
14-491 |
7.76e-141 |
|
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: 413.81 E-value: 7.76e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 14 VALPNRPFIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRMAPADRRRILLRFSELIL 93
Cdd:cd07140 2 LKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 94 ANREELALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEV----AATAYDMTTLVMREPLGIVAAVVPWNYPM 169
Cdd:cd07140 82 EHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTipinQARPNRNLTLTKREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 170 SMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKY 249
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 250 FMQYSGQSNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAP 329
Cdd:cd07140 242 IMKSCAVSNLKKVSLELGGKSPLII-FADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 330 GDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVL--SA 407
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP--GFFFEPTVFTDVEDHMFIAKEESFGPIMiiSK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 408 IPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTD 487
Cdd:cd07140 399 FDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLK 478
|
....
gi 77389950 488 LKAV 491
Cdd:cd07140 479 TKTV 482
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-491 |
1.21e-140 |
|
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: 412.11 E-value: 1.21e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNGDV 119
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGeVAATAY--DMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFT 197
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEG-PAAGEYlpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 198 ALKFGELAIEaGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQySGQSNIKRIGLELGGKSPqVVLAD 277
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVAR-AAADTLKRVHLELGGKAP-VIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 278 CDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDA 357
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 358 GRAdGARPVIGGGRvkTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVK 437
Cdd:cd07092 318 APA-HARVLTGGRR--AEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 438 NAHRAAKSLRAGVVWVNcfDRGSLA--VPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07092 395 RAMRLSARLDFGTVWVN--THIPLAaeMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
38-491 |
4.39e-140 |
|
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: 410.97 E-value: 4.39e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNG 117
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYA---EAIDKVYGE-VAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQ 193
Cdd:cd07110 79 DVDDVAGCFEYYAdlaEQLDAKAERaVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 194 SPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQV 273
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 274 VLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLG 353
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFW-NNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 354 YIDAGRADGARPVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWT 433
Cdd:cd07110 317 FIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 77389950 434 GSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
13-491 |
3.39e-139 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 410.28 E-value: 3.39e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 13 AVALPNRP-FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAF---EAGVWSRMAPADRRRILLRF 88
Cdd:PLN02467 2 AIPVPRRQlFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 89 SELILANREELALLETLNVGKPIANAyNGDVVSAAACIAWYA---EAIDKVYGevAATAYDMTTL---VMREPLGIVAAV 162
Cdd:PLN02467 82 AAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYAdlaEALDAKQK--APVSLPMETFkgyVLKEPLGVVGLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 163 VPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTG 242
Cdd:PLN02467 159 TPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 243 STEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANtGQVCNAGSRLIVDEKIHDQLLEKIAA 322
Cdd:PLN02467 239 STATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTN-GQICSATSRLLVHERIASEFLEKLVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 323 QAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFG 402
Cdd:PLN02467 317 WAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 403 PVLSaipVKGF---DEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSL 479
Cdd:PLN02467 397 PVLC---VKTFsteDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGE 473
|
490
....*....|..
gi 77389950 480 HAMDKYTDLKAV 491
Cdd:PLN02467 474 WGLENYLSVKQV 485
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
21-495 |
3.29e-138 |
|
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: 406.73 E-value: 3.29e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPL-TDVASCNAADVDVAVRSARKAFeaGVWSRMAPADRRRILLRFSELILANREEL 99
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 100 ALLETLNVGKPIANAyNGDVVSAAACIAWYAEAIDKVYGEVAATAY-DMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGP 178
Cdd:cd07131 80 ARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSELpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 179 ALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSN 258
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 259 iKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATR 338
Cdd:cd07131 239 -KRVALEMGGKNPIIV-MDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 339 MGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETG--GFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEA 416
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 417 MATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLA-VPFGGFKQSGFG-RDKSLHAMDKYTDLKAVWFA 494
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWKAVYVD 476
|
.
gi 77389950 495 H 495
Cdd:cd07131 477 Y 477
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-491 |
1.35e-135 |
|
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: 399.43 E-value: 1.35e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNGDV 119
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPE--WAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTAL 199
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 200 KFGELAIEAgMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCD 279
Cdd:cd07108 162 LLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 280 DLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGR 359
Cdd:cd07108 240 LDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 360 A-DGARpVIGGGRVKTETG---GFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGS 435
Cdd:cd07108 320 StSGAT-VLRGGPLPGEGPladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 436 VKNAHRAAKSLRAGVVWVNcfdRGSLAVP---FGGFKQSGFGRDKSLHAM-DKYTDLKAV 491
Cdd:cd07108 399 LGRALRAAHALEAGWVQVN---QGGGQQPgqsYGGFKQSGLGREASLEGMlEHFTQKKTV 455
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
21-493 |
4.30e-134 |
|
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: 395.87 E-value: 4.30e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYnGDVVSAAACIAWYAEAIDKVYGEV-AATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPA 179
Cdd:cd07088 79 KLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIiPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 180 LATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNI 259
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 260 KRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRM 339
Cdd:cd07088 237 TKVSLELGGKAPAIV-MKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 340 GSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETGGFYiEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMAT 419
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFY-EPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77389950 420 ANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWF 493
Cdd:cd07088 395 ANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
21-489 |
2.15e-132 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 392.20 E-value: 2.15e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELaIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIK 260
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 261 RIGLELGGKSPQV----VLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTA 336
Cdd:cd07116 240 PVTLELGGKSPNIffadVMDADDAFFDKALEGFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 337 TRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGR--VKTETGGFYIEPTIFEGvRNDMKIAQEEIFGPVLSAIPVKGFD 414
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERneLGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77389950 415 EAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLK 489
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
19-485 |
1.10e-130 |
|
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: 387.52 E-value: 1.10e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 19 RPFIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREE 98
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 99 LALLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAAtaydmttlvmREPLGIVAAVVPWNYPMSMAAWKLGP 178
Cdd:cd07111 101 FAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAG----------WKPVGVVGQIVPWNFPLLMLAWKICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 179 ALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHiAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSN 258
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 259 iKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATR 338
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWF-NQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAID 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 339 MGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMA 418
Cdd:cd07111 328 MGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSK--GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77389950 419 TANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKY 485
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-493 |
1.89e-128 |
|
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: 380.72 E-value: 1.89e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNGDV 119
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVygEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTAL 199
Cdd:cd07106 81 GGAVAWLRYTASLDLPD--EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 200 KFGELAIEAgMPPGVLNVVPGLGHIaGKALGLHMDVDCVGFTGSTEVGKYFMQySGQSNIKRIGLELGGKSPQVVLADCD 279
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMA-SAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 280 DLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGR 359
Cdd:cd07106 236 IDAVAPKLFWGAFI-NSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 360 ADGARPVIGGGRVktETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNA 439
Cdd:cd07106 315 AKGAKVLAGGEPL--DGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 77389950 440 HRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWF 493
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
21-491 |
4.43e-124 |
|
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: 370.62 E-value: 4.43e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEaGVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNGDVVSAAACIAWYAEAIDKVYGEVAATAY------DMTTLVMREPLGIVAAVVPWNYPMSMAAW 174
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIpsmqgeRYTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 175 KLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGlHMDVDCVGFTGSTEVGKYfMQYS 254
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLIS-HPDVAKVSFTGSVATGKK-IGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 255 GQSNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLD 334
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAF-LKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 335 TATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFD 414
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGE--GYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77389950 415 EAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
62-493 |
9.16e-123 |
|
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: 363.47 E-value: 9.16e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 62 RSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYnGDVVSAAACIAWYAEAIDKVYG-EV 140
Cdd:cd06534 1 AAARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGpEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 141 AATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPG 220
Cdd:cd06534 78 PSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 221 LGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVC 300
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIV-DEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 301 NAGSRLIVDEKIHDQLLEKIAaqakvfapgdpldtatrmgsmvseeqmdrvlgyidagradgarpvigggrvktetggfy 380
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 381 iepTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRG- 459
Cdd:cd06534 257 ---TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGv 333
|
410 420 430
....*....|....*....|....*....|....
gi 77389950 460 SLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWF 493
Cdd:cd06534 334 GPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
21-491 |
1.26e-119 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 360.16 E-value: 1.26e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEagVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYnGDVVSAAACIAWYAEAIDKVYGEVAATAY-DMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPA 179
Cdd:PLN02278 106 QLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPFpDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 180 LATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSnI 259
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT-V 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 260 KRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRM 339
Cdd:PLN02278 264 KRVSLELGGNAPFIV-FDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 340 GSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVkTETGGFYiEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMAT 419
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRH-SLGGTFY-EPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77389950 420 ANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
38-493 |
9.26e-119 |
|
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: 356.14 E-value: 9.26e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEAGvwSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYnG 117
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM--KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR-K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYAEAIDKVYGEV-----AATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAE 192
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETipfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 193 QSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGqsnIKRIGLELGGKSPQ 272
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 273 VVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVL 352
Cdd:cd07149 238 IV-DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 353 GYIDAGRADGARPVIGGGRvkteTGGFYiEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVW 432
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKR----DGAIL-EPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 433 TGSVKNAHRAAKSLRAGVVWVNC-----FDrgslAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWF 493
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMINDsstfrVD----HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
20-474 |
6.93e-117 |
|
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: 353.45 E-value: 6.93e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 20 PFIDGQYVDSlsGETFACIYPGD-GRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREE 98
Cdd:cd07124 35 LVIGGKEVRT--EEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 99 LALLETLNVGKPIANAYnGDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGP 178
Cdd:cd07124 111 LAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 179 ALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYS---- 254
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAakvq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 255 -GQSNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANtGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPL 333
Cdd:cd07124 270 pGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQ-GQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 334 DTATRMGSMVSEEQMDRVLGYIDAGRADGaRPVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGF 413
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 414 DEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNcfdRGSLAV-----PFGGFKQSGFG 474
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN---RKITGAlvgrqPFGGFKMSGTG 490
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
56-491 |
9.54e-113 |
|
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: 339.89 E-value: 9.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 56 DVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALL---ETlnvGKPIANAyNGDVVSAAACIAWYAEA 132
Cdd:cd07104 1 DVDRAYAAAAAAQKA--WAATPPQERAAILRKAAEILEERRDEIADWlirES---GSTRPKA-AFEVGAAIAILREAAGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 133 IDKVYGEVAATAYDMTT-LVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFT-ALKFGELAIEAGM 210
Cdd:cd07104 75 PRRPEGEILPSDVPGKEsMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 211 PPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAA 290
Cdd:cd07104 155 PKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 291 GIFANtGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGg 370
Cdd:cd07104 234 AFLHQ-GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 371 rvkTETGGFYiEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGV 450
Cdd:cd07104 312 ---TYEGLFY-QPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 77389950 451 VWVNCfdrGSLA----VPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07104 388 VHIND---QTVNdephVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
40-489 |
1.68e-112 |
|
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: 340.09 E-value: 1.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEagVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNGDV 119
Cdd:cd07145 6 PANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGE---VAATAYDMTTLVM--REPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQS 194
Cdd:cd07145 83 ERTIRLFKLAAEEAKVLRGEtipVDAYEYNERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 195 PFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGqSNIKRIGLELGGKSPQVV 274
Cdd:cd07145 163 PLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGSDPMIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 275 lADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGY 354
Cdd:cd07145 242 -LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 355 IDAGRADGARPVIGGGRvkteTGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTG 434
Cdd:cd07145 321 VNDAVEKGGKILYGGKR----DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 77389950 435 SVKNAHRAAKSLRAGVVWVNcfDRGSL---AVPFGGFKQSGFGRDKSLHAMDKYTDLK 489
Cdd:cd07145 397 DINRALKVARELEAGGVVIN--DSTRFrwdNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
21-491 |
7.29e-110 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 334.15 E-value: 7.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSlSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFeaGVWsRMAPADRR-RILLRFSELILANREEL 99
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEW-RKVPAPRRgEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 100 ALLETLNVGKPIANAYnGDVVsaaaciawyaEAID----------KVYGEVAAT---AYDMTTlvMREPLGIVAAVVPWN 166
Cdd:cd07086 78 GRLVSLEMGKILPEGL-GEVQ----------EMIDicdyavglsrMLYGLTIPSerpGHRLME--QWNPLGVVGVITAFN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 167 YPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEA----GMPPGVLNVVPGLGHIaGKALGLHMDVDCVGFTG 242
Cdd:cd07086 145 FPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 243 STEVGKYFMQYSGQSNiKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAA 322
Cdd:cd07086 224 STEVGRRVGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVG-TAGQRCTTTRRLIVHESVYDEFLERLVK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 323 QAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFG 402
Cdd:cd07086 302 AYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 403 PVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRA--AKSLRAGVVWVNCFDRGS-LAVPFGGFKQSGFGRDKSL 479
Cdd:cd07086 382 PILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGEKETGGGRESGS 461
|
490
....*....|..
gi 77389950 480 HAMDKYTDLKAV 491
Cdd:cd07086 462 DAWKQYMRRSTC 473
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
40-491 |
1.12e-109 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 332.76 E-value: 1.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYnGDV 119
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW-FET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEVAATAY-DMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTA 198
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 199 LKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVlADC 278
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPLIV-LAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 279 DDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAG 358
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 359 RADGARPVIGGgrvkTETGGFYiEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKN 438
Cdd:cd07150 321 VAKGAKLLTGG----KYDGNFY-QPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 77389950 439 AHRAAKSLRAGVVWVNCFD-RGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07150 396 AFKLAERLESGMVHINDPTiLDEAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
27-491 |
1.02e-105 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 324.91 E-value: 1.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 27 VDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAfeAGVWSRMAPADRRRILLRFSELILANREELALLETLN 106
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 107 VGKPIANAYNgDVVSAAACIAWYAEAIDKVYGE--VAATAYDMT-TLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATG 183
Cdd:PRK09407 104 TGKARRHAFE-EVLDVALTARYYARRAPKLLAPrrRAGALPVLTkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 184 NSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHmdVDCVGFTGSTEVGKYFMQYSGQsniKRIG 263
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGR---RLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 264 --LELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGS 341
Cdd:PRK09407 258 fsLELGGKNPMIVLDDADLDKAAAGAVRACFS-NAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 342 MVSEEQMDRVLGYIDAGRADGARpVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATAN 421
Cdd:PRK09407 337 LISEAQLETVSAHVDDAVAKGAT-VLAGGKARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77389950 422 DTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVN---CFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:PRK09407 416 DTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyAAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-491 |
1.48e-105 |
|
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: 323.31 E-value: 1.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07085 4 FINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYnGDV-----VSAAACIAWYAEAIDkvYGEVAATayDMTTLVMREPLGIVAAVVPWNYPMSMAAWK 175
Cdd:cd07085 82 RLITLEHGKTLADAR-GDVlrgleVVEFACSIPHLLKGE--YLENVAR--GIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 176 LGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGlGHIAGKALGLHMDVDCVGFTGSTEVGKYFmqYS- 254
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYI--YEr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 255 GQSNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLD 334
Cdd:cd07085 234 AAANGKRVQALGGAKNHAVV-MPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 335 TATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTE--TGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKG 412
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 413 FDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCfdrgSLAVP-----FGGFKQSGFGrdkSLHAMDK--- 484
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV----PIPVPlaffsFGGWKGSFFG---DLHFYGKdgv 465
|
....*....
gi 77389950 485 --YTDLKAV 491
Cdd:cd07085 466 rfYTQTKTV 474
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
40-491 |
2.40e-105 |
|
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: 321.99 E-value: 2.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAGVWSRmAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNGDV 119
Cdd:cd07120 4 PATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTAL 199
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 200 KFGELAIEA-GMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQySGQSNIKRIGLELGGKSPQVVLADC 278
Cdd:cd07120 162 AIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMA-AAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 279 DDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAG 358
Cdd:cd07120 241 DLDAALPKLERALTI-FAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 359 RADGARPVIGGGRVKTE-TGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVK 437
Cdd:cd07120 320 IAAGAEVVLRGGPVTEGlAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 77389950 438 NAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
40-491 |
2.22e-101 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 311.55 E-value: 2.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNgDV 119
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE-EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEV---AATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPF 196
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRrrrGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 197 TALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHmdVDCVGFTGSTEVGKYFMQYSGQsniKRIG--LELGGKSPQVV 274
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR---RLIGcsLELGGKNPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 275 lADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGY 354
Cdd:cd07101 235 -LEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 355 IDAGRADGARpVIGGGRVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTG 434
Cdd:cd07101 314 VDDAVAKGAT-VLAGGRARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 435 SVKNAHRAAKSLRAGVVWVN---CFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNegyAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
24-491 |
6.36e-100 |
|
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: 308.08 E-value: 6.36e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 24 GQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLE 103
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKE--WAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 104 TLNVGKPIANAyNGDVVSAAACIAWYAEAIDKVYGE-VAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALAT 182
Cdd:cd07151 79 IRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRiLPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 183 GNSVILKPAEQSPFTA-LKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKR 261
Cdd:cd07151 158 GNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 262 IGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANtGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGS 341
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQ-GQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 342 MVSEEQMDRVLGYIDAGRADGARPVIGGGRVktetgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATAN 421
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGGEAE-----GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77389950 422 DTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLA-VPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
22-472 |
3.41e-99 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 308.02 E-value: 3.41e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 22 IDGQYVDSlsGETFACIYPGDGRPLT-DVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:PRK03137 41 IGGERITT--EDKIVSINPANKSEVVgRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAyNGDVvsaaaciawyAEAID--KVYGEVAATAYDMTTLVMRE---------PLGIVAAVVPWNYPM 169
Cdd:PRK03137 117 AWLVKEAGKPWAEA-DADT----------AEAIDflEYYARQMLKLADGKPVESRPgehnryfyiPLGVGVVISPWNFPF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 170 SMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKY 249
Cdd:PRK03137 186 AIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 250 FMQYS-----GQSNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANtGQVCNAGSRLIVDEKIHDQLLEKIAAQA 324
Cdd:PRK03137 266 IYERAakvqpGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFS-GQKCSACSRAIVHEDVYDEVLEKVVELT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 325 KVFAPGDPLDtATRMGSMVSEEQMDRVLGYIDAGRADGaRPVIGGGRvkTETGGFYIEPTIFEGVRNDMKIAQEEIFGPV 404
Cdd:PRK03137 345 KELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEG--DDSKGYFIQPTIFADVDPKARIMQEEIFGPV 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77389950 405 LSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNcfdRGSLAV-----PFGGFKQSG 472
Cdd:PRK03137 421 VAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN---RGCTGAivgyhPFGGFNMSG 490
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
38-489 |
1.07e-97 |
|
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: 301.86 E-value: 1.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEagVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNG 117
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYAEAIDKVYGEV-----AATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAE 192
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVlpldiSARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 193 QSPFTALKFGELAIEAGMPPGVLNVVPgLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsniKRIGLELGGKSPq 272
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNAA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 273 VVLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVL 352
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 353 GYIDAGRADGARPVIGGGRvktetGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVW 432
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGKR-----DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 433 TGSVKNAHRAAKSLRAGVVWVNcfDRGSLAV---PFGGFKQSGFGRDKSLHAMDKYTDLK 489
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVIN--DVPTFRVdhmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
57-492 |
5.69e-97 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 299.38 E-value: 5.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 57 VDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNGDVVSAAACIAWYAEAI--- 133
Cdd:cd07100 1 IEAALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAENAeaf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 134 --DKVYGEVAATAYdmttlVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMP 211
Cdd:cd07100 78 laDEPIETDAGKAY-----VRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 212 PGVLNVVPgLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAG 291
Cdd:cd07100 153 EGVFQNLL-IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 292 IFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGR 371
Cdd:cd07100 231 LQ-NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 372 VKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVV 451
Cdd:cd07100 310 PDGP--GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 77389950 452 WVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVW 492
Cdd:cd07100 388 FINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
21-486 |
1.92e-96 |
|
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: 299.49 E-value: 1.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSlSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEaGVWSRMAPADRRRILLRFSELILANREELA 100
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR-GWWPTMPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAyNGDVVSAAACIAWYAEAIDKVYGEVA-----ATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWK 175
Cdd:cd07082 83 NLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRLDGDSLpgdwfPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 176 LGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQysg 255
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 256 QSNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANtGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDT 335
Cdd:cd07082 239 QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 336 ATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRvkteTGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDE 415
Cdd:cd07082 318 GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR----EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77389950 416 AMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCF-DRGSLAVPFGGFKQSGFGRD---KSLHAMDKYT 486
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcQRGPDHFPFLGRKDSGIGTQgigDALRSMTRRK 468
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-491 |
3.92e-96 |
|
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: 298.19 E-value: 3.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEagVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNGDV 119
Cdd:cd07094 6 PYDGEVIGKVPADDRADAEEALATARAGAE--NRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKVYGEV-----AATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQS 194
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEipldaTQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 195 PFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFmqySGQSNIKRIGLELGGKSPQVV 274
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL---RANAGGKRIALELGGNAPVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 275 LADCDDLDAAAAGIAAGIFAnTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGY 354
Cdd:cd07094 240 DRDADLDAAIEALAKGGFYH-AGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 355 IDAGRADGARPVIGGGRVKTetggfYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTG 434
Cdd:cd07094 319 VEEAVEAGARLLCGGERDGA-----LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 435 SVKNAHRAAKSLRAGVVWVN---CFDrgSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNdssAFR--TDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
21-489 |
3.66e-95 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 296.43 E-value: 3.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAyNGDVVSAAACIAWYAEAIDKVYGE-VAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPA 179
Cdd:PRK11241 92 RLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDtIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 180 LATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNI 259
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 260 KRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRM 339
Cdd:PRK11241 250 KKVSLELGGNAPFIV-FDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 340 GSMVSEEQMDRVLGYIDAGRADGARpVIGGGRVKtETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMAT 419
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGAR-VVCGGKAH-ELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQ 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 420 ANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLK 489
Cdd:PRK11241 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-491 |
2.12e-93 |
|
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: 291.05 E-value: 2.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYnGDV 119
Cdd:cd07099 3 PATGEVLGEVPVTDPAEVAAAVARARAAQRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEAIDKV--YGEVAATAYDM--TTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSP 195
Cdd:cd07099 80 LLALEAIDWAARNAPRVlaPRKVPTGLLMPnkKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 196 FTALKFGELAIEAGMPPGVLNVVPGLGHiAGKALgLHMDVDCVGFTGSTEVGKYFMQYSGQSNIKrIGLELGGKSPQVVL 275
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAAL-IDAGVDKVAFTGSVATGRKVMAAAAERLIP-VVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 276 ADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYI 355
Cdd:cd07099 237 ADADLERAAAAAVWGAMV-NAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 356 DAGRADGARPVIGGGRvkTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGS 435
Cdd:cd07099 316 DDAVAKGAKALTGGAR--SNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 77389950 436 VKNAHRAAKSLRAGVVWVNC--FDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
39-489 |
1.68e-91 |
|
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: 286.18 E-value: 1.68e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 39 YPGDGRPLTDVASCNAADVDVAVRSArkafeAGVWSRMAPADRRRILLRFSELILANREELALLETLNVGK-------PI 111
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALA-----ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLclkdtryEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 112 ANAYNGDVVSAAACIAWYAEAIDKvygEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPA 191
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFSC---DLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 192 EQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFmqySGQSNIKRIGLELGGKSP 271
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 272 QVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRV 351
Cdd:cd07146 234 LIV-MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 352 LGYIDAGRADGARPVIGGGRVktetGGFYiEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAV 431
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQRQ----GALY-APTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77389950 432 WTGSVKNAHRAAKSLRAGVVWVN---CFDrgSLAVPFGGFKQSGFG-RDKSLHAMDKYTDLK 489
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNevpGFR--SELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
38-491 |
1.72e-91 |
|
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: 286.06 E-value: 1.72e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIAnAYNG 117
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIA-QAGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYAEAIDKVYGEVAATAYD-MTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPF 196
Cdd:cd07102 78 EIRGMLERARYMISIAEEALADIRVPEKDgFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 197 TALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHmDVDCVGFTGSTEVGKYfMQYSGQSNIKRIGLELGGKSPQVVLA 276
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRA-IQRAAAGRFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 277 DCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYID 356
Cdd:cd07102 236 DADLDAAAESLVDGAFF-NSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 357 AGRADGARPVIGGGR-VKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGS 435
Cdd:cd07102 315 DAIAKGARALIDGALfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 436 VKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07102 395 IARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
56-491 |
1.03e-90 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 283.31 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 56 DVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPiANAYNGDVVSAAACIAWYAEAIDK 135
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 136 VYGE-VAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGV 214
Cdd:cd07105 78 IIGGsIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 215 LNVV---PGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAG 291
Cdd:cd07105 158 LNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 292 IFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQA-KVFAPGDPLdtatrmGSMVSEEQMDRVLGYIDAGRADGARpVIGGG 370
Cdd:cd07105 237 FL-NSGQICMSTERIIVHESIADEFVEKLKAAAeKLFAGPVVL------GSLVSAAAADRVKELVDDALSKGAK-LVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 371 RVKTETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGV 450
Cdd:cd07105 309 LADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 77389950 451 VWVNcfdrgSLAV------PFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07105 389 VHIN-----GMTVhdeptlPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
43-474 |
4.47e-85 |
|
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: 269.16 E-value: 4.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 43 GRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAynGDVVSA 122
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA--GFEVGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 123 AACIAWYAEAI-DKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTA-LK 200
Cdd:cd07152 77 AIGELHEAAGLpTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 201 FGELAIEAGMPPGVLNVVPGlGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDD 280
Cdd:cd07152 157 IARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 281 LDAAaAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRA 360
Cdd:cd07152 235 DLAA-SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 361 DGARPVIGGgrvkTETGGFYiEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAH 440
Cdd:cd07152 314 AGARLEAGG----TYDGLFY-RPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 77389950 441 RAAKSLRAGVVWVNcfDRGSLA---VPFGGFKQSGFG 474
Cdd:cd07152 389 ALADRLRTGMLHIN--DQTVNDephNPFGGMGASGNG 423
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
40-475 |
3.40e-81 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 259.92 E-value: 3.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNGDV 119
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQRE--WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 120 VSAAACIAWYAEaidkvYGEVA-ATAYDMTTLVM--------REPLGIVAAVVPWNYPMSMAawkLGPALA---TGNSVI 187
Cdd:cd07098 81 LVTCEKIRWTLK-----HGEKAlRPESRPGGLLMfykrarveYEPLGVVGAIVSWNYPFHNL---LGPIIAalfAGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 188 LKPAEQSPFTALKFGELAIEA----GMPPGVLNVVPGLGHiAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSNIKRIg 263
Cdd:cd07098 153 VKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVV- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 264 LELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMV 343
Cdd:cd07098 231 LELGGKDPAIVLDDADLDQIASIIMRGTFQ-SSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 344 SEEQMDRVLGYIDAGRADGARPVIGGGRVK--TETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATAN 421
Cdd:cd07098 310 SPARFDRLEELVADAVEKGARLLAGGKRYPhpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 422 DTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSLAV--PFGGFKQSGFGR 475
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGR 445
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
85-492 |
6.21e-77 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 246.96 E-value: 6.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 85 LLRFSELILANREELALLETLNVGKPIANAyNGDVVSAAACIAWYAEAIDKVYGE-VAATAYDMTTLVMREPLGIVAAVV 163
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEiIQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 164 PWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGS 243
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 244 TEVGKYFMQYSGQsNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQ 323
Cdd:PRK10090 160 VSAGEKIMAAAAK-NITKVCLELGGKAPAIV-MDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 324 AKVFAPGDPLD-TATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRvkTETGGFYIEPTIFEGVRNDMKIAQEEIFG 402
Cdd:PRK10090 238 MQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKA--VEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 403 PVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNcfdRGSLAVPFG---GFKQSGFGRDKSL 479
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN---RENFEAMQGfhaGWRKSGIGGADGK 392
|
410
....*....|...
gi 77389950 480 HAMDKYTDLKAVW 492
Cdd:PRK10090 393 HGLHEYLQTQVVY 405
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
56-483 |
3.82e-71 |
|
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: 232.55 E-value: 3.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 56 DVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNGDVVSAAACIAWYAEAIDK 135
Cdd:cd07095 1 QVDAAVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 136 VYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVL 215
Cdd:cd07095 78 RTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 216 NVVPGlGHIAGKALGLHMDVDCVGFTGSTEVGKYF-MQYSGQSNiKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFA 294
Cdd:cd07095 158 NLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPG-KILALEMGGNNPLVV-WDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 295 NTGQVCNAGSRLIVDEK-IHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVk 373
Cdd:cd07095 235 TAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERL- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 374 tETGGFYIEPTIFEgvRNDMK-IAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVW 452
Cdd:cd07095 314 -VAGTAFLSPGIID--VTDAAdVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
410 420 430
....*....|....*....|....*....|..
gi 77389950 453 VNCFDRG-SLAVPFGGFKQSGFGRDKSLHAMD 483
Cdd:cd07095 391 WNRPTTGaSSTAPFGGVGLSGNHRPSAYYAAD 422
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
36-494 |
1.89e-70 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 231.55 E-value: 1.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 36 ACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEagVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAy 115
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFR--DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 116 NGDVVSAAACIAWYAEAIDKVYGEVAATAYDM---TTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAE 192
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADEPADAAAVgasRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 193 QSPFTALKFGELAIEAGMPPGVLNVVPgLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSnIKRIGLELGGKSPQ 272
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 273 VVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVL 352
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQ-NNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 353 GYIDAGRADGARPVIGGGRVktETGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVW 432
Cdd:PRK09406 318 KQVDDAVAAGATILCGGKRP--DGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77389950 433 TGSVKNAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWFA 494
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
49-491 |
1.42e-69 |
|
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: 230.54 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 49 VASCNAADVDVAVRSARKAFeaGVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNgDVVSAAACIAW 128
Cdd:cd07083 49 TAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAID-DVAEAIDFIRY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 129 YAEAIDKVYG---EVAATAYDMTTLVMRePLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELA 205
Cdd:cd07083 126 YARAALRLRYpavEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 206 IEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQ-----YSGQSNIKRIGLELGGKSPQVVLADCDD 280
Cdd:cd07083 205 HEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEaaarlAPGQTWFKRLYVETGGKNAIIVDETADF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 281 LDAAAAGIAAGIFANtGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRA 360
Cdd:cd07083 285 ELVVEGVVVSAFGFQ-GQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 361 DGaRPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKG--FDEAMATANDTVYGLAGAVWTGSVKN 438
Cdd:cd07083 364 EG-QLVLGGKRLEGE--GYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDddFAEALEVANSTPYGLTGGVYSRKREH 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 439 AHRAAKSLRAGVVWVNCFDRGSLA--VPFGGFKQSGFG-RDKSLHAMDKYTDLKAV 491
Cdd:cd07083 441 LEEARREFHVGNLYINRKITGALVgvQPFGGFKLSGTNaKTGGPHYLRRFLEMKAV 496
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
21-483 |
1.81e-65 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 219.06 E-value: 1.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSlSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNgDVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPAL 180
Cdd:PRK09457 81 EVIARETGKPLWEAAT-EVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 181 ATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGlGHIAGKALGLHMDVDCVGFTGSTEVGKYF-MQYSGQSNi 259
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQFAGQPE- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 260 KRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIH-DQLLEKIAAQAKVFAPGDPL-DTAT 337
Cdd:PRK09457 238 KILALEMGGNNPLVI-DEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDaEPQP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 338 RMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETGgfYIEPTIFEgVRNDMKIAQEEIFGPVLSAIPVKGFDEAM 417
Cdd:PRK09457 317 FMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTG--LLTPGIID-VTGVAELPDEEYFGPLLQVVRYDDFDEAI 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77389950 418 ATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVV-WVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMD 483
Cdd:PRK09457 394 RLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHRPSAYYAAD 460
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
4-474 |
8.76e-62 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 210.13 E-value: 8.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 4 EIDWHARAKAVALPN------RPFIDGQyvDSLSGETFACIYPGDG-RPLTDVASCNAADVDVAVRSARKAFEAgvWSRM 76
Cdd:cd07125 13 EVPLEALADALKAFDekeweaIPIINGE--ETETGEGAPVIDPADHeRTIGEVSLADAEDVDAALAIAAAAFAG--WSAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 77 APADRRRILLRFSELILANREELALLETLNVGKPIANAyngDV-VSAAA--CiAWYAEAIDKVYGEVAATAY-DMTTLVM 152
Cdd:cd07125 89 PVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA---DAeVREAIdfC-RYYAAQARELFSDPELPGPtGELNGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 153 REPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLH 232
Cdd:cd07125 165 LHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 233 MDVDCVGFTGSTEVGKYFMqysgQSNIKRIGL------ELGGKSP----------QVVladcddldaaaAGIAAGIFANT 296
Cdd:cd07125 245 PRIDGVIFTGSTETAKLIN----RALAERDGPilpliaETGGKNAmivdstalpeQAV-----------KDVVQSAFGSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 297 GQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADG---ARPVIGggrvk 373
Cdd:cd07125 310 GQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAwliAPAPLD----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 374 tETGGFYIEPTIFEGVRNDmkIAQEEIFGPVLSAIPVKGF--DEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVV 451
Cdd:cd07125 385 -DGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNL 461
|
490 500
....*....|....*....|....*...
gi 77389950 452 WVNcfdRGSL-AV----PFGGFKQSGFG 474
Cdd:cd07125 462 YIN---RNITgAIvgrqPFGGWGLSGTG 486
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-492 |
1.85e-61 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 208.18 E-value: 1.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 38 IYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNG 117
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-RA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 118 DVVSAAACIAWYAEAIDKVYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFT 197
Cdd:PRK13968 89 EVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 198 ALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGlHMDVDCVGFTGSTEVGKYFMQYSGQSnIKRIGLELGGKSPQVVLAD 277
Cdd:PRK13968 169 AQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 278 CDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDA 357
Cdd:PRK13968 247 ADLELAVKAAVAGRYQ-NTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 358 GRADGARPVIGGGRVKTEtgGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVK 437
Cdd:PRK13968 326 TLAEGARLLLGGEKIAGA--GNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 77389950 438 NAHRAAKSLRAGVVWVNCFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVW 492
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
31-475 |
2.06e-60 |
|
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: 205.52 E-value: 2.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 31 SGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEagVWsRMAPADRRRILLR-FSELILANREELALLETLNVGK 109
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EW-RDVPAPKRGEIVRqIGDALRKKKEALGKLVSLEMGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 110 PIANAYnGDVvsaaaciawyAEAID----------KVYGEVAATayDMTTLVMRE---PLGIVAAVVPWNYPMSMAAWKL 176
Cdd:cd07130 87 ILPEGL-GEV----------QEMIDicdfavglsrQLYGLTIPS--ERPGHRMMEqwnPLGVVGVITAFNFPVAVWGWNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 177 GPALATGNSVILKPAEQSPFTALK----FGELAIEAGMPPGVLNVVPGlGHIAGKALGLHMDVDCVGFTGSTEVGKYFmq 252
Cdd:cd07130 154 AIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 253 ysGQSNIKRIG---LELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAP 329
Cdd:cd07130 231 --GQAVAARFGrslLELGGNNAIIVMEDADLDLAVRAVLFAAVG-TAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 330 GDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVktETGGFYIEPTIFEGvRNDMKIAQEEIFGPVLSAIP 409
Cdd:cd07130 308 GDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVI--DGPGNYVEPTIVEG-LSDAPIVKEETFAPILYVLK 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 77389950 410 VKGFDEAMATANDTVYGLAGAVWTGSVKNAHR--AAKSLRAGVVWVNCFDRGS-LAVPFGGFKQSGFGR 475
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRwlGPKGSDCGIVNVNIGTSGAeIGGAFGGEKETGGGR 453
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
40-492 |
5.91e-57 |
|
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: 195.72 E-value: 5.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 40 PGDGRPLTDVASCNAADVDVAVRSARKAF-EAGVWsrMAPADRRRILLRFSELILANREELALLETLNVGKPIANAyNGD 118
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA-KVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 119 VVSAAACIAWYAEAIDKVYGE-----VAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQ 193
Cdd:cd07148 83 VTRAIDGVELAADELGQLGGReipmgLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 194 SPFTALKFGELAIEAGMPPGVLNVVPgLGHIAGKALGLHMDVDCVGFTGSTEVGkyFMQYSGQSNIKRIGLELGGKSPqV 273
Cdd:cd07148 163 TPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVG--WMLRSKLAPGTRCALEHGGAAP-V 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 274 VLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLG 353
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 354 YIDAGRADGARPVIGGGRVKTETggfyIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWT 433
Cdd:cd07148 319 WVNEAVAAGARLLCGGKRLSDTT----YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77389950 434 GSVKNAHRAAKSLRAGVVWVNcfDRGSLAV---PFGGFKQSGFGRDKSLHAMDKYTDLK-AVW 492
Cdd:cd07148 395 KDLDVALKAVRRLDATAVMVN--DHTAFRVdwmPFAGRRQSGYGTGGIPYTMHDMTQEKmAVI 455
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
60-475 |
1.02e-55 |
|
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: 191.59 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 60 AVRSARKAFEAGvwsRMAP-ADRRRILLRFSELILANREEL--ALLETLnvGKPIANAYNGDVVSAAACIAWYAEAIDK- 135
Cdd:cd07087 3 LVARLRETFLTG---KTRSlEWRKAQLKALKRMLTENEEEIaaALYADL--GKPPAEAYLTEIAVVLGEIDHALKHLKKw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 136 -----VygEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAawkLGP---ALATGNSVILKPAEQSPFTALKFGELaIE 207
Cdd:cd07087 78 mkprrV--SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKL-IP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 208 AGMPPGVLNVVPGLGHIAGKALGLHMdvDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVlADCDDLDAAAAG 287
Cdd:cd07087 152 KYFDPEAVAVVEGGVEVATALLAEPF--DHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIV-DKDANLEVAARR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 288 IAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTAtRMGSMVSEEQMDRVLGYIDAGradgaRPVI 367
Cdd:cd07087 228 IAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDG-----KVVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 368 GGGRVKTETggfYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLR 447
Cdd:cd07087 302 GGQVDKEER---YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETS 378
|
410 420 430
....*....|....*....|....*....|
gi 77389950 448 AGVVWVN--CFDRGSLAVPFGGFKQSGFGR 475
Cdd:cd07087 379 SGGVCVNdvLLHAAIPNLPFGGVGNSGMGA 408
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-474 |
2.93e-54 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 189.58 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 21 FIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELA 100
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA--WAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 101 LLETLNVGKPIANAYNgDVVSAAACIAWYAEAIDKVYGE-----------VAATAYDMTTLVmrePLGIVAAVVPWNYPM 169
Cdd:PLN00412 97 ECLVKEIAKPAKDAVT-EVVRSGDLISYTAEEGVRILGEgkflvsdsfpgNERNKYCLTSKI---PLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 170 SMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGstevGKY 249
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG----GDT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 250 FMQYSGQSNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFAnTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAP 329
Cdd:PLN00412 249 GIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSY-SGQRCTAVKVVLVMESVADALVEKVNAKVAKLTV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 330 GDPLDTATrMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRvktetGGFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIP 409
Cdd:PLN00412 328 GPPEDDCD-ITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-----EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77389950 410 VKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFD-RGSLAVPFGGFKQSGFG 474
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPaRGPDHFPFQGLKDSGIG 467
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
16-491 |
4.92e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 188.80 E-value: 4.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 16 LPNrpFIDGQYVDSLSGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAFEagVWSRMAPADRRRILLRFSELILAN 95
Cdd:PLN02419 114 VPN--LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRKN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 96 REELALLETLNVGKPIANAYnGDVVSAAACIAWYAEAIDKVYGE-VAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAW 174
Cdd:PLN02419 190 MDKLAMNITTEQGKTLKDSH-GDIFRGLEVVEHACGMATLQMGEyLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLW 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 175 KLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAgKALGLHMDVDCVGFTGSTEVGKYFMQYS 254
Cdd:PLN02419 269 MFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARA 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 255 GQSNiKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFAnTGQVCNAGSRLIV--DEKI-HDQLLEKiAAQAKVFAPGD 331
Cdd:PLN02419 348 AAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGA-AGQRCMALSTVVFvgDAKSwEDKLVER-AKALKVTCGSE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 332 PldtATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKT---ETGGFyIEPTIFEGVRNDMKIAQEEIFGPVLSAI 408
Cdd:PLN02419 425 P---DADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVpgyEKGNF-IGPTILSGVTPDMECYKEEIFGPVLVCM 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 409 PVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCfdrgSLAVPFGGFKQSG----FGRDKSLH---A 481
Cdd:PLN02419 501 QANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV----PIPVPLPFFSFTGnkasFAGDLNFYgkaG 576
|
490
....*....|
gi 77389950 482 MDKYTDLKAV 491
Cdd:PLN02419 577 VDFFTQIKLV 586
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
22-472 |
6.05e-49 |
|
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: 175.85 E-value: 6.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 22 IDGQYVDSlsGETFACIYPGD-GRPLTDVASCNAADVDVAVRSARKAfeAGVWSRMAPADRRRILLRFSELILAN-REEL 99
Cdd:cd07123 37 IGGKEVRT--GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA--RKEWARMPFEDRAAIFLKAADLLSGKyRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 100 ALLETLNVGKpiaNAYNGDVVSAAACI------AWYAEAIDKvyGEVAATAYDMTTLVMREPL-GIVAAVVPWNYPMSMA 172
Cdd:cd07123 113 NAATMLGQGK---NVWQAEIDAACELIdflrfnVKYAEELYA--QQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 173 AWKLGPALaTGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQ 252
Cdd:cd07123 188 NLAGAPAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 253 YSGQS-----NIKRIGLELGGKSPQVVLADCDDLDAAAagiaagifaNT--------GQVCNAGSRLIVDEKIHDQLLEK 319
Cdd:cd07123 267 QIGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVT---------ATvrgafeyqGQKCSAASRAYVPESLWPEVKER 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 320 IAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPVIGGGRVKTETgGFYIEPTIFEGVRNDMKIAQEE 399
Cdd:cd07123 338 LLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSV-GYFVEPTVIETTDPKHKLMTEE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 400 IFGPVLSA--IPVKGFDEAMATANDTV-YGLAGAVWTGSVKNAHRAAKSLR--AGVVWVNCFDRGSL--AVPFGGFKQSG 472
Cdd:cd07123 417 IFGPVLTVyvYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVvgQQPFGGARASG 496
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
151-475 |
8.18e-47 |
|
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: 168.45 E-value: 8.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 151 VMREPLGIVAAVVPWNYPMSMAawkLGP---ALATGNSVILKPAEQSPFTAlKFGELAIEAGMPPGVLNVVPGLGHIAgK 227
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTS-KVIAKIIEETFDEEYVAVVEGGVEEN-Q 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 228 ALgLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVladcddldaaaagiaagifaNTGQVCNAGSRLI 307
Cdd:cd07136 171 EL-LDQKFDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVdedanlklaa-krivwgkflNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 308 VDEKIHDQLLEKIAAQAKVFAPGDPLDTAtRMGSMVSEEQMDRVLGYIDAGRAdgarpVIGGgrvKTETGGFYIEPTIFE 387
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNGKI-----VFGG---NTDRETLYIEPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 388 GVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNcfDR----GSLAV 463
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTimhlANPYL 396
|
330
....*....|..
gi 77389950 464 PFGGFKQSGFGR 475
Cdd:cd07136 397 PFGGVGNSGMGS 408
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
65-475 |
9.21e-46 |
|
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: 165.09 E-value: 9.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 65 RKAFEA---GVWSRMAP--ADRRRILLRFSELILANREEL--ALLEtlNVGKPIANAyngDVVSAAACIAWYAEAIDKVY 137
Cdd:cd07134 1 RRVFAAqqaHALALRAStaAERIAKLKRLKKAILARREEIiaALAA--DFRKPAAEV---DLTEILPVLSEINHAIKHLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 138 G-----EVAATaydMTTL-----VMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELaIE 207
Cdd:cd07134 76 KwmkpkRVRTP---LLLFgtkskIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKI-IR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 208 AGMPPGVLNVVPGLGHIAgKALgLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDDLDAAAAG 287
Cdd:cd07134 152 EAFDEDEVAVFEGDAEVA-QAL-LELPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 288 IAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEK-IAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGARPV 366
Cdd:cd07134 229 AWGKFL-NAGQTCIAPDYVFVHESVKDAFVEHlKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 367 IGGGRVKTETggfYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSL 446
Cdd:cd07134 308 FGGQFDAAQR---YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
410 420 430
....*....|....*....|....*....|....*
gi 77389950 447 RAGVVWVNcfdrGSLA------VPFGGFKQSGFGR 475
Cdd:cd07134 385 SSGGVVVN----DVVLhflnpnLPFGGVNNSGIGS 415
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
6-474 |
1.71e-45 |
|
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: 166.24 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 6 DWHARakavalpnrPFIDGQYVDSlsGETFACIYPGDGRPLT-DVASCNAADVDVAVRSARKAFEagVWSRMAPADRRRI 84
Cdd:TIGR01238 35 TWQAA---------PIIGHSYKAD--GEAQPVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFP--TWNATPAKERAAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 85 LLRFSELILANREELALLETLNVGKPIANAYNgDVVSAAACIAWYAEAIDKVYGEVAAtaydmttlvmrEPLGIVAAVVP 164
Cdd:TIGR01238 102 LDRLADLLELHMPELMALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVRDVLGEFSV-----------ESRGVFVCISP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 165 WNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGST 244
Cdd:TIGR01238 170 WNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGST 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 245 EVGKYFMQYSGQSNIKRIGL--ELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAA 322
Cdd:TIGR01238 250 EVAQLINQTLAQREDAPVPLiaETGGQNAMIV-DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 323 QAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGAR--PVIGGGRVKTETGGFyIEPTIFEgvRNDMKIAQEEI 400
Cdd:TIGR01238 329 AMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKiaQLTLDDSRACQHGTF-VAPTLFE--LDDIAELSEEV 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77389950 401 FGPVLSAIPVKG--FDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNCFDRGSL--AVPFGGFKQSGFG 474
Cdd:TIGR01238 406 FGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVvgVQPFGGQGLSGTG 483
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
55-491 |
3.92e-44 |
|
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: 160.85 E-value: 3.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 55 ADVDVAVRSARKAFEAGvwsRMAPAD-RRRILLRFSELILANREELALLETLNVGKPIANAYNGDVVSAAACIAWYAEAI 133
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEyRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 134 DK------VyGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAawkLGP---ALATGNSVILKPAEQSPFTALKFGEL 204
Cdd:cd07135 82 KKwakdekV-KDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 205 aIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCvgFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPqVVLADCDDLDAA 284
Cdd:cd07135 158 -VPKYLDPDAFQVVQGGVPETTALLEQKFDKIF--YTGSGRVGRIIAEAAAK-HLTPVTLELGGKSP-VIVTKNADLELA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 285 AAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDtATRMGSMVSEEQMDRVLGYIDAGRADgar 364
Cdd:cd07135 233 AKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTTKGK--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 365 PVIGGGRVKTETggfYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAK 444
Cdd:cd07135 309 VVIGGEMDEATR---FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 77389950 445 SLRAG-VVWVNCFDRGSL-AVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07135 386 RTRSGgVVINDTLIHVGVdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
7-474 |
5.19e-43 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 163.57 E-value: 5.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 7 WHARakavalpnrPFIDGQyvdSLSGETFACIYPGDGR-PLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPADRRRIL 85
Cdd:COG4230 556 WQAA---------PLIAGE---AASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAIL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 86 LRFSELILANREEL-ALL--ETlnvGKPIANAyngdvvsaaacIAWYAEAID--KVYGEVAATayDMTTLVMREPLGIVA 160
Cdd:COG4230 622 ERAADLLEAHRAELmALLvrEA---GKTLPDA-----------IAEVREAVDfcRYYAAQARR--LFAAPTVLRGRGVFV 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 161 AVVPWNYPMS-----MAAwklgpALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDV 235
Cdd:COG4230 686 CISPWNFPLAiftgqVAA-----ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRI 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 236 DCVGFTGSTEVGkyfmqysgqsniKRIGLELGGKS-PQVVladcddldaaaagiaagIFANTG--------------QVC 300
Cdd:COG4230 761 AGVAFTGSTETA------------RLINRTLAARDgPIVP-----------------LIAETGgqnamivdssalpeQVV 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 301 ---------NAGSR------LIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGaRP 365
Cdd:COG4230 812 ddvlasafdSAGQRcsalrvLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RL 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 366 VIGGGRVKTETGGFYIEPTIFEgvRNDMKIAQEEIFGPVLSAIPVKG--FDEAMATANDTVYGLAGAVWTGSVKNAHRAA 443
Cdd:COG4230 891 VHQLPLPEECANGTFVAPTLIE--IDSISDLEREVFGPVLHVVRYKAdeLDKVIDAINATGYGLTLGVHSRIDETIDRVA 968
|
490 500 510
....*....|....*....|....*....|....*...
gi 77389950 444 KSLRAGVVWVNcfdR---GslAV----PFGGFKQSGFG 474
Cdd:COG4230 969 ARARVGNVYVN---RniiG--AVvgvqPFGGEGLSGTG 1001
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
151-491 |
2.82e-42 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 157.11 E-value: 2.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 151 VMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELaIEAGMPPGVLNVVPGLGHIAGKALG 230
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVIEGGVEVTTELLK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 231 LHMDVdcVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVlADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDE 310
Cdd:PTZ00381 184 EPFDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIV-DKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 311 KIHDQLLEKIAAQAKVFAPGDPLdTATRMGSMVSEEQMDRVLGYIDAGRADgarpVIGGGRVKTETGgfYIEPTIFEGVR 390
Cdd:PTZ00381 260 SIKDKFIEALKEAIKEFFGEDPK-KSEDYSRIVNEFHTKRLAELIKDHGGK----VVYGGEVDIENK--YVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 391 NDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVN--CFDRGSLAVPFGGF 468
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGV 412
|
330 340
....*....|....*....|...
gi 77389950 469 KQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPV 435
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
2-474 |
1.62e-40 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 156.18 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 2 LQEIDWHARakavalpnrPFIDGqyvDSLSGETFACIYPGDGRPLT-DVASCNAADVDVAVRSARKAFEAgvWSRMAPAD 80
Cdd:PRK11905 548 FAAKTWHAA---------PLLAG---GDVDGGTRPVLNPADHDDVVgTVTEASAEDVERALAAAQAAFPE--WSATPAAE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 81 RRRILLRFSELILANREELALLETLNVGKPIANAyngdvvsaaacIAWYAEAID--KVYGEVAATAYDMTTlvmREPLGI 158
Cdd:PRK11905 614 RAAILERAADLMEAHMPELFALAVREAGKTLANA-----------IAEVREAVDflRYYAAQARRLLNGPG---HKPLGP 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 159 VAAVVPWNYPMSM-----AAwklgpALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHM 233
Cdd:PRK11905 680 VVCISPWNFPLAIftgqiAA-----ALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADP 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 234 DVDCVGFTGSTEVGKYF---MQYSGQSNIKRIGlELGGKSP----------QVVladcddldaaaAGIAAGIFANTGQVC 300
Cdd:PRK11905 755 RIAGVMFTGSTEVARLIqrtLAKRSGPPVPLIA-ETGGQNAmivdssalpeQVV-----------ADVIASAFDSAGQRC 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 301 NAGSRLIVDEKIHDQLLEKIA---AQAKVfapGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGaRPVIGGGRVKTETG 377
Cdd:PRK11905 823 SALRVLCLQEDVADRVLTMLKgamDELRI---GDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAG-RLVHQLPLPAETEK 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 378 GFYIEPTIFE-GVRNDMKiaqEEIFGPVLSAIPVK--GFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVN 454
Cdd:PRK11905 899 GTFVAPTLIEiDSISDLE---REVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
490 500
....*....|....*....|....*
gi 77389950 455 cfdRGSL-AV----PFGGFKQSGFG 474
Cdd:PRK11905 976 ---RNIIgAVvgvqPFGGEGLSGTG 997
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1-474 |
3.06e-40 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 155.36 E-value: 3.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 1 MLQEIDWHARAKAVAlpnRPFIDGqyvdslSGETFACIYPGDGR-PLTDVASCNAADVDVAVRSARKAFEAgvWSRMAPA 79
Cdd:PRK11904 539 LAAAIAAFLEKQWQA---GPIING------EGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPA--WSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 80 DRRRILLRFSELILANREELALLETLNVGKPIANayngdvvsaaaCIAWYAEAID--KVYGEVAATAYDMTTL------- 150
Cdd:PRK11904 608 ERAAILERAADLLEANRAELIALCVREAGKTLQD-----------AIAEVREAVDfcRYYAAQARRLFGAPEKlpgptge 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 151 ---VMREPLGIVAAVVPWNYPMsmaAWKLGP---ALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHI 224
Cdd:PRK11904 677 sneLRLHGRGVFVCISPWNFPL---AIFLGQvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGAT 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 225 AGKALGLHMDVDCVGFTGSTEVGKYfmqysgqsnIKR---------IGL--ELGGKS---------P-QVVladcddlda 283
Cdd:PRK11904 754 VGAALTADPRIAGVAFTGSTETARI---------INRtlaardgpiVPLiaETGGQNamivdstalPeQVV--------- 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 284 aaAGIAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADgA 363
Cdd:PRK11904 816 --DDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-A 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 364 RPVIGGGRVKTETGGFYIEPTIFEgvRNDMKIAQEEIFGPVLSAIPVK--GFDEAMATANDTVYGLAGAVWTGSVKNAHR 441
Cdd:PRK11904 893 RLLAQLPLPAGTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADR 970
|
490 500 510
....*....|....*....|....*....|....*...
gi 77389950 442 AAKSLRAGVVWVNcfdRGSL-AV----PFGGFKQSGFG 474
Cdd:PRK11904 971 IADRVRVGNVYVN---RNQIgAVvgvqPFGGQGLSGTG 1005
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
61-491 |
6.46e-39 |
|
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: 146.40 E-value: 6.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 61 VRSARKAFEAGvwsRMAPADRRRILLRfSELILANREELALLETL--NVGKPIANAYNGDV-VSAAACIA-------WYA 130
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLK-GLLRLVDENEDDIFAALrqDLGKPSAESFRDEVsVLVSSCKLaikelkkWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 131 EaiDKVYGEVaaTAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELaIEAGM 210
Cdd:cd07137 81 P--EKVKTPL--TTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 211 PPGVLNVVPGlGHIAGKALgLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAA 290
Cdd:cd07137 156 DTKAIKVIEG-GVPETTAL-LEQKWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 291 GIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATrMGSMVSEEQMDRVLGYIDAGRAdgARPVIGGG 370
Cdd:cd07137 233 KWGCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKD-LSRIVNSHHFQRLSRLLDDPSV--ADKIVHGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 371 RVKTETggFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGV 450
Cdd:cd07137 310 ERDEKN--LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 77389950 451 VWVN--CFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07137 388 VTFNdtVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
151-475 |
2.29e-37 |
|
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: 142.24 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 151 VMREPLGIVAAVVPWNYPMSMAawkLGP---ALATGNSVILKPAEQSPFTALKFGELaIEAGMPPGVLNVVPGlGHIAGK 227
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDEVAVVTG-GADVAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 228 ALGlHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPqVVLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLI 307
Cdd:cd07133 172 AFS-SLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSP-AIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 308 VDEKIHDQLLEKIAAQAKVFAP---GDPLDTatrmgSMVSEEQMDRVLGYIDAGRADGAR--PVIGGGRVKTETGgfYIE 382
Cdd:cd07133 249 VPEDKLEEFVAAAKAAVAKMYPtlaDNPDYT-----SIINERHYARLQGLLEDARAKGARviELNPAGEDFAATR--KLP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 383 PTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNcfdrGSL- 461
Cdd:cd07133 322 PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN----DTLl 397
|
330
....*....|....*....
gi 77389950 462 -----AVPFGGFKQSGFGR 475
Cdd:cd07133 398 hvaqdDLPFGGVGASGMGA 416
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
60-491 |
2.95e-36 |
|
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: 139.28 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 60 AVRSARKAFEAGvwsRMAPAD-RRRILLRFSELILANREEL--ALLETLNvgKPIANAY-------NGDVVSAAACI-AW 128
Cdd:cd07132 3 AVRRAREAFSSG---KTRPLEfRIQQLEALLRMLEENEDEIveALAKDLR--KPKFEAVlseillvKNEIKYAISNLpEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 129 YA-EAIDKVYgevaATAYDmTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTAlKFGELAIE 207
Cdd:cd07132 78 MKpEPVKKNL----ATLLD-DVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA-KLLAELIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 208 AGMPPGVLNVVpgLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPqVVLADCDDLDAAAAG 287
Cdd:cd07132 152 KYLDKECYPVV--LGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSP-CYVDKSCDIDVAARR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 288 IAAGIFANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTAtRMGSMVSEEQMDRVLGYIDAGRadgarPVI 367
Cdd:cd07132 228 IAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLLSGGK-----VAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 368 GGGRVKTETggfYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLR 447
Cdd:cd07132 302 GGQTDEKER---YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTS 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 77389950 448 AGVVWVN-CFDRGSLAV-PFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:cd07132 379 SGGVCVNdTIMHYTLDSlPFGGVGNSGMGAYHGKYSFDTFSHKRSC 424
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
20-474 |
5.24e-35 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 139.72 E-value: 5.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 20 PFIDGQYVDslsGETFACIYPGDGRPLTD-VASCNAADVDVAVRSARKAfeAGVWSRMAPADRRRILLRFSELILANREE 98
Cdd:PRK11809 649 PMLEDPVAA---GEMSPVINPADPRDIVGyVREATPAEVEQALESAVNA--APIWFATPPAERAAILERAADLMEAQMQT 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 99 LALLETLNVGKPIANAyngdvvsaaacIAWYAEAID--KVYGEVAATAYDMTTlvmREPLGIVAAVVPWNYPMSMAAWKL 176
Cdd:PRK11809 724 LMGLLVREAGKTFSNA-----------IAEVREAVDflRYYAGQVRDDFDNDT---HRPLGPVVCISPWNFPLAIFTGQV 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 177 GPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFmqysgQ 256
Cdd:PRK11809 790 AAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLL-----Q 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 257 SNI--------KRIGL--ELGGK----------SPQVVladcddldaaaAGIAAGIFANTGQVCNAGSRLIVDEKIHDQL 316
Cdd:PRK11809 865 RNLagrldpqgRPIPLiaETGGQnamivdssalTEQVV-----------ADVLASAFDSAGQRCSALRVLCLQDDVADRT 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 317 LEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADGaRPVIGGGRVKTETG--GFYIEPTIFEgvRNDMK 394
Cdd:PRK11809 934 LKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKG-RPVFQAARENSEDWqsGTFVPPTLIE--LDSFD 1010
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 395 IAQEEIFGPVLSAI--PVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVNcfdRGSL-AV----PFGG 467
Cdd:PRK11809 1011 ELKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN---RNMVgAVvgvqPFGG 1087
|
....*..
gi 77389950 468 FKQSGFG 474
Cdd:PRK11809 1088 EGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
61-491 |
7.27e-34 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 133.31 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 61 VRSARKAFEAGvwsRMAPADRRRILLR-FSELILANREEL--ALLETLnvGKPIANAYNGDVVSAAACIAWYAEAIDK-- 135
Cdd:PLN02203 12 VAELRETYESG---RTRSLEWRKSQLKgLLRLLKDNEEAIfkALHQDL--GKHRVEAYRDEVGVLTKSANLALSNLKKwm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 136 --VYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTAlKFGELAIEAGMPPG 213
Cdd:PLN02203 87 apKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-AFLAANIPKYLDSK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 214 VLNVVPGlGHIAGKALgLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIF 293
Cdd:PLN02203 166 AVKVIEG-GPAVGEQL-LQHKWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVDSLSSSRDTKVAVNRIVGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 294 ---ANTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATrMGSMVSEEQMDRVLGYIDAGRAdgARPVIGGG 370
Cdd:PLN02203 243 kwgSCAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRV--AASIVHGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 371 RVKTETggFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGV 450
Cdd:PLN02203 320 SIDEKK--LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGS 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 77389950 451 VWVN--CFDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAV 491
Cdd:PLN02203 398 VTFNdaIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
31-476 |
4.91e-32 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 128.41 E-value: 4.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 31 SGETFACIYPGDGRPLTDVASCNAADVDVAVRSARKAfeAGVWSRMAPADRRRILLRFSELILANREELALLETLNVGKP 110
Cdd:PLN02315 32 NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEA--AKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 111 IANAYnGDVVSAAACIAWYAEAIDKVYGEVAATAY-DMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILK 189
Cdd:PLN02315 110 LAEGI-GEVQEIIDMCDFAVGLSRQLNGSIIPSERpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 190 PAEQSPFTALKFGELAIEA----GMPPGVLNVVPGLGHIaGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSNIKRIgLE 265
Cdd:PLN02315 189 GAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCGGAEI-GEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCL-LE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 266 LGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSE 345
Cdd:PLN02315 267 LSGNNAIIVMDDADIQLAVRSVLFAAVG-TAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 346 EQMDRVLGYIDAGRADGARPVIGGGRVktETGGFYIEPTIFEgVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVY 425
Cdd:PLN02315 346 ESKKNFEKGIEIIKSQGGKILTGGSAI--ESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQ 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 77389950 426 GLAGAVWTGSVKNAHR--AAKSLRAGVVWVNCFDRGS-LAVPFGGFKQSGFGRD 476
Cdd:PLN02315 423 GLSSSIFTRNPETIFKwiGPLGSDCGIVNVNIPTNGAeIGGAFGGEKATGGGRE 476
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
138-493 |
8.44e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 115.91 E-value: 8.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 138 GEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELaIEAGMPPGVLNV 217
Cdd:PLN02174 95 AKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 218 VPGLghIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANTG 297
Cdd:PLN02174 174 VEGA--VTETTALLEQKWDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCNNG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 298 QVCNAGSRLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTATrMGSMVSEEQMDRVLGYIDagRADGARPVIGGGRVKTETg 377
Cdd:PLN02174 251 QACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKD-MSRIVNSTHFDRLSKLLD--EKEVSDKIVYGGEKDREN- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 378 gFYIEPTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAAKSLRAGVVWVN--C 455
Cdd:PLN02174 327 -LKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiA 405
|
330 340 350
....*....|....*....|....*....|....*...
gi 77389950 456 FDRGSLAVPFGGFKQSGFGRDKSLHAMDKYTDLKAVWF 493
Cdd:PLN02174 406 VHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLY 443
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
60-463 |
1.62e-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: 108.86 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 60 AVRSARKAfeAGVWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYN--GDVV--SAAACIAwYAEAIDK 135
Cdd:cd07084 4 ALLAADIS--TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENicGDQVqlRARAFVI-YSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 136 VYGEVAATAYDMTTLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAG-MPPGV 214
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 215 LNVVPGLGHiAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSnikRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFA 294
Cdd:cd07084 161 VTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 295 NTGQVCNAGSRLIVDEKIHDQ-LLEKIAAQAKVFAPGDpldtatrmgSMVSEEQMDRVLGYIDAGRADGARPVIGGGRV- 372
Cdd:cd07084 237 CSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED---------LLLGPVQTFTTLAMIAHMENLLGSVLLFSGKEl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 373 ----KTETGGFYIEPTIF---EGVRNDMKIAQEEIFGPVLSAIPVKgfDEAMATANDTVYGLAGAVWTGSVKN-----AH 440
Cdd:cd07084 308 knhsIPSIYGACVASALFvpiDEILKTYELVTEEIFGPFAIVVEYK--KDQLALVLELLERMHGSLTAAIYSNdpiflQE 385
|
410 420
....*....|....*....|...
gi 77389950 441 RAAKSLRAGVVWVNCFDRGSLAV 463
Cdd:cd07084 386 LIGNLWVAGRTYAILRGRTGVAP 408
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
16-420 |
1.86e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 88.22 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 16 LPNrpFIDGQYVDSlSGETFACIYPGDGRPLTDVASCN---AADVDVAVRSARKAFEAgvwsrMAPADRRRILLRFSELI 92
Cdd:PRK11903 5 LAN--YVAGRWQAG-SGAGTPLFDPVTGEELVRVSATGldlAAAFAFAREQGGAALRA-----LTYAQRAALLAAIVKVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 93 LANREELALLETLNVGKpIANAYNGDVVSAAACIAWYAEAIDKVyGEVAATAYDMTTLVMREPL-----------GIVAA 161
Cdd:PRK11903 77 QANRDAYYDIATANSGT-TRNDSAVDIDGGIFTLGYYAKLGAAL-GDARLLRDGEAVQLGKDPAfqgqhvlvptrGVALF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 162 VVPWNYPmsmaAW----KLGPALATGNSVILKPAEQSPFTALKFGELAIEAG-MPPGVLNVVpglghiAGKALGLhMD-- 234
Cdd:PRK11903 155 INAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVV------CGSSAGL-LDhl 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 235 --VDCVGFTGSTEVGKY------FMQYSGQSNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRL 306
Cdd:PRK11903 224 qpFDVVSFTGSAETAAVlrshpaVVQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTV-KSGQKCTAIRRI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 307 IVDEKIHDQLLEKIAAQAKVFAPGDPLDTATRMGSMVSEEQMDRVLGYIDAGRAdGARPVIGGGRVKT----ETGGFYIE 382
Cdd:PRK11903 303 FVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRA-QAEVLFDGGGFALvdadPAVAACVG 381
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 77389950 383 PTIF--EGVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATA 420
Cdd:PRK11903 382 PTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
166-443 |
3.71e-14 |
|
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: 74.61 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 166 NYPmsmaAW----KLGPALATGNSVILKPAEQSPFTALKFGELAIEAG-MPPGVLNVVPG-----LGHIAGKalglhmdv 235
Cdd:cd07128 155 NFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGsvgdlLDHLGEQ-------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 236 DCVGFTGSTEVGKY------FMQYSGQSNIKRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFaNTGQVCNAGSRLIVD 309
Cdd:cd07128 223 DVVAFTGSAATAAKlrahpnIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTV-KAGQKCTAIRRAFVP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 310 EKIHDQLLEKIAAQ-AKVFApGDPLDTATRMGSMVSEEQMDRVLGYIDAGRADgARPVIGGGRVKTETG-----GFYIEP 383
Cdd:cd07128 302 EARVDAVIEALKARlAKVVV-GDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGPDRFEVVGadaekGAFFPP 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77389950 384 TIFEGvRNDMKIA---QEEIFGPVLSAIPVKGFDEAMATANDTVYGLAGAVWTGSVKNAHRAA 443
Cdd:cd07128 380 TLLLC-DDPDAATavhDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
57-248 |
1.78e-11 |
|
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: 66.03 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 57 VDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREEL---ALLETlnvGKPIANAyNGDVVS--------AAAC 125
Cdd:cd07129 1 VDAAAAAAAAAFES--YRALSPARRAAFLEAIADEIEALGDELvarAHAET---GLPEARL-QGELGRttgqlrlfADLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 126 IA--WYAEAIDKVYGEVA-ATAYDMTTlvMREPLGIVAAVVPWNYPM--SMAAWKLGPALATGNSVILKPAEQSPFTALK 200
Cdd:cd07129 75 REgsWLDARIDPADPDRQpLPRPDLRR--MLVPLGPVAVFGASNFPLafSVAGGDTASALAAGCPVVVKAHPAHPGTSEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 77389950 201 FGELAIEA----GMPPGVLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGK 248
Cdd:cd07129 153 VARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGR 204
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
55-424 |
1.20e-09 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 60.57 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 55 ADVDVAVRSARKAFEAgvWSRMAPADRRRILLRFSELILANREELALLETLNVGKPIANAYNGDVVSAAAC----IAWYA 130
Cdd:cd07127 84 CDPDALLAAARAAMPG--WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQAGGPHAQDRgleaVAYAW 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 131 EAIDKV---------YGEVAATAYDMTTLVMREPLGIVAAVVP---WN-YPMSMAAwklgpaLATGNSVILKPaeqSPFT 197
Cdd:cd07127 162 REMSRIpptaewekpQGKHDPLAMEKTFTVVPRGVALVIGCSTfptWNgYPGLFAS------LATGNPVIVKP---HPAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 198 ALKFG-------ELAIEAGMPPG-VLNVVPGLGHIAGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQsniKRIGLELGGK 269
Cdd:cd07127 233 ILPLAitvqvarEVLAEAGFDPNlVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 270 SpQVVLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIV---------DEKIHDQLLEKIAAQAKVFApGDPLDTATRMG 340
Cdd:cd07127 310 N-TVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAADLAAAIDGLL-ADPARAAALLG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 341 SMVSEEQMDRV-----LGYIDAGRADGARPVIGGGRVKTetggfyiePTIFEGVRNDMKIAQEEIFGPVLSAIPVKGFDE 415
Cdd:cd07127 388 AIQSPDTLARIaearqLGEVLLASEAVAHPEFPDARVRT--------PLLLKLDASDEAAYAEERFGPIAFVVATDSTDH 459
|
....*....
gi 77389950 416 AMATANDTV 424
Cdd:cd07127 460 SIELARESV 468
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
149-420 |
9.58e-08 |
|
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: 54.19 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 149 TLVMREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKP---AEQSPFTALK-FGELAIEAGMPPGVLNVVPGLGHI 224
Cdd:cd07081 89 TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKVTQRAATlLLQAAVAAGAPENLIGWIDNPSIE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 225 AGKALGLHMDVDCVGFTGSTEVGKyfmqySGQSNIKRIgLELGGKSPQVVLADCDDLDAAAAGIAAGIFANTGQVCNAGS 304
Cdd:cd07081 169 LAQRLMKFPGIGLLLATGGPAVVK-----AAYSSGKPA-IGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 305 RLIVDEKIHDQLLEKIAAQAKVFAPGDPLDTAtrmgsmvseeqMDRVLGYIDAGRADGARPV-----IGGGRVKTETGGF 379
Cdd:cd07081 243 SVIVVDSVYDEVMRLFEGQGAYKLTAEELQQV-----------QPVILKNGDVNRDIVGQDAykiaaAAGLKVPQETRIL 311
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 77389950 380 YIEPTifegVRNDMKIAQEEIFGPVLSAIPVKGFDEAMATA 420
Cdd:cd07081 312 IGEVT----SLAEHEPFAHEKLSPVLAMYRAANFADADAKA 348
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
152-403 |
1.10e-06 |
|
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: 50.96 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 152 MREPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKPAEQSPFTALKFGELAIEAGMPPGVLNVVPGLGHIAGKALgL 231
Cdd:cd07126 139 YRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL-L 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 232 HMDVDCVGFTGSTEVG-KYFMQYSGqsnikRIGLELGGKSPQVVLADCDDLDAAAAGIAAGIFANTGQVCNAGSRLIVDE 310
Cdd:cd07126 218 EANPRMTLFTGSSKVAeRLALELHG-----KVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 311 KIHDQ-LLEKIAAQAKVFAPGD----PLDTAT--RMgsmvsEEQMDRVLGYIDAGRADGARPVIGGGrvKTETGGFYiEP 383
Cdd:cd07126 293 NWVQAgILDKLKALAEQRKLEDltigPVLTWTteRI-----LDHVDKLLAIPGAKVLFGGKPLTNHS--IPSIYGAY-EP 364
|
250 260
....*....|....*....|....*.
gi 77389950 384 T-IF---EGVRN--DMKIAQEEIFGP 403
Cdd:cd07126 365 TaVFvplEEIAIeeNFELVTTEVFGP 390
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
154-243 |
1.17e-05 |
|
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: 47.49 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 154 EPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKP---AEQSPFTALKF-GELAIEAGMPPGVLNVVPGLGHIAGKAL 229
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90
....*....|....
gi 77389950 230 GLHMDVDCVGFTGS 243
Cdd:cd07122 174 MKHPDVDLILATGG 187
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
149-326 |
1.45e-05 |
|
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: 47.22 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 149 TLVMREPLGIVAAVVPWNYPMSmAAWKLGPALATGNSVILKPAEQSPFT----ALKFGElAIEAGMPPGVLNVVPGLGHI 224
Cdd:cd07077 94 TYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTnralALLFQA-ADAAHGPKILVLYVPHPSDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 225 AGKALGLHMDVDCVGFTGSTEVGKYFMQYSGQSNIKRIGlelGGKSPQVVLADCDDLDAAAAGIAAGIFANTgqVCNAGS 304
Cdd:cd07077 172 LAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFG---AGNSPVVVDETADEERASGSVHDSKFFDQN--ACASEQ 246
|
170 180
....*....|....*....|..
gi 77389950 305 RLIVDEKIHDQLLEKIAAQAKV 326
Cdd:cd07077 247 NLYVVDDVLDPLYEEFKLKLVV 268
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
154-242 |
1.82e-04 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 44.02 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77389950 154 EPLGIVAAVVPWNYPMSMAAWKLGPALATGNSVILKP---AEQSPFTALKF-GELAIEAGMPPGVLNVVPGLGHIAGKAL 229
Cdd:PRK13805 107 EPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFhprAQKSSIAAAKIvLDAAVAAGAPKDIIQWIEEPSVELTNAL 186
|
90
....*....|...
gi 77389950 230 GLHMDVDCVGFTG 242
Cdd:PRK13805 187 MNHPGIALILATG 199
|
|
| |
