|
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: 792.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 32 GATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPV 111
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 112 MDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPA 191
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 192 EQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSNLKQVWLECGGKSP 271
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 272 NLVFADCRDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGI 351
Cdd:cd07112 241 NIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 352 LAAIERAQGEGATLLGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASL 431
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489174509 432 WSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKTTW 492
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTW 461
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
19-495 |
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: 601.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 19 QALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFdeGPWARLAPVERKRVLLRLAELMLAHREE 98
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 99 LALLDSLNMGKPVMDAWnIDVPGAAHVFAWYAESLDKLYDQVAPTAQQ-ALATITRVPLGVIGAVVPWNFPLDMAAWKLA 177
Cdd:COG1012 85 LAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPgTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 178 PALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQs 257
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 258 NLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPAS 337
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDA-DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 338 RAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGsDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAI 417
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEG-GYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489174509 418 RLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVA-VPFGGGKQSGFGRDLSLHSFDKYTQLKTTWFQL 495
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
4-495 |
0e+00 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 575.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 4 LSDWQRRAATQRFIDQALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKR 83
Cdd:PRK09847 6 LAYWQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 84 VLLRLAELMLAHREELALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVV 163
Cdd:PRK09847 86 VLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 164 PWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGS 243
Cdd:PRK09847 166 PWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 244 TEVGKYFMQYSAQSNLKQVWLECGGKSPNLVFADCRDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAK 323
Cdd:PRK09847 246 TRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 324 ARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGaTLLGGGRQltiNGSDNFIEPTLFGDVRPDMQLAREEIFGP 403
Cdd:PRK09847 326 AQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRN---AGLAAAIGPTIFVDVDPNASLSREEIFGP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 404 VLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFD 483
Cdd:PRK09847 402 VLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALE 481
|
490
....*....|..
gi 489174509 484 KYTQLKTTWFQL 495
Cdd:PRK09847 482 KFTELKTIWISL 493
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
19-490 |
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: 574.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 19 QALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVLLRLAELMLAHREE 98
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 99 LALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAP 178
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 179 ALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSN 258
Cdd:cd07091 165 ALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 259 LKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASR 338
Cdd:cd07091 245 LKKVTLELGGKSPNIVFDDA-DLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 339 AGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGsdNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIR 418
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKG--YFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489174509 419 LANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKA 473
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
29-490 |
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: 559.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 29 AASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELALLDSLNMG 108
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 109 KPVMDAWnIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVL 188
Cdd:pfam00171 81 KPLAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 189 KPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGG 268
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 269 KSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQT 348
Cdd:pfam00171 239 KNPLIVLEDA-DLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 349 AGILAAIERAQGEGATLLGGGRQLTINGsdNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLA 428
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAGLDNG--YFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489174509 429 ASLWSDDLHRAHRVARRLNAGTVSVNTVDALDV-AVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
39-495 |
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: 527.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 39 DPASNRLLARVAACDAADVDAAVAAARRAFDegPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNID 118
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 119 VPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSA 198
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 199 LRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADC 278
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQ-GAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 279 rDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERA 358
Cdd:cd07115 240 -DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 359 QGEGATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHR 438
Cdd:cd07115 319 REEGARLLTGGKRPGARGF--FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489174509 439 AHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKTTWFQL 495
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
73-493 |
0e+00 |
|
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: 522.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLY-DQVAPTAQQALATI 151
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA-LGEVARAADTFRYYAGLARRLHgEVIPSPDPGELAIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGL 231
Cdd:cd07078 93 RREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERS 311
Cdd:cd07078 173 HPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDA-DLDAAVKGAVFGAFGNAGQVCTAASRLLVHES 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 IHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLL-GGGRQLTINGsdNFIEPTLFGDVR 390
Cdd:cd07078 251 IYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLcGGKRLEGGKG--YFVPPTVLTDVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 391 PDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVA-VPFGGGK 469
Cdd:cd07078 329 PDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPsAPFGGVK 408
|
410 420
....*....|....*....|....
gi 489174509 470 QSGFGRDLSLHSFDKYTQLKTTWF 493
Cdd:cd07078 409 QSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
73-491 |
0e+00 |
|
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: 516.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATIT 152
Cdd:cd07093 35 WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 153 RVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLH 232
Cdd:cd07093 115 RQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 233 PEVDALVFTGSTEVGKYFMQYSAqSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSI 312
Cdd:cd07093 195 PDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPNIVFADA-DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 313 HDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGR--QLTINGSDNFIEPTLFGDVR 390
Cdd:cd07093 273 YDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGrpELPDLEGGYFVEPTVITGLD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 391 PDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQ 470
Cdd:cd07093 353 NDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKA 432
|
410 420
....*....|....*....|.
gi 489174509 471 SGFGRDLSLHSFDKYTQLKTT 491
Cdd:cd07093 433 SGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
22-495 |
1.21e-178 |
|
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: 509.93 E-value: 1.21e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVLLRLAELMLAHREELAL 101
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 102 LDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALA 181
Cdd:cd07119 82 LETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 182 AGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQySAQSNLKQ 261
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMR-AAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 262 VWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGA 341
Cdd:cd07119 240 VALELGGKNPNIVFADA-DFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 342 IVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDN--FIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRL 419
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489174509 420 ANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKTTWFQL 495
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
19-489 |
9.17e-175 |
|
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: 500.10 E-value: 9.17e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 19 QALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVLLRLAELMLAHREE 98
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 99 LALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAP 178
Cdd:cd07142 85 LAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 179 ALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSN 258
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 259 LKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASR 338
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 339 AGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIR 418
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY--YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489174509 419 LANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
68-493 |
2.35e-173 |
|
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: 495.53 E-value: 2.35e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 68 FDEGPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPV--MDAwniDVPGAAHVFAWYAESLDKLYDQVAPTAQ 145
Cdd:cd07114 32 FEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIreTRA---QVRYLAEWYRYYAGLADKIEGAVIPVDK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 146 Q-ALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQ 224
Cdd:cd07114 109 GdYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 225 AGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANS 304
Cdd:cd07114 189 TGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFDDA-DLDAAVNGVVAGIFAAAGQTCVAGS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 305 RLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDN--FIE 382
Cdd:cd07114 267 RLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLGAgyFFE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 383 PTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVA 462
Cdd:cd07114 347 PTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPS 426
|
410 420 430
....*....|....*....|....*....|.
gi 489174509 463 VPFGGGKQSGFGRDLSLHSFDKYTQLKTTWF 493
Cdd:cd07114 427 SPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
22-490 |
1.58e-170 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 490.10 E-value: 1.58e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVLLRLAELMLAHREELAL 101
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 102 LDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALA 181
Cdd:PLN02766 105 LDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 182 AGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSNLKQ 261
Cdd:PLN02766 185 AGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 262 VWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGA 341
Cdd:PLN02766 265 VSLELGGKSPLLIFDDA-DVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 342 IVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLAN 421
Cdd:PLN02766 344 QVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGY--YIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKAN 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489174509 422 DSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:PLN02766 422 NTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKS 490
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
28-495 |
7.00e-170 |
|
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: 487.69 E-value: 7.00e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 28 PAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFdEGPWARLAPVERKRVLLRLAELMLAHREELALLDSLNM 107
Cdd:cd07144 18 KSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAF-ESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 108 GKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVV 187
Cdd:cd07144 97 GKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 188 LKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECG 267
Cdd:cd07144 177 IKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ-NLKAVTLECG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 268 GKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKAR-DWQPGDPLDPASRAGAIVDRR 346
Cdd:cd07144 256 GKSPALVFEDA-DLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 347 QTAGILAAIERAQGEGATL-LGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRY 425
Cdd:cd07144 335 QYDRVLSYIEKGKKEGAKLvYGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTY 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 426 GLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKTTWFQL 495
Cdd:cd07144 415 GLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
29-490 |
7.43e-165 |
|
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: 474.91 E-value: 7.43e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 29 AASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEG-PWARLAPVERKRVLLRLAELMLAHREELALLDSLNM 107
Cdd:cd07141 18 SVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 108 GKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALaTITRV-PLGVIGAVVPWNFPLDMAAWKLAPALAAGNSV 186
Cdd:cd07141 98 GKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFF-TYTRHePVGVCGQIIPWNFPLLMAAWKLAPALACGNTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 187 VLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSNLKQVWLEC 266
Cdd:cd07141 177 VLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRVTLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 267 GGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRR 346
Cdd:cd07141 257 GGKSPNIVFADA-DLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 347 QTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYG 426
Cdd:cd07141 336 QFKKILELIESGKKEGAKLECGGKRHGDKGY--FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYG 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489174509 427 LAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07141 414 LAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
70-490 |
5.89e-162 |
|
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: 466.33 E-value: 5.89e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 70 EGPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNiDVPGAAHVFAWYAESLDKLYDQVAPTAQQALA 149
Cdd:cd07109 33 ESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA-DVEAAARYFEYYGGAADKLHGETIPLGPGYFV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 150 TITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKAL 229
Cdd:cd07109 112 YTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 230 GLHPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVE 309
Cdd:cd07109 192 VAHPGVDHISFTGSVETGIAVMR-AAAENVVPVTLELGGKSPQIVFADA-DLEAALPVVVNAIIQNAGQTCSAGSRLLVH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 310 RSIHDEFVERLLAKARDWQPGDPLDPASrAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDN-FIEPTLFGD 388
Cdd:cd07109 270 RSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGAPAGGyFVAPTLLDD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 389 VRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTV-DALDVAVPFGG 467
Cdd:cd07109 349 VPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYgAGGGIELPFGG 428
|
410 420
....*....|....*....|...
gi 489174509 468 GKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07109 429 VKKSGHGREKGLEALYNYTQTKT 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
21-489 |
6.47e-161 |
|
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: 464.89 E-value: 6.47e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 21 LIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELA 100
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 101 LLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPAL 180
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 181 AAGNSVVLKPAEQSPFSALRLAELALEAgVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLK 260
Cdd:cd07559 162 AAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 261 QVWLECGGKSPNLVFAD----CRDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPA 336
Cdd:cd07559 240 PVTLELGGKSPNIFFDDamdaDDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 337 SRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDN--FIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSED 414
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489174509 415 EAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07559 400 EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
68-491 |
1.53e-159 |
|
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: 460.27 E-value: 1.53e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 68 FDEGPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNiDVPGAAHVFAwYAESLDKL-----YDQVAP 142
Cdd:cd07118 32 FDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EIEGAADLWR-YAASLARTlhgdsYNNLGD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 143 taqQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLG 222
Cdd:cd07118 110 ---DMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 223 EQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSA 302
Cdd:cd07118 187 ATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADA-DLDAAADAVVFGVYFNAGECCNS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 303 NSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTiNGSDNFIE 382
Cdd:cd07118 265 GSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLA-SAAGLFYQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 383 PTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVA 462
Cdd:cd07118 344 PTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPE 423
|
410 420
....*....|....*....|....*....
gi 489174509 463 VPFGGGKQSGFGRDLSLHSFDKYTQLKTT 491
Cdd:cd07118 424 LPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
73-490 |
5.16e-156 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 451.12 E-value: 5.16e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAPT-AQQALATI 151
Cdd:cd07103 35 WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGL 231
Cdd:cd07103 114 IKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFMQYSAqSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERS 311
Cdd:cd07103 194 SPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVFDDA-DLDKAVDGAIASKFRNAGQTCVCANRIYVHES 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 IHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGsdNFIEPTLFGDVRP 391
Cdd:cd07103 272 IYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRLGLGG--YFYEPTVLTDVTD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 392 DMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQS 471
Cdd:cd07103 350 DMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKES 429
|
410
....*....|....*....
gi 489174509 472 GFGRDLSLHSFDKYTQLKT 490
Cdd:cd07103 430 GLGREGGKEGLEEYLETKY 448
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-489 |
3.18e-154 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 450.03 E-value: 3.18e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 19 QALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVLLRLAELMLAHREE 98
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 99 LALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAP 178
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 179 ALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSN 258
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 259 LKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASR 338
Cdd:PLN02466 299 LKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 339 AGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIR 418
Cdd:PLN02466 378 QGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY--YIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489174509 419 LANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:PLN02466 456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-490 |
3.68e-153 |
|
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: 444.71 E-value: 3.68e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVLLRLAELMLAHREELAL 101
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 102 LDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKL-YDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPAL 180
Cdd:cd07139 83 LWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 181 AAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGlGEQAGKALGLHPEVDALVFTGSTEVGKYFMQySAQSNLK 260
Cdd:cd07139 163 AAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAA-VCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 261 QVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAG 340
Cdd:cd07139 241 RVTLELGGKSAAIVLDDA-DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 341 AIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLA 420
Cdd:cd07139 320 PLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 421 NDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVdALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07139 400 NDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKS 468
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-495 |
3.74e-152 |
|
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: 442.74 E-value: 3.74e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFdEGPWAR-LAPVERKRVLLRLAELMLAHREELA 100
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAF-ETDWGLkVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 101 LLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPAL 180
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 181 AAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSNLK 260
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 261 QVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAG 340
Cdd:cd07143 250 KVTLELGGKSPNIVFDDA-DLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 341 AIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLA 420
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY--FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489174509 421 NDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKTTWFQL 495
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
68-490 |
3.80e-152 |
|
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: 441.68 E-value: 3.80e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 68 FDEGPWARlAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQV-----AP 142
Cdd:cd07089 32 FDTGDWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWEFdlpvpAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 143 TAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLG 222
Cdd:cd07089 111 RGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 223 EQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSA 302
Cdd:cd07089 191 NAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSANIVLDDA-DLAAAAPAAVGVCMHNAGQGCAL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 303 NSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLL-GGGRQLtinGSDN-- 379
Cdd:cd07089 269 TTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVtGGGRPA---GLDKgf 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 380 FIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDAL 459
Cdd:cd07089 346 YVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGY 425
|
410 420 430
....*....|....*....|....*....|.
gi 489174509 460 DVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07089 426 GPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
37-491 |
4.64e-151 |
|
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: 439.05 E-value: 4.64e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 37 AIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwN 116
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 117 IDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPF 196
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 197 SALRLAELALEAGVPEGVLNVVPGLGEqAGKALGLHPEVDALVFTGSTEVGKYFMQYSAqSNLKQVWLECGGKSPNLVFA 276
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 277 DCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIE 356
Cdd:cd07090 236 DA-DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 357 RAQGEGATLLGGGRQLTI-NGSDN--FIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWS 433
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPeDGLENgfYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489174509 434 DDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKTT 491
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
19-490 |
9.06e-151 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 439.32 E-value: 9.06e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 19 QALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREE 98
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI--WAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 99 LALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGV---IGAvvpWNFPLDMAAWK 175
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVcagIGA---WNYPIQIACWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 176 LAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEqAGKALGLHPEVDALVFTGSTEVGKYFMQYSA 255
Cdd:PRK13252 163 SAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 256 QSnLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDP 335
Cdd:PRK13252 242 AS-LKEVTMELGGKSPLIVFDDA-DLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 336 ASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDN--FIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSE 413
Cdd:PRK13252 320 ATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANgaFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489174509 414 DEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:PRK13252 400 DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
38-489 |
1.29e-149 |
|
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: 435.24 E-value: 1.29e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 38 IDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNI 117
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 118 DVPGAAHVFAWYAESLDKLyDQVAPTA-----QQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAE 192
Cdd:cd07110 79 DVDDVAGCFEYYADLAEQL-DAKAERAvplpsEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 193 QSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPN 272
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 273 LVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGIL 352
Cdd:cd07110 237 IVFDDA-DLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 353 AAIERAQGEGATLLGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLW 432
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489174509 433 SDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
18-489 |
2.02e-148 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 432.80 E-value: 2.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 18 DQALIGGrQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHRE 97
Cdd:PRK13473 3 TKLLING-ELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 98 ELALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYdqvAPTAQQALA----TITRVPLGVIGAVVPWNFPLDMAA 173
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLE---GKAAGEYLEghtsMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 174 WKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAgVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQy 253
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 254 SAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPL 333
Cdd:PRK13473 235 AAADSVKRTHLELGGKAPVIVFDDA-DLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 334 DPASRAGAIVDRRQTAGILAAIERAQGEG-ATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDS 412
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY--YYEPTLLAGARQDDEIVQREVFGPVVSVTPFDD 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489174509 413 EDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:PRK13473 392 EDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-490 |
2.09e-148 |
|
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: 432.31 E-value: 2.09e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDegPWARLAPVERKRVLLRLAELMLAHREELAL 101
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 102 LDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDklydQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALA 181
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALK----DFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 182 AGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSnLKQ 261
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT-VKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 262 VWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGA 341
Cdd:cd07138 236 VALELGGKSANIILDDA-DLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 342 IVDRRQTAGILAAIERAQGEGATLLGGGRQLTiNGSDN--FIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRL 419
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGARLVAGGPGRP-EGLERgyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489174509 420 ANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTvDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07138 394 ANDTPYGLAGYVWSADPERARAVARRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKS 463
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-490 |
9.36e-145 |
|
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: 423.83 E-value: 9.36e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 13 TQRFIDQALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVLLRLAELM 92
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 93 LAHREELALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQ----QALATITRVPLGVIGAVVPWNFP 168
Cdd:cd07140 81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQarpnRNLTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 169 LDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGK 248
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 249 YFMQYSAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQ 328
Cdd:cd07140 241 HIMKSCAVSNLKKVSLELGGKSPLIIFADC-DMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 329 PGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAIS 408
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF--FFEPTVFTDVEDHMFIAKEESFGPIMIIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 409 AFDSED--EAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYT 486
Cdd:cd07140 398 KFDDGDvdGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYL 477
|
....
gi 489174509 487 QLKT 490
Cdd:cd07140 478 KTKT 481
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
73-493 |
1.46e-144 |
|
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: 418.94 E-value: 1.46e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKL-YDQVAPTAQQALATI 151
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLgGPELPSPDPGGEAYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGL 231
Cdd:cd06534 89 RREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERS 311
Cdd:cd06534 169 HPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDA-DLDAAVEGAVFGAFFNAGQICTAASRLLVHES 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 IHDEFVERLLakardwqpgdpldpasragaivdrrqtagilaaieraqgegatllgggrqltingsdnfiepTLFGDVRP 391
Cdd:cd06534 247 IYDEFVEKLV--------------------------------------------------------------TVLVDVDP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 392 DMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVA-VPFGGGKQ 470
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPFGGVKN 344
|
410 420
....*....|....*....|...
gi 489174509 471 SGFGRDLSLHSFDKYTQLKTTWF 493
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
21-489 |
1.01e-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: 418.40 E-value: 1.01e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 21 LIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELA 100
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 101 LLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPAL 180
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 181 AAGNSVVLKPAEQSPFSALRLAELaLEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGkYFMQYSAQSNLK 260
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVG-RDVAIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 261 QVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAG 340
Cdd:cd07117 240 PATLELGGKSANIIFDDA-NWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 341 AIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDN--FIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIR 418
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489174509 419 LANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
73-489 |
6.89e-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: 410.18 E-value: 6.89e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQA-LATI 151
Cdd:cd07092 35 WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAGAARTLEGPAAGEYLPGhTSMI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEaGVPEGVLNVVPGLGEQAGKALGL 231
Cdd:cd07092 115 RREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERS 311
Cdd:cd07092 194 HPRVRMVSLTGSVRTGKKVAR-AAADTLKRVHLELGGKAPVIVFDDA-DLDAAVAGIATAGYYNAGQDCTAACRVYVHES 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 IHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQgEGATLLGGGRQLTINGSdnFIEPTLFGDVRP 391
Cdd:cd07092 272 VYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP-AHARVLTGGRRAEGPGY--FYEPTVVAGVAQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 392 DMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQS 471
Cdd:cd07092 349 DDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQS 428
|
410
....*....|....*...
gi 489174509 472 GFGRDLSLHSFDKYTQLK 489
Cdd:cd07092 429 GYGKDLSIYALEDYTRIK 446
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
73-490 |
4.64e-139 |
|
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: 408.95 E-value: 4.64e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNiDVPGAAHVFAWYA-ESLDKLYDQVAPTAQQALATI 151
Cdd:cd07097 53 WRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARG-EVTRAGQIFRYYAgEALRLSGETLPSTRPGVEVET 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGL 231
Cdd:cd07097 132 TREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYfMQYSAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERS 311
Cdd:cd07097 212 HPDVDAVSFTGSTAVGRR-IAAAAAARGARVQLEMGGKNPLVVLDDA-DLDLAVECAVQGAFFSTGQRCTASSRLIVTEG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 IHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDNFIEPTLFGDVRP 391
Cdd:cd07097 290 IHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTN 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 392 DMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDA-LDVAVPFGGGKQ 470
Cdd:cd07097 370 DMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKG 449
|
410 420
....*....|....*....|.
gi 489174509 471 SGFG-RDLSLHSFDKYTQLKT 490
Cdd:cd07097 450 SSYGpREQGEAALEFYTTIKT 470
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
73-489 |
1.07e-137 |
|
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: 403.83 E-value: 1.07e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALldslnmgkpvmdaWNIDVPGAAHVFAWY------------AESLDKLYDQV 140
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIAD-------------WLIRESGSTRPKAAFevgaaiailreaAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 141 APTAQQA-LATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFS-ALRLAELALEAGVPEGVLNVV 218
Cdd:cd07104 83 LPSDVPGkESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 219 PGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGE 298
Cdd:cd07104 163 PGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGE-LAGRHLKKVALELGGNNPLIVLDDA-DLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 299 VCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGrqlTINGsd 378
Cdd:cd07104 241 ICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG---TYEG-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 379 NFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDA 458
Cdd:cd07104 316 LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTV 395
|
410 420 430
....*....|....*....|....*....|..
gi 489174509 459 LDVA-VPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07104 396 NDEPhVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-489 |
2.03e-137 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 405.66 E-value: 2.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 19 QALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDE---GPWARLAPVERKRVLLRLAELMLAH 95
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 96 REELALLDSLNMGKPVMDA-WNI-DVPGAAHVFAWYAESLDKlyDQVAPTA---QQALATITRVPLGVIGAVVPWNFPLD 170
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAaWDMdDVAGCFEYYADLAEALDA--KQKAPVSlpmETFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 171 MAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYF 250
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 251 MQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPG 330
Cdd:PLN02467 247 MTAAAQ-MVKPVSLELGGKSPIIVFDDV-DLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 331 DPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAF 410
Cdd:PLN02467 325 DPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489174509 411 DSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
21-490 |
3.36e-136 |
|
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: 401.73 E-value: 3.36e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 21 LIGGRQRPAASGATFDAIDPASNR-LLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREEL 99
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAFPE--WRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 100 ALLDSLNMGKPVMDAWNiDVPGAAHVFAWYAESLDKLYDQVAPT--AQQALATItRVPLGVIGAVVPWNFPLDMAAWKLA 177
Cdd:cd07131 80 ARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSelPNKDAMTR-RQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 178 PALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQS 257
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 258 NlKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPAS 337
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDA-DLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 338 RAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSD--NFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDE 415
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEkgYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489174509 416 AIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDAlDVAVPFGGGKQSGFG-RDLSLHSFDKYTQLKT 490
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
73-493 |
5.50e-133 |
|
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: 392.28 E-value: 5.50e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAeSLDkLYDQVAPTAQQALATIT 152
Cdd:cd07106 35 WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGGAVAWLRYTA-SLD-LPDEVIEDDDTRRVELR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 153 RVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAgVPEGVLNVVPGLGEQaGKALGLH 232
Cdd:cd07106 112 RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 233 PEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSI 312
Cdd:cd07106 190 PDIRKISFTGSTATGKKVMA-SAAKTLKRVTLELGGNDAAIVLPDV-DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 313 HDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGsdNFIEPTLFGDVRPD 392
Cdd:cd07106 268 YDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPG--YFIPPTIVDDPPEG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 393 MQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSG 472
Cdd:cd07106 346 SRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSG 425
|
410 420
....*....|....*....|.
gi 489174509 473 FGRDLSLHSFDKYTQLKTTWF 493
Cdd:cd07106 426 IGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
22-490 |
1.07e-132 |
|
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: 392.40 E-value: 1.07e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELAL 101
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 102 LDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAP---TAQQALatITRVPLGVIGAVVPWNFPLDMAAWKLAP 178
Cdd:cd07088 80 LIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPsdrPNENIF--IFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 179 ALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsN 258
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 259 LKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASR 338
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDA-DLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 339 AGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIR 418
Cdd:cd07088 315 MGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKG-YFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489174509 419 LANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTvDALDVAVPFGGG-KQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINR-ENFEAMQGFHAGwKKSGLGGADGKHGLEEYLQTKV 465
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
38-495 |
2.39e-132 |
|
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: 390.97 E-value: 2.39e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 38 IDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNi 117
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 118 DVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFS 197
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 198 ALRLAELALEAgVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSnLKQVWLECGGKSPNLVFAD 277
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 278 CrDLDLAAEKAAFGIFFN-QGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIE 356
Cdd:cd07107 237 A-DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 357 RAQGEGATLL-GGGRQLTINGSDNF-IEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSD 434
Cdd:cd07107 316 SAKREGARLVtGGGRPEGPALEGGFyVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489174509 435 DLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKTTWFQL 495
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
38-490 |
1.77e-131 |
|
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: 389.03 E-value: 1.77e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 38 IDPASNRLLARVAACDAADVDAAVAAARRAFdeGPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNI 117
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 118 DVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFS 197
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 198 ALRLAELALEAgVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFAD 277
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYR-AAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 278 CrDLDLAAEKAAFGI-FFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIE 356
Cdd:cd07108 238 A-DLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 357 RAQGE-GATLLGGGRQLT--INGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWS 433
Cdd:cd07108 317 LGLSTsGATVLRGGPLPGegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489174509 434 DDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHS-FDKYTQLKT 490
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKT 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
22-476 |
9.03e-127 |
|
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: 377.89 E-value: 9.03e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELAL 101
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 102 LDSLNMGKPVMDAWNIDVPGAAHVFAWYAESldklydqvAPTAQQALATitRVPLGVIGAVVPWNFPLDMAAWKLAPALA 181
Cdd:cd07111 104 LESLDNGKPIRESRDCDIPLVARHFYHHAGW--------AQLLDTELAG--WKPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 182 AGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEqAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSNlKQ 261
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAGTG-KK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 262 VWLECGGKSPNLVFaDCRDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGA 341
Cdd:cd07111 252 LSLELGGKSPFIVF-DDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 342 IVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLAN 421
Cdd:cd07111 331 IVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP--FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489174509 422 DSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRD 476
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGRE 463
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
16-489 |
5.95e-126 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 376.34 E-value: 5.95e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 16 FIDQALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDegPWARLAPVERKRVLLRLAELMLAH 95
Cdd:PLN02278 23 LRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIAN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 96 REELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAPTAQ---QALATitRVPLGVIGAVVPWNFPLDMA 172
Cdd:PLN02278 101 KEDLAQLMTLEQGKPLKEA-IGEVAYGASFLEYFAEEAKRVYGDIIPSPFpdrRLLVL--KQPVGVVGAITPWNFPLAMI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 173 AWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQ 252
Cdd:PLN02278 178 TRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 253 YSAQSnLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDP 332
Cdd:PLN02278 258 GAAAT-VKRVSLELGGNAPFIVFDDA-DLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 333 LDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGsdNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDS 412
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGG--TFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKT 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489174509 413 EDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNT-VDALDVAvPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:PLN02278 414 EEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEgLISTEVA-PFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
22-489 |
5.87e-125 |
|
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: 372.94 E-value: 5.87e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELAL 101
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 102 LDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALA 181
Cdd:cd07116 83 AETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 182 AGNSVVLKPAEQSPFSALRLAELALEAgVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQ 261
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 262 VWLECGGKSPNLVFADCRD-----LDLAAEkaAFGIF-FNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDP 335
Cdd:cd07116 241 VTLELGGKSPNIFFADVMDaddafFDKALE--GFVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 336 ASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGR--QLTINGSDNFIEPTLFGDVRpDMQLAREEIFGPVLAISAFDSE 413
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGErnELGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489174509 414 DEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07116 398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
35-489 |
1.55e-124 |
|
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: 370.89 E-value: 1.55e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 35 FDAIDPASNRLLARVAACDAADVDAAVAAARRAFdeGPWARLAPVERKRVLLRLAELMLAHREELAllDSLnmgkpvmda 114
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLI--DLL--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 115 wnIDVPGAAHVFAWY------------AESLDKLYDQVAPT-AQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALA 181
Cdd:cd07150 68 --IDEGGSTYGKAWFettftpellraaAGECRRVRGETLPSdSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 182 AGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQySAQSNLKQ 261
Cdd:cd07150 146 AGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAE-KAGRHLKK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 262 VWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGA 341
Cdd:cd07150 225 ITLELGGKNPLIVLADA-DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 342 IVDRRQTAGILAAIERAQGEGATLLGGGRqltinGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLAN 421
Cdd:cd07150 304 LISPRQVERIKRQVEDAVAKGAKLLTGGK-----YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELAN 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489174509 422 DSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVA-VPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07150 379 DTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-490 |
1.10e-122 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 367.15 E-value: 1.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 22 IGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDeGPWARLAPVERKRVLLRLAELMLAHREELAL 101
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 102 LDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQV------APTAQQALATITRVPLGVIGAVVPWNFPLDMAAWK 175
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsipSMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 176 LAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGeQAGKALGLHPEVDALVFTGSTEVGKYFMQySA 255
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGR-QA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 256 QSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDP 335
Cdd:cd07113 241 ASDLTRVTLELGGKNAAAFLKDA-DIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 336 ASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRqlTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDE 415
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE--ALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489174509 416 AIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKS 472
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
35-490 |
1.14e-122 |
|
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: 366.15 E-value: 1.14e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 35 FDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGpwARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDA 114
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM--KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 115 wNIDVPGAAHVFAWYAESLDKLYDQV-----APTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLK 189
Cdd:cd07149 79 -RKEVDRAIETLRLSAEEAKRLAGETipfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 190 PAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKyfmQYSAQSNLKQVWLECGGK 269
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGE---AIARKAGLKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 270 SPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTA 349
Cdd:cd07149 235 AAVIVDADA-DLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 350 GILAAIERAQGEGATLLGGGRQltingSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAA 429
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKR-----DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489174509 430 SLWSDDLHRAHRVARRLNAGTVSVNTVDALDV-AVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07149 389 GVFTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGREGPRYAIEEMTEIKL 450
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
24-489 |
3.07e-120 |
|
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: 360.47 E-value: 3.07e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 24 GRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELALLD 103
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKE--WAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 104 SLNMGKPVMDAwNIDVpGAAHVFAWYAESLdklydqVAPTAQQALATIT--------RVPLGVIGAVVPWNFPLDMAAWK 175
Cdd:cd07151 79 IRESGSTRIKA-NIEW-GAAMAITREAATF------PLRMEGRILPSDVpgkenrvyREPLGVVGVISPWNFPLHLSMRS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 176 LAPALAAGNSVVLKPAEQSPFSA-LRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQyS 254
Cdd:cd07151 151 VAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGE-L 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 255 AQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLD 334
Cdd:cd07151 230 AGRHLKKVALELGGNNPFVVLEDA-DIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 335 PASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGrqlTINGsdNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSED 414
Cdd:cd07151 309 PDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEG--NVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEE 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489174509 415 EAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVA-VPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07151 384 EALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDK 459
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
73-489 |
8.97e-120 |
|
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: 358.84 E-value: 8.97e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDK-LYDQVAPTAQQA---L 148
Cdd:cd07099 34 WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA-GLEVLLALEAIDWAARNAPRvLAPRKVPTGLLMpnkK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 149 ATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEqAGKA 228
Cdd:cd07099 113 ATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 229 LgLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLV 308
Cdd:cd07099 192 L-IDAGVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIVLADA-DLERAAAAAVWGAMVNAGQTCISVERVYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 309 ERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRqlTINGSDNFIEPTLFGD 388
Cdd:cd07099 269 HESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGA--RSNGGGPFYEPTVLTD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 389 VRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTV--DALDVAVPFG 466
Cdd:cd07099 347 VPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVllTAGIPALPFG 426
|
410 420
....*....|....*....|...
gi 489174509 467 GGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07099 427 GVKDSGGGRRHGAEGLREFCRPK 449
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
73-492 |
6.84e-119 |
|
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: 355.61 E-value: 6.84e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDK-LYDQVAPTAQQAlATI 151
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAENAEAfLADEPIETDAGK-AYV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGl 231
Cdd:cd07100 93 RYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEAIIA- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERS 311
Cdd:cd07100 172 DPRVRGVTLTGSERAGRAVAA-EAGKNLKKSVLELGGSDPFIVLDDA-DLDKAVKTAVKGRLQNAGQSCIAAKRFIVHED 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 IHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLtiNGSDNFIEPTLFGDVRP 391
Cdd:cd07100 250 VYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP--DGPGAFYPPTVLTDVTP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 392 DMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQS 471
Cdd:cd07100 328 GMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRS 407
|
410 420
....*....|....*....|.
gi 489174509 472 GFGRDLSLHSFDKYTQLKTTW 492
Cdd:cd07100 408 GYGRELGRFGIREFVNIKTVW 428
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
73-490 |
2.11e-114 |
|
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: 345.10 E-value: 2.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAPT-----AQQA 147
Cdd:cd07145 37 MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RVEVERTIRLFKLAAEEAKVLRGETIPVdayeyNERR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 LATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGK 227
Cdd:cd07145 116 IAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 228 ALGLHPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLL 307
Cdd:cd07145 196 EIVTNPKVNMISFTGSTAVGLLIAS-KAGGTGKKVALELGGSDPMIVLKDA-DLERAVSIAVRGRFENAGQVCNAVKRIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 308 VERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQltINGSdnFIEPTLFG 387
Cdd:cd07145 274 VEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKR--DEGS--FFPPTVLE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 388 DVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDV-AVPFG 466
Cdd:cd07145 350 NDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTRFRWdNLPFG 429
|
410 420
....*....|....*....|....
gi 489174509 467 GGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07145 430 GFKKSGIGREGVRYTMLEMTEEKT 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
73-492 |
9.03e-113 |
|
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: 339.94 E-value: 9.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPvmDAW-NIDVPGAAHVFAWYAESLDKLYDQVAPTAQQA-LAT 150
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT--AAWaGFNVDLAAGMLREAASLITQIIGGSIPSDKPGtLAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 151 ITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGK--- 227
Cdd:cd07105 94 VVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEDAPEvve 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 228 ALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLL 307
Cdd:cd07105 174 ALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDA-DLDAAANAALFGAFLNSGQICMSTERII 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 308 VERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRrqtagILAAIERAQGEGATLLGGGRQLTiNGSDNFIEPTLFG 387
Cdd:cd07105 252 VHESIADEFVEKLKAAAEKLFAGPVVLGSLVSAAAADR-----VKELVDDALSKGAKLVVGGLADE-SPSGTSMPPTILD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 388 DVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDAlDVAVPF 465
Cdd:cd07105 326 NVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINgmTVHD-EPTLPH 404
|
410 420
....*....|....*....|....*...
gi 489174509 466 GGGKQSGFGRDLSLHSFDKYTQLKT-TW 492
Cdd:cd07105 405 GGVKSSGYGRFNGKWGIDEFTETKWiTI 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
73-489 |
6.60e-110 |
|
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: 333.44 E-value: 6.60e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwnidvPGAAHVFAWYAESL-----DKLYDQVAPTAQQA 147
Cdd:cd07102 34 WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-----GGEIRGMLERARYMisiaeEALADIRVPEKDGF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 LATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGK 227
Cdd:cd07102 109 ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 228 ALGLhPEVDALVFTGSTEVGKYfMQYSAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLL 307
Cdd:cd07102 189 LIAD-PRIDHVSFTGSVAGGRA-IQRAAAGRFIKVGLELGGKDPAYVRPDA-DLDAAAESLVDGAFFNSGQSCCSIERIY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 308 VERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGAT-LLGGGRQLTINGSDNFIEPTLF 386
Cdd:cd07102 266 VHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARaLIDGALFPEDKAGGAYLAPTVL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 387 GDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFG 466
Cdd:cd07102 346 TNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWT 425
|
410 420
....*....|....*....|...
gi 489174509 467 GGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07102 426 GVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
38-490 |
3.04e-109 |
|
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: 332.00 E-value: 3.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 38 IDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARlAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNI 117
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 118 DVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFS 197
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 198 ALRLAELALEA-GVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFA 276
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAP-TLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 277 DCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIE 356
Cdd:cd07120 239 DA-DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 357 RAQGEGAT-LLGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDD 435
Cdd:cd07120 318 RAIAAGAEvVLRGGPVTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489174509 436 LHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKH 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
21-474 |
3.78e-109 |
|
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: 333.42 E-value: 3.78e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 21 LIGGRQRPaaSGATFDAIDPA-SNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREEL 99
Cdd:cd07124 36 VIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 100 ALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPA 179
Cdd:cd07124 112 AAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 180 LAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSA---- 255
Cdd:cd07124 191 LVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqp 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 256 -QSNLKQVWLECGGKSPNLVFADCrDLDLAAE---KAAFGIffnQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGD 331
Cdd:cd07124 271 gQKWLKRVIAEMGGKNAIIVDEDA-DLDEAAEgivRSAFGF---QGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 332 PLDPASRAGAIVDRRQTAGILAAIERAQGEGaTLLGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFD 411
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489174509 412 SEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDALDVAVPFGGGKQSGFG 474
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
21-490 |
7.65e-109 |
|
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: 331.45 E-value: 7.65e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 21 LIGGRQRPAASGaTFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARL-APVeRKRVLLRLAELMLAHREEL 99
Cdd:cd07086 2 VIGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE--WRKVpAPR-RGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 100 ALLDSLNMGKP-------VMDAWNIdvpgaahvfAWYAESLDK-LYDQVAPT--AQQALATiTRVPLGVIGAVVPWNFPL 169
Cdd:cd07086 78 GRLVSLEMGKIlpeglgeVQEMIDI---------CDYAVGLSRmLYGLTIPSerPGHRLME-QWNPLGVVGVITAFNFPV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 170 DMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEA----GVPEGVLNVVPGLGEqAGKALGLHPEVDALVFTGSTE 245
Cdd:cd07086 148 AVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 246 VGKYFMQYSAQSNlKQVWLECGGKSPNLVFaDCRDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKAR 325
Cdd:cd07086 227 VGRRVGETVARRF-GRVLLELGGNNAIIVM-DDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 326 DWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVL 405
Cdd:cd07086 305 QVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPIL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 406 AISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRV--ARRLNAGTVSVN--TVDAlDVAVPFGGGKQSGFGRDLSLHS 481
Cdd:cd07086 385 YVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDA 463
|
....*....
gi 489174509 482 FDKYTQLKT 490
Cdd:cd07086 464 WKQYMRRST 472
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
74-490 |
5.94e-108 |
|
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: 328.55 E-value: 5.94e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 74 ARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQ-----VAPTAQQAL 148
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT-RYEVGRAADVLRFAAAEALRDDGEsfscdLTANGKARK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 149 ATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKA 228
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 229 LGLHPEVDALVFTGSTEVGKYFmqySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLV 308
Cdd:cd07146 194 LITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPLIVMDDA-DLERAATLAVAGSYANSGQRCTAVKRILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 309 ERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQltiNGSdnFIEPTLFGD 388
Cdd:cd07146 270 HESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR---QGA--LYAPTVLDH 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 389 VRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVA-VPFGG 467
Cdd:cd07146 345 VPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGG 424
|
410 420
....*....|....*....|....
gi 489174509 468 GKQSGFG-RDLSLHSFDKYTQLKT 490
Cdd:cd07146 425 VKDSGLGgKEGVREAMKEMTNVKT 448
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
73-490 |
1.24e-106 |
|
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: 325.16 E-value: 1.24e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQA----- 147
Cdd:cd07094 37 RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEVDRAIDTLRLAAEEAERIRGEEIPLDATQgsdnr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 LATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGK 227
Cdd:cd07094 116 LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 228 ALGLHPEVDALVFTGSTEVGKYFmqySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLL 307
Cdd:cd07094 196 AFAADERVAMLSFTGSAAVGEAL---RANAGGKRIALELGGNAPVIVDRDA-DLDAAIEALAKGGFYHAGQVCISVQRIY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 308 VERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQltingSDNFIEPTLFG 387
Cdd:cd07094 272 VHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGER-----DGALFKPTVLE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 388 DVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDV-AVPFG 466
Cdd:cd07094 347 DVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFG 426
|
410 420
....*....|....*....|....
gi 489174509 467 GGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07094 427 GVKESGVGREGVPYAMEEMTEEKT 450
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
73-487 |
1.36e-105 |
|
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: 321.94 E-value: 1.36e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDA-WNIDVpgAAHVFAWYAESLDKLYDQVAPTAQQALATI 151
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAgFEVGA--AIGELHEAAGLPTQPQGEILPSAPGRLSLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSA-LRLAELALEAGVPEGVLNVVPGlGEQAGKALG 230
Cdd:cd07152 107 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GADAGEALV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 231 LHPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVER 310
Cdd:cd07152 186 EDPNVAMISFTGSTAVGRKVGE-AAGRHLKKVSLELGGKNALIVLDDA-DLDLAASNGAWGAFLHQGQICMAAGRHLVHE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 311 SIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGrqlTINGSdnFIEPTLFGDVR 390
Cdd:cd07152 264 SVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGG---TYDGL--FYRPTVLSGVK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 391 PDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALD-VAVPFGGGK 469
Cdd:cd07152 339 PGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDePHNPFGGMG 418
|
410
....*....|....*....
gi 489174509 470 QSGFGRDLS-LHSFDKYTQ 487
Cdd:cd07152 419 ASGNGSRFGgPANWEEFTQ 437
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
73-486 |
1.83e-105 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 322.60 E-value: 1.83e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPV-ERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAP-----TAQQ 146
Cdd:cd07082 54 WWPTMPLeERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRLDGDSLPgdwfpGTKG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 147 ALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAG 226
Cdd:cd07082 133 KIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 227 KALGLHPEVDALVFTGSTEVGKYFMQysaQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRL 306
Cdd:cd07082 213 DPLVTHGRIDVISFTGSTEVGNRLKK---QHPMKRLVLELGGKDPAIVLPDA-DLELAAKEIVKGALSYSGQRCTAIKRV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 307 LVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTingsDNFIEPTLF 386
Cdd:cd07082 289 LVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG----GNLIYPTLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 387 GDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDALDVaVP 464
Cdd:cd07082 365 DPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskCQRGPDH-FP 443
|
410 420
....*....|....*....|....*.
gi 489174509 465 FGGGKQSGFG----RDlSLHSFDKYT 486
Cdd:cd07082 444 FLGRKDSGIGtqgiGD-ALRSMTRRK 468
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
73-490 |
1.46e-103 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 319.52 E-value: 1.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWN--IDVPGAAhvfAWYAESLDKLYDQ-----VAPTAQ 145
Cdd:PRK09407 70 WAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEevLDVALTA---RYYARRAPKLLAPrrragALPVLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 146 QAlaTITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQA 225
Cdd:PRK09407 147 KT--TELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 226 GKALGlhPEVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSR 305
Cdd:PRK09407 225 GTALV--DNADYLMFTGSTATGRVLAE-QAGRRLIGFSLELGGKNPMIVLDDA-DLDKAAAGAVRACFSNAGQLCISIER 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 306 LLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdNFIEPTL 385
Cdd:PRK09407 301 IYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGP-LFYEPTV 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 386 FGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--------TVD 457
Cdd:PRK09407 380 LTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaawgSVD 459
|
410 420 430
....*....|....*....|....*....|...
gi 489174509 458 AldvavPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:PRK09407 460 A-----PMGGMKDSGLGRRHGAEGLLKYTESQT 487
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-489 |
5.94e-103 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 316.85 E-value: 5.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 13 TQRFIDQALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDegPWARLAPVERKRVLLRLAELM 92
Cdd:PRK11241 6 STLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 93 LAHREELALLDSLNMGKPVMDAWNiDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATIT-RVPLGVIGAVVPWNFPLDM 171
Cdd:PRK11241 84 MEHQDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 172 AAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFM 251
Cdd:PRK11241 163 ITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 252 QYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGD 331
Cdd:PRK11241 243 EQCAK-DIKKVSLELGGNAPFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 332 PLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGsdNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFD 411
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGG--NFFQPTILVDVPANAKVAKEETFGPLAPLFRFK 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489174509 412 SEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:PRK11241 399 DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
72-489 |
8.73e-102 |
|
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: 312.64 E-value: 8.73e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 72 PWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQV-----APTAQQ 146
Cdd:cd07147 36 PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RGEVARAIDTFRIAAEEATRIYGEVlpldiSARGEG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 147 ALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAg 226
Cdd:cd07147 115 RQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 227 KALGLHPEVDALVFTGSTEVGkYFMqySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRL 306
Cdd:cd07147 194 DLLVTDERIKLLSFTGSPAVG-WDL--KARAGKKKVVLELGGNAAVIVDSDA-DLDFAAQRIIFGAFYQAGQSCISVQRV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 307 LVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQltingSDNFIEPTLF 386
Cdd:cd07147 270 LVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR-----DGALLEPTIL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 387 GDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDV-AVPF 465
Cdd:cd07147 345 EDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVdHMPY 424
|
410 420
....*....|....*....|....
gi 489174509 466 GGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07147 425 GGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
73-490 |
4.27e-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: 310.78 E-value: 4.27e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWN--IDVPGAAHVFAWYAESLdkLYDQVAPTAQQALAT 150
Cdd:cd07101 34 WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEevLDVAIVARYYARRAERL--LKPRRRRGAIPVLTR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 151 IT--RVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKA 228
Cdd:cd07101 112 TTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 229 LGLHpeVDALVFTGSTEVGKYFMQySAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLV 308
Cdd:cd07101 192 IVDN--ADYVMFTGSTATGRVVAE-RAGRRLIGCSLELGGKNPMIVLEDA-DLDKAAAGAVRACFSNAGQLCVSIERIYV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 309 ERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdNFIEPTLFGD 388
Cdd:cd07101 268 HESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGP-YFYEPTVLTG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 389 VRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--------TVDAld 460
Cdd:cd07101 347 VTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegyaaawaSIDA-- 424
|
410 420 430
....*....|....*....|....*....|
gi 489174509 461 vavPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07101 425 ---PMGGMKDSGLGRRHGAEGLLKYTETQT 451
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
19-490 |
8.57e-101 |
|
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: 310.99 E-value: 8.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 19 QALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREE 98
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 99 LALLDSLNMGKPVMDAWNiDVPGAAHV--FAWYAESLDKlydqvAPTAQQALATI----TRVPLGVIGAVVPWNFPLDMA 172
Cdd:cd07085 80 LARLITLEHGKTLADARG-DVLRGLEVveFACSIPHLLK-----GEYLENVARGIdtysYRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 173 AWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGlGEQAGKALGLHPEVDALVFTGSTEVGKYFmq 252
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYI-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 253 YS-AQSNLKQVWLECGGKSPNLVFADCrDLDLAAEK---AAFGiffNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQ 328
Cdd:cd07085 231 YErAAANGKRVQALGGAKNHAVVMPDA-DLEQTANAlvgAAFG---AAGQRCMALSVAVAVGDEADEWIPKLVERAKKLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 329 PGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSD--NFIEPTLFGDVRPDMQLAREEIFGPVLA 406
Cdd:cd07085 307 VGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYEngNFVGPTILDNVTPDMKIYKEEIFGPVLS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 407 ISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNtvdaLDVAVP-----FGGGKQSGFGrDLSLH- 480
Cdd:cd07085 387 IVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLHFYg 461
|
490
....*....|..
gi 489174509 481 --SFDKYTQLKT 490
Cdd:cd07085 462 kdGVRFYTQTKT 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
73-491 |
3.31e-91 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 287.22 E-value: 3.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQA-LATI 151
Cdd:PRK03137 89 WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLADGKPVESRPGeHNRY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGViGAVV-PWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALG 230
Cdd:PRK03137 168 FYIPLGV-GVVIsPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 231 LHPEVDALVFTGSTEVGKYFMQYSA-----QSNLKQVWLECGGKSPNLVFADCrDLDLAAE---KAAFGIffnQGEVCSA 302
Cdd:PRK03137 247 DHPKTRFITFTGSREVGLRIYERAAkvqpgQIWLKRVIAEMGGKDAIVVDEDA-DLDLAAEsivASAFGF---SGQKCSA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 303 NSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASrAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQltiNGSDNFIE 382
Cdd:PRK03137 323 CSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAY-MGPVINQASFDKIMSYIEIGKEEGRLVLGGEGD---DSKGYFIQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 383 PTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDALD 460
Cdd:PRK03137 399 PTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIV 478
|
410 420 430
....*....|....*....|....*....|....*..
gi 489174509 461 VAVPFGGGKQSGF-----GRD-LSLHsfdkyTQLKTT 491
Cdd:PRK03137 479 GYHPFGGFNMSGTdskagGPDyLLLF-----LQAKTV 510
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
73-475 |
2.20e-87 |
|
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: 275.72 E-value: 2.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwnidvpgaahVFAWYAESLDKLyDQVAPTAQQALATIT 152
Cdd:cd07098 34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDA----------SLGEILVTCEKI-RWTLKHGEKALRPES 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 153 R---------------VPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSA---LRLAELALEA-GVPEG 213
Cdd:cd07098 103 RpggllmfykrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSgffLSIIRECLAAcGHDPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 214 VLNVVPGLGEqAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSnLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIF 293
Cdd:cd07098 183 LVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGGKDPAIVLDDA-DLDQIASIIMRGTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 294 FNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGR--Q 371
Cdd:cd07098 260 QSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKryP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 372 LTINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTV 451
Cdd:cd07098 340 HPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMV 419
|
410 420
....*....|....*....|....*.
gi 489174509 452 SVN--TVDALDVAVPFGGGKQSGFGR 475
Cdd:cd07098 420 AINdfGVNYYVQQLPFGGVKGSGFGR 445
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
155-494 |
5.15e-83 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 262.75 E-value: 5.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 155 PLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPE 234
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 235 VDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHD 314
Cdd:PRK10090 151 VAMVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDA-DLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 315 EFVERLLAKARDWQPGDPLDPASRA-GAIVDRRQTAGILAAIERAQGEGATLLGGGRQLtiNGSDNFIEPTLFGDVRPDM 393
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKAV--EGKGYYYPPTLLLDVRQEM 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 394 QLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTvDALDVAVPFGGG-KQSG 472
Cdd:PRK10090 307 SIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR-ENFEAMQGFHAGwRKSG 385
|
330 340
....*....|....*....|..
gi 489174509 473 FGRDLSLHSFDKYTQLKTTWFQ 494
Cdd:PRK10090 386 IGGADGKHGLHEYLQTQVVYLQ 407
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
37-492 |
3.01e-80 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 257.48 E-value: 3.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 37 AIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwN 116
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 117 IDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPF 196
Cdd:PRK13968 88 AEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 197 SALRLAELALEAGVPEGVLNVVPGLGEQAGKALGlHPEVDALVFTGSTEVGKYfMQYSAQSNLKQVWLECGGKSPNLVFA 276
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAA-IGAQAGAALKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 277 DCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAG--AIVDRRQTagILAA 354
Cdd:PRK13968 246 DA-DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGpmARFDLRDE--LHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 355 IERAQGEGATLLGGGRQltINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSD 434
Cdd:PRK13968 323 VEATLAEGARLLLGGEK--IAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489174509 435 DLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGRDLSLHSFDKYTQLKTTW 492
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
80-492 |
6.63e-79 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 253.51 E-value: 6.63e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 80 ERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLY-----DQVAPTAQQALATITrv 154
Cdd:PRK09406 46 QRARWANAAADLLEAEADQVAALMTLEMGKTLASA-KAEALKCAKGFRYYAEHAEALLadepaDAAAVGASRAYVRYQ-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 155 PLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPgLGEQAGKALGLHPE 234
Cdd:PRK09406 123 PLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 235 VDALVFTGSTEVGKYFMQYsAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHD 314
Cdd:PRK09406 202 VAAATLTGSEPAGRAVAAI-AGDEIKKTVLELGGSDPFIVMPSA-DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 315 EFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLtiNGSDNFIEPTLFGDVRPDMQ 394
Cdd:PRK09406 280 AFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRP--DGPGWFYPPTVITDITPDMR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 395 LAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFG 474
Cdd:PRK09406 358 LYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYG 437
|
410
....*....|....*...
gi 489174509 475 RDLSLHSFDKYTQLKTTW 492
Cdd:PRK09406 438 RELSAHGIREFCNIKTVW 455
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
72-475 |
1.86e-73 |
|
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: 238.71 E-value: 1.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 72 PWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQqALATI 151
Cdd:cd07095 15 GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGERATPMAQ-GRAVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEqAGKALGL 231
Cdd:cd07095 94 RHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRE-TGEALAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFMQYSAQSNLKQVWLECGGKSPnLVFADCRDLDLAAEKAAFGIFFNQGEVCSANSRLLVERS 311
Cdd:cd07095 173 HEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNP-LVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 -IHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFgDVR 390
Cdd:cd07095 252 aVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTA--FLSPGII-DVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 391 PDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDAlDVAVPFGGG 468
Cdd:cd07095 329 DAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrpTTGA-SSTAPFGGV 407
|
....*..
gi 489174509 469 KQSGFGR 475
Cdd:cd07095 408 GLSGNHR 414
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
68-490 |
7.71e-73 |
|
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: 236.65 E-value: 7.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 68 FDEGpwaRLAPVE-RKRVLLRLAELMLAHREEL--ALLDSLnmGKPvmdawnidvpgaaHVFAWYAE----------SLD 134
Cdd:cd07087 11 FLTG---KTRSLEwRKAQLKALKRMLTENEEEIaaALYADL--GKP-------------PAEAYLTEiavvlgeidhALK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 135 KLYDQVAP-------TAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELaLE 207
Cdd:cd07087 73 HLKKWMKPrrvsvplLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL-IP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 208 AGVPEGVLNVVPGLGEQAgKALGLHPeVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEK 287
Cdd:cd07087 152 KYFDPEAVAVVEGGVEVA-TALLAEP-FDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDA-NLEVAARR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 288 AAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASrAGAIVDRRQTagilaaiERAQG--EGATL 365
Cdd:cd07087 228 IAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPD-YGRIINERHF-------DRLASllDDGKV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 366 LGGGRqltINGSDNFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARR 445
Cdd:cd07087 300 VIGGQ---VDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAE 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489174509 446 LNAGTVSVN------TVDALdvavPFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07087 377 TSSGGVCVNdvllhaAIPNL----PFGGVGNSGMGAYHGKAGFDTFSHLKS 423
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
21-490 |
1.99e-69 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 229.38 E-value: 1.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 21 LIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFdeGPWARLAPVERKRVLLRLAELMLAHREELA 100
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF--LTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 101 LLDSLNMGKPVMDAWNiDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATIT-RVPLGVIGAVVPWNFPLDMAAWKLAPA 179
Cdd:TIGR01722 82 ELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSiRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 180 LAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGlHPEVDALVFTGSTEVGKYfMQYSAQSNL 259
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLE-HPDVKAVSFVGSTPIGRY-IHTTGSAHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 260 KQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIhDEFVERLLAKARDWQPGDPLDPASRA 339
Cdd:TIGR01722 239 KRVQALGGAKNHMVVMPDA-DKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 340 GAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSD--NFIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAI 417
Cdd:TIGR01722 317 GPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEegNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 418 RLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTvdALDVAVP---FGGGKQSGFGrdlSLHSFDK-----YTQLK 489
Cdd:TIGR01722 397 ALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV--PIPVPLPyfsFTGWKDSFFG---DHHIYGKqgthfYTRGK 471
|
.
gi 489174509 490 T 490
Cdd:TIGR01722 472 T 472
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
69-474 |
1.64e-68 |
|
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: 226.53 E-value: 1.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 69 DEGPWarLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQ-----VAPT 143
Cdd:cd07148 36 DRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA-KVEVTRAIDGVELAADELGQLGGReipmgLTPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 144 AQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPgLGE 223
Cdd:cd07148 113 SAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CEN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 224 QAGKALGLHPEVDALVFTGSTEVGKYFmqysaQSNLK---QVWLECGGKSPNLVfADCRDLDLAAEKAAFGIFFNQGEVC 300
Cdd:cd07148 192 AVAEKLVTDPRVAFFSFIGSARVGWML-----RSKLApgtRCALEHGGAAPVIV-DRSADLDAMIPPLVKGGFYHAGQVC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 301 SANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLtingSDNF 380
Cdd:cd07148 266 VSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRL----SDTT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 381 IEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALD 460
Cdd:cd07148 342 YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFR 421
|
410
....*....|....*
gi 489174509 461 VA-VPFGGGKQSGFG 474
Cdd:cd07148 422 VDwMPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
69-474 |
8.44e-68 |
|
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: 226.31 E-value: 8.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 69 DEGPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLY-DQVAPTAQQA 147
Cdd:cd07125 81 AFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFsDPELPGPTGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 LATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGK 227
Cdd:cd07125 160 LNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 228 ALGLHPEVDALVFTGSTEVGKYFMQYSAQSNLKQVWL--ECGGKspNLVFADCR-DLDLAAE---KAAFGiffNQGEVCS 301
Cdd:cd07125 240 ALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGK--NAMIVDSTaLPEQAVKdvvQSAFG---SAGQRCS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 302 ANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEgATLLGggrQLTINGSD-NF 380
Cdd:cd07125 315 ALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIA---PAPLDDGNgYF 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 381 IEPTLFGDVRPDmqLAREEIFGPVLAISAFDSE--DEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TV 456
Cdd:cd07125 391 VAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnIT 468
|
410
....*....|....*....
gi 489174509 457 DALdVAV-PFGGGKQSGFG 474
Cdd:cd07125 469 GAI-VGRqPFGGWGLSGTG 486
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
71-490 |
4.03e-67 |
|
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: 223.99 E-value: 4.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 71 GPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNiDVPGAAHVFAWYAESLDKLYDQ--VAPTAQQAL 148
Cdd:cd07083 69 KTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPavEVVPYPGED 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 149 ATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKA 228
Cdd:cd07083 148 NESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 229 LGLHPEVDALVFTGSTEVGKYFMQYSAQSNLKQVWL-----ECGGKspNLVFAD-CRDLDLAAEKAAFGIFFNQGEVCSA 302
Cdd:cd07083 228 LTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFkrlyvETGGK--NAIIVDeTADFELVVEGVVVSAFGFQGQKCSA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 303 NSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRqltINGSDNFIE 382
Cdd:cd07083 306 ASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKR---LEGEGYFVA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 383 PTLFGDVRPDMQLAREEIFGPVLAISAFDSED--EAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDA 458
Cdd:cd07083 383 PTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGA 462
|
410 420 430
....*....|....*....|....*....|...
gi 489174509 459 LDVAVPFGGGKQSGFG-RDLSLHSFDKYTQLKT 490
Cdd:cd07083 463 LVGVQPFGGFKLSGTNaKTGGPHYLRRFLEMKA 495
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-490 |
6.57e-67 |
|
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: 221.71 E-value: 6.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 75 RLAPVE-RKRVLLRLAELMLAHREelALLDSL--NMGKPVMDAWNIDVPGAAHVFAWYAESLDKL----YDQVAPTAQQA 147
Cdd:cd07135 22 KTKDLEyRLWQLKQLYWAVKDNEE--AIVEALkkDLGRPPFETLLTEVSGVKNDILHMLKNLKKWakdeKVKDGPLAFMF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 L-ATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELaLEAGVPEGVLNVVPGLGEQAG 226
Cdd:cd07135 100 GkPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGGVPETT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 227 KALGLHpeVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRL 306
Cdd:cd07135 179 ALLEQK--FDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNA-DLELAAKRILWGKFGNAGQICVAPDYV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 307 LVERSIHDEFVERLLAKARDWQPGDPLDPaSRAGAIVDRRQTAGILAAIERAQGEgaTLLGGGRqltiNGSDNFIEPTLF 386
Cdd:cd07135 255 LVDPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLDTTKGK--VVIGGEM----DEATRFIPPTIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 387 GDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVdALDVAV--- 463
Cdd:cd07135 328 SDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDT-LIHVGVdna 406
|
410 420
....*....|....*....|....*..
gi 489174509 464 PFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:cd07135 407 PFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
30-475 |
6.18e-65 |
|
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: 217.46 E-value: 6.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 30 ASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARL-APVeRKRVLLRLAELMLAHREELALLDSLNMG 108
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRDVpAPK-RGEIVRQIGDALRKKKEALGKLVSLEMG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 109 KPVMDAWN-----IDVpgaahvfAWYAESLDK-LYDQVAPTAQQALATI-TRVPLGVIGAVVPWNFPLDMAAWKLAPALA 181
Cdd:cd07130 86 KILPEGLGevqemIDI-------CDFAVGLSRqLYGLTIPSERPGHRMMeQWNPLGVVGVITAFNFPVAVWGWNAAIALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 182 AGNSVVLKPAEQSPFSAL---RLAELALEA-GVPEGVLNVVPGlGEQAGKALGLHPEVDALVFTGSTEVGKYFMQySAQS 257
Cdd:cd07130 159 CGNVVVWKPSPTTPLTAIavtKIVARVLEKnGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQ-AVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 258 NLKQVWLECGGKSPNLVFaDCRDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPAS 337
Cdd:cd07130 237 RFGRSLLELGGNNAIIVM-EDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 338 RAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGsdNFIEPTLFgDVRPDMQLAREEIFGPVLAISAFDSEDEAI 417
Cdd:cd07130 316 LVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPG--NYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489174509 418 RLANDSRYGLAASLWSDDLHRAHRV--ARRLNAGTVSVN--TVDAlDVAVPFGGGKQSGFGR 475
Cdd:cd07130 393 AWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNigTSGA-EIGGAFGGEKETGGGR 453
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
80-475 |
1.21e-64 |
|
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: 215.55 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 80 ERKRVLLRLAELMLAHREEL--ALLDSLnmGKPVMDA---------WNIDvPGAAHVFAWYAEsldklyDQVAPTAQQ-- 146
Cdd:cd07134 21 ERIAKLKRLKKAILARREEIiaALAADF--RKPAAEVdlteilpvlSEIN-HAIKHLKKWMKP------KRVRTPLLLfg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 147 ALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVlNVVPGLGEQAG 226
Cdd:cd07134 92 TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEGDAEVAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 227 KALGLhPeVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRL 306
Cdd:cd07134 171 ALLEL-P-FDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETA-DLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 307 LVERSIHDEFVERLLAK-ARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGrqlTINGSDNFIEPTL 385
Cdd:cd07134 247 FVHESVKDAFVEHLKAEiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG---QFDAAQRYIAPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 386 FGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTV--DALDVAV 463
Cdd:cd07134 324 LTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVvlHFLNPNL 403
|
410
....*....|..
gi 489174509 464 PFGGGKQSGFGR 475
Cdd:cd07134 404 PFGGVNNSGIGS 415
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
80-475 |
2.04e-64 |
|
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: 215.04 E-value: 2.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 80 ERKRVLLRLAELMLAHREELAlldslnmgkpvmDAWNIDVPGAAHVFAWYAE----------SLDKLYD-------QVAP 142
Cdd:cd07133 21 ERRDRLDRLKALLLDNQDALA------------EAISADFGHRSRHETLLAEilpsiagikhARKHLKKwmkpsrrHVGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 143 TAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSP-FSALrLAELaLEAGVPEGVLNVVPGl 221
Cdd:cd07133 89 LFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPrTSAL-LAEL-LAEYFDEDEVAVVTG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 222 GEQAGKALGLHPeVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCS 301
Cdd:cd07133 166 GADVAAAFSSLP-FDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDA-DLAKAAERIAFGKLLNAGQTCV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 302 ANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPAsrAGAIVDRRQTAGILAAIERAQGEGATLLgggrQLTINGSDNF- 380
Cdd:cd07133 243 APDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPD--YTSIINERHYARLQGLLEDARAKGARVI----ELNPAGEDFAa 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 381 ---IEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVd 457
Cdd:cd07133 317 trkLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDT- 395
|
410 420
....*....|....*....|.
gi 489174509 458 ALDVAV---PFGGGKQSGFGR 475
Cdd:cd07133 396 LLHVAQddlPFGGVGASGMGA 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
73-491 |
2.53e-62 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 211.15 E-value: 2.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAE----SLDK----LYDQVAPTA 144
Cdd:PLN00412 69 WAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVRSGDLISYTAEegvrILGEgkflVSDSFPGNE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 145 QQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQ 224
Cdd:PLN00412 148 RNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 225 AGKALGLHPEVDALVFTGstevGKYFMQYSAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANS 304
Cdd:PLN00412 228 IGDFLTMHPGVNCISFTG----GDTGIAISKKAGMVPLQMELGGKDACIVLEDA-DLDLAAANIIKGGFSYSGQRCTAVK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 305 RLLVERSIHDEFVERLLAKARDWQPGDPLDPASrAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQltingSDNFIEPT 384
Cdd:PLN00412 303 VVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-----EGNLIWPL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 385 LFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDV-AV 463
Cdd:PLN00412 377 LLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHF 456
|
410 420
....*....|....*....|....*...
gi 489174509 464 PFGGGKQSGFGRDLSLHSFDKYTQLKTT 491
Cdd:PLN00412 457 PFQGLKDSGIGSQGITNSINMMTKVKST 484
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
29-472 |
9.69e-61 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 206.73 E-value: 9.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 29 AASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEgpWARLAPVERKRVLLRLAELMLAHREELALLDSLNMG 108
Cdd:PRK09457 11 AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEELAEVIARETG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 109 KPVMDAwnidVPGAAHVFAWYAESLdKLYDQVAPTAQQALATITRV----PLGVIGAVVPWNFPLDMAAWKLAPALAAGN 184
Cdd:PRK09457 89 KPLWEA----ATEVTAMINKIAISI-QAYHERTGEKRSEMADGAAVlrhrPHGVVAVFGPYNFPGHLPNGHIVPALLAGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 185 SVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGlGEQAGKALGLHPEVDALVFTGSTEVGKYF-MQYSAQSNlKQVW 263
Cdd:PRK09457 164 TVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQFAGQPE-KILA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 264 LECGGKSPnLVFADCRDLDLAAEKAAFGIFFNQGEVCSANSRLLVERSIH-DEFVERLLAKARDWQPGDPL-DPASRAGA 341
Cdd:PRK09457 242 LEMGGNNP-LVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDaEPQPFMGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 342 IVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSdnFIEPTLFgDV-----RPDmqlarEEIFGPVLAISAFDSEDEA 416
Cdd:PRK09457 321 VISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTG--LLTPGII-DVtgvaeLPD-----EEYFGPLLQVVRYDDFDEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489174509 417 IRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDALDVAvPFGGGKQSG 472
Cdd:PRK09457 393 IRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkpLTGASSAA-PFGGVGASG 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
151-489 |
1.34e-59 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 203.72 E-value: 1.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 151 ITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELaLEAGVPEGVLNVVPGlGEQAGKALG 230
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVIEG-GVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 231 LHPeVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVER 310
Cdd:PTZ00381 183 KEP-FDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSC-NLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 311 SIHDEFVERLlAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGegaTLLGGGRqltINGSDNFIEPTLFGDVR 390
Cdd:PTZ00381 260 SIKDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGG---KVVYGGE---VDIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 391 PDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--TVDALDVAVPFGGG 468
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGV 412
|
330 340
....*....|....*....|.
gi 489174509 469 KQSGFGRDLSLHSFDKYTQLK 489
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPK 433
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
81-495 |
2.38e-57 |
|
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: 196.57 E-value: 2.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 81 RKRVLLRLAELMLAHREEL--ALLDSLNmgKPVMDAWNIDVPGAAHVFAWYAESLDKLY--DQV-APTAQQ-ALATITRV 154
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEIleALKKDLG--KSEFEAYMTEIGFVLSEINYAIKHLKKWMkpKRVkTPLLNFpSKSYIYYE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 155 PLGVIGAVVPWNFPLDMAawkLAP---ALAAGNSVVLKPAEQSPFSALRLAELaLEAGVPEGVLNVVPGLGEQAgKALgL 231
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGGVEEN-QEL-L 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVERS 311
Cdd:cd07136 174 DQKFDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDA-NLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 IHDEFVERLLAKARDWQPGDPLDpASRAGAIVDRRQTAGILAAIEraqgEGATLLGGGrqltINGSDNFIEPTLFGDVRP 391
Cdd:cd07136 252 VKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLD----NGKIVFGGN----TDRETLYIEPTILDNVTW 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 392 DMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN-TVdaLDVA---VPFGG 467
Cdd:cd07136 323 DDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdTI--MHLAnpyLPFGG 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 489174509 468 GKQSGFGrdlSLH---SFDKYTQLK-----TTWFQL 495
Cdd:cd07136 401 VGNSGMG---SYHgkySFDTFSHKKsilkkSTWFDL 433
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
21-496 |
3.92e-55 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 194.58 E-value: 3.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 21 LIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFdegPWARLAPVE-RKRVLLRLAELMLAHREEL 99
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAF---PLWRNTPITtRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 100 ALLDSLNMGKPVMDAWNiDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATIT-RVPLGVIGAVVPWNFPLDMAAWKLAP 178
Cdd:PLN02419 194 AMNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSiREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 179 ALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAgKALGLHPEVDALVFTGSTEVGKYFMQYSAQSN 258
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 259 lKQVWLECGGKSPNLVFADCR-DLDLAAEKAA-FGIffnQGEVCSANSRLLV---ERSIHDEFVERllAKARDWQPGDpl 333
Cdd:PLN02419 352 -KRIQSNMGAKNHGLVLPDANiDATLNALLAAgFGA---AGQRCMALSTVVFvgdAKSWEDKLVER--AKALKVTCGS-- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 334 DPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSD--NFIEPTLFGDVRPDMQLAREEIFGPVLAISAFD 411
Cdd:PLN02419 424 EPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEkgNFIGPTILSGVTPDMECYKEEIFGPVLVCMQAN 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 412 SEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTvdALDVAVPFGG--GKQSGFGRDLSLH---SFDKYT 486
Cdd:PLN02419 504 SFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSftGNKASFAGDLNFYgkaGVDFFT 581
|
490
....*....|
gi 489174509 487 QLKTTWFQLR 496
Cdd:PLN02419 582 QIKLVTQKQK 591
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
73-472 |
1.05e-51 |
|
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: 183.56 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLA-HREELALLDSLNMGKPVMDAwNIDVPGAAHVF----AWYAEsldKLYDQVAPTaqQA 147
Cdd:cd07123 85 WARMPFEDRAAIFLKAADLLSGkYRYELNAATMLGQGKNVWQA-EIDAACELIDFlrfnVKYAE---ELYAQQPLS--SP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 LATITRV---PL-GVIGAVVPWNFPLDMAAWKLAPALAaGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGE 223
Cdd:cd07123 159 AGVWNRLeyrPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGP 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 224 QAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQS-----NLKQVWLECGGKspNLVF----ADCRDLDLAAEKAAFGIff 294
Cdd:cd07123 238 VVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGETGGK--NFHLvhpsADVDSLVTATVRGAFEY-- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 295 nQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGE-GATLLGGGrqlt 373
Cdd:cd07123 314 -QGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGG---- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 374 iNGSDN---FIEPTLFGDVRPDMQLAREEIFGPVLAISAFDSED--EAIRLAND-SRYGLAASLWSDDlHRAHRVAR--- 444
Cdd:cd07123 389 -KCDDSvgyFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDfeETLELVDTtSPYALTGAIFAQD-RKAIREATdal 466
|
410 420 430
....*....|....*....|....*....|..
gi 489174509 445 RLNAGTVSVNtvDALDVAV----PFGGGKQSG 472
Cdd:cd07123 467 RNAAGNFYIN--DKPTGAVvgqqPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
155-489 |
5.81e-48 |
|
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: 171.64 E-value: 5.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 155 PLGV---IGAvvpWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAEL-----------ALEAGVPEgvlnvVPG 220
Cdd:cd07132 100 PLGVvliIGA---WNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELipkyldkecypVVLGGVEE-----TTE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 221 LGEQagkalglhpEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVC 300
Cdd:cd07132 172 LLKQ---------RFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSC-DIDVAARRIAWGKFINAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 301 SANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASrAGAIVDRRQTAGILAAIEraqgeGATLLGGGRqltINGSDNF 380
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPD-YGRIINDRHFQRLKKLLS-----GGKVAIGGQ---TDEKERY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 381 IEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN------ 454
Cdd:cd07132 312 IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtimhy 391
|
330 340 350
....*....|....*....|....*....|....*
gi 489174509 455 TVDALdvavPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07132 392 TLDSL----PFGGVGNSGMGAYHGKYSFDTFSHKR 422
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
73-474 |
2.61e-45 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 170.38 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwnID-VPGAAHVFAWYAESLDKLYDQ----VAPTAQqa 147
Cdd:PRK11904 601 WSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDA--IAeVREAVDFCRYYAAQARRLFGApeklPGPTGE-- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 LATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGK 227
Cdd:PRK11904 677 SNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 228 ALGLHPEVDALVFTGSTEVGKYFMQYSAQSNLKQVWL--ECGGKspNLVFAD--------CRDLDLAAekaafgiFFNQG 297
Cdd:PRK11904 757 ALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLiaETGGQ--NAMIVDstalpeqvVDDVVTSA-------FRSAG 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 298 EVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEgATLLGGG--RQLTIN 375
Cdd:PRK11904 828 QRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLplPAGTEN 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 376 GsdNFIEPTLFGDVRPDmQLaREEIFGPVLAISAFDSED-----EAIrlaNDSRYGLAASLWSDDLHRAHRVARRLNAGT 450
Cdd:PRK11904 907 G--HFVAPTAFEIDSIS-QL-EREVFGPILHVIRYKASDldkviDAI---NATGYGLTLGIHSRIEETADRIADRVRVGN 979
|
410 420
....*....|....*....|....*..
gi 489174509 451 VSVN--TVDALdVAV-PFGGGKQSGFG 474
Cdd:PRK11904 980 VYVNrnQIGAV-VGVqPFGGQGLSGTG 1005
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
73-474 |
1.31e-43 |
|
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: 160.85 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNiDVPGAAHVFAWYAESLDKLYDQvaptaqqalatIT 152
Cdd:TIGR01238 90 WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVRDVLGE-----------FS 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 153 RVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLH 232
Cdd:TIGR01238 158 VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 233 PEVDALVFTGSTEVGKYFMQYSAQSNLKQVWL--ECGGKSPNLVFAD------CRDLDLAAekaafgiFFNQGEVCSANS 304
Cdd:TIGR01238 238 PRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTalpeqvVRDVLRSA-------FDSAGQRCSALR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 305 RLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLlgggRQLTINGS-----DN 379
Cdd:TIGR01238 311 VLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKI----AQLTLDDSracqhGT 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 380 FIEPTLFGdvRPDMQLAREEIFGPVLAISAF--DSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN--T 455
Cdd:TIGR01238 387 FVAPTLFE--LDDIAELSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrnQ 464
|
410
....*....|....*....
gi 489174509 456 VDALDVAVPFGGGKQSGFG 474
Cdd:TIGR01238 465 VGAVVGVQPFGGQGLSGTG 483
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
73-474 |
1.72e-42 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 162.03 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWN-----IDvpgaahvFA-WYAESLDKLYDqvAPTAQQ 146
Cdd:COG4230 609 WSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAevreaVD-------FCrYYAAQARRLFA--APTVLR 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 147 alatitrvPLGVIGAVVPWNFPL-----DMAAwklapALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGL 221
Cdd:COG4230 680 --------GRGVFVCISPWNFPLaiftgQVAA-----ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGD 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 222 GEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSNLKQVWL--ECGGKspNLVFAD--------CRDLDLAAekaafg 291
Cdd:COG4230 747 GETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLiaETGGQ--NAMIVDssalpeqvVDDVLASA------ 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 292 iFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATL----LG 367
Cdd:COG4230 819 -FDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhqlpLP 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 368 GGrqlTINGSdnFIEPTLF--GDVRpdmQLAReEIFGPVLAISAFDSED-----EAIrlaNDSRYGLAASLWS--DDlhR 438
Cdd:COG4230 898 EE---CANGT--FVAPTLIeiDSIS---DLER-EVFGPVLHVVRYKADEldkviDAI---NATGYGLTLGVHSriDE--T 963
|
410 420 430
....*....|....*....|....*....|....*....
gi 489174509 439 AHRVARRLNAGTVSVN--TVDALdVAV-PFGGGKQSGFG 474
Cdd:COG4230 964 IDRVAARARVGNVYVNrnIIGAV-VGVqPFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
73-474 |
4.88e-42 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 160.80 E-value: 4.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwnID-VPGAAHVFAWYAEsldklydqvapTAQQALATI 151
Cdd:PRK11905 606 WSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANA--IAeVREAVDFLRYYAA-----------QARRLLNGP 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGL 231
Cdd:PRK11905 673 GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFMQYSAQSNLKQVWL--ECGGKSPNLVfaDCRDLdlaAEKAAFGI----FFNQGEVCSANSR 305
Cdd:PRK11905 753 DPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIV--DSSAL---PEQVVADViasaFDSAGQRCSALRV 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 306 LLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLlgggRQLTINGSDN---FIE 382
Cdd:PRK11905 828 LCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLPAETEkgtFVA 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 383 PTLF--GDVRpDMQlarEEIFGPVLAISAFDSED-----EAIrlaNDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN- 454
Cdd:PRK11905 904 PTLIeiDSIS-DLE---REVFGPVLHVVRFKADEldrviDDI---NATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNr 976
|
410 420
....*....|....*....|..
gi 489174509 455 -TVDALdVAV-PFGGGKQSGFG 474
Cdd:PRK11905 977 nIIGAV-VGVqPFGGEGLSGTG 997
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
155-490 |
2.02e-37 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 143.82 E-value: 2.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 155 PLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEA----GVPEGVLNVVPGlGEQAGKALG 230
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 231 LHPEVDALVFTGSTEVGKyFMQYSAQSNLKQVWLECGGKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCSANSRLLVER 310
Cdd:PLN02315 233 KDTRIPLVSFTGSSKVGL-MVQQTVNARFGKCLLELSGNNAIIVMDDA-DIQLAVRSVLFAAVGTAGQRCTTCRRLLLHE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 311 SIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRqlTINGSDNFIEPTLFgDVR 390
Cdd:PLN02315 311 SIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGS--AIESEGNFVQPTIV-EIS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 391 PDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSddlhRAHRVARRL------NAGTVSVNT-VDALDVAV 463
Cdd:PLN02315 388 PDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT----RNPETIFKWigplgsDCGIVNVNIpTNGAEIGG 463
|
330 340
....*....|....*....|....*..
gi 489174509 464 PFGGGKQSGFGRDLSLHSFDKYTQLKT 490
Cdd:PLN02315 464 AFGGEKATGGGREAGSDSWKQYMRRST 490
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
147-489 |
1.60e-36 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 139.85 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 147 ALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELaLEAGVPEGVLNVVPGlGEQAG 226
Cdd:cd07137 93 AKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEG-GVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 227 KALgLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPnLVFADCRDLDLAAEKAAFGIF-FNQGEVCSANSR 305
Cdd:cd07137 171 TAL-LEQKWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCP-VIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 306 LLVERSIHDEFVERLLAKARDWQPGDPL--DPASRagaIVDRRQTAgILAAIERAQGEGATLLGGGRqltINGSDNFIEP 383
Cdd:cd07137 248 VLVEESFAPTLIDALKNTLEKFFGENPKesKDLSR---IVNSHHFQ-RLSRLLDDPSVADKIVHGGE---RDEKNLYIEP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 384 TLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVN------TVD 457
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtvvqyAID 400
|
330 340 350
....*....|....*....|....*....|..
gi 489174509 458 ALdvavPFGGGKQSGFGRDLSLHSFDKYTQLK 489
Cdd:cd07137 401 TL----PFGGVGESGFGAYHGKFSFDAFSHKK 428
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
73-474 |
3.01e-33 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 134.33 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwnidvpgaahvFAWYAESLDKLY---DQVAPTaqqaLA 149
Cdd:PRK11809 698 WFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNA-----------IAEVREAVDFLRyyaGQVRDD----FD 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 150 TITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKAL 229
Cdd:PRK11809 763 NDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAAL 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 230 GLHPEVDALVFTGSTEVGKYFMQ-----YSAQSNLKQVWLECGGKspNLVFADCRDLdlaAEKAAFGI----FFNQGEVC 300
Cdd:PRK11809 843 VADARVRGVMFTGSTEVARLLQRnlagrLDPQGRPIPLIAETGGQ--NAMIVDSSAL---TEQVVADVlasaFDSAGQRC 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 301 SAnSRLLVersIHDEFVERLLAKARD----WQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQltiNG 376
Cdd:PRK11809 918 SA-LRVLC---LQDDVADRTLKMLRGamaeCRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARE---NS 990
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 377 SD----NFIEPTL-----FGDVrpdmqlaREEIFGPVLAISAFDSE--DEAIRLANDSRYGLAASLWSDDLHRAHRVARR 445
Cdd:PRK11809 991 EDwqsgTFVPPTLieldsFDEL-------KREVFGPVLHVVRYNRNqlDELIEQINASGYGLTLGVHTRIDETIAQVTGS 1063
|
410 420 430
....*....|....*....|....*....|..
gi 489174509 446 LNAGTVSV--NTVDALdVAV-PFGGGKQSGFG 474
Cdd:PRK11809 1064 AHVGNLYVnrNMVGAV-VGVqPFGGEGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
155-489 |
2.69e-32 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 129.08 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 155 PLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAElALEAGVPEGVLNVVPGlGEQAGKALGLHPe 234
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAA-NIPKYLDSKAVKVIEG-GPAVGEQLLQHK- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 235 VDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLV--FADCRDLDLAAEKAAFGIFFN-QGEVCSANSRLLVERS 311
Cdd:PLN02203 185 WDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 312 IHDEFVERLLAKARDWQPGDPLDPASRAgAIVDRRQTAGILAAIERAQGEGATLLGGgrqlTINGSDNFIEPTLFGDVRP 391
Cdd:PLN02203 264 FAPILIELLKSTIKKFFGENPRESKSMA-RILNKKHFQRLSNLLKDPRVAASIVHGG----SIDEKKLFIEPTILLNPPL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 392 DMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTV---DALDvAVPFGGG 468
Cdd:PLN02203 339 DSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAiiqYACD-SLPFGGV 417
|
330 340
....*....|....*....|.
gi 489174509 469 KQSGFGRDLSLHSFDKYTQLK 489
Cdd:PLN02203 418 GESGFGRYHGKYSFDTFSHEK 438
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
69-451 |
2.73e-32 |
|
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: 128.12 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 69 DEGPWARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNIDVPGA---AHVFAWYAESL-DKLYDQVAPTA 144
Cdd:cd07084 11 STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVqlrARAFVIYSYRIpHEPGNHLGQGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 145 QQAlATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAG-VPEGVLNVVPGLGe 223
Cdd:cd07084 91 KQQ-SHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDG- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 224 QAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSnlkQVWLECGGKSPNLVFADCRDLDLAAEKAAFGIFFNQGEVCSAN 303
Cdd:cd07084 169 KTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTACSGQKCTAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 304 SRLLVERSIHDE-FVERLLAKARDWQPGDpldpasragAIVDRRQTAGILAAIERAQGE-GATLLGGGRQLTINGSDNFI 381
Cdd:cd07084 246 SMLFVPENWSKTpLVEKLKALLARRKLED---------LLLGPVQTFTTLAMIAHMENLlGSVLLFSGKELKNHSIPSIY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 382 ----EPTLFGDVRPDMQ---LAREEIFGPVLAISAFDSEDEAIRLANDSRY--GLAASLWSDDLHRAHRVARRLN-AGTV 451
Cdd:cd07084 317 gacvASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLALVLELLERMhgSLTAAIYSNDPIFLQELIGNLWvAGRT 396
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
80-435 |
6.34e-31 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 125.59 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 80 ERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAwNIDVPGAAHVFAWYAESLDKLYDQVA------------PTAQ-Q 146
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDARLlrdgeavqlgkdPAFQgQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 147 ALATITRvplGVIGAVVPWNFPldmaAW----KLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGV-PEGVLNVVpgL 221
Cdd:PRK11903 143 HVLVPTR---GVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVV--C 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 222 GEQAGKALGLHPEvDALVFTGSTEVGKY------FMQYSAQSNLKQVWLECGGKSPNLVfADCRDLDLAAEKAAFGIFFN 295
Cdd:PRK11903 214 GSSAGLLDHLQPF-DVVSFTGSAETAAVlrshpaVVQRSVRVNVEADSLNSALLGPDAA-PGSEAFDLFVKEVVREMTVK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 296 QGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTIN 375
Cdd:PRK11903 292 SGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVD 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489174509 376 GSDN---FIEPTLFGDVRPD-MQLARE-EIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDD 435
Cdd:PRK11903 372 ADPAvaaCVGPTLLGASDPDaATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
80-443 |
8.08e-28 |
|
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: 116.22 E-value: 8.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 80 ERKRVLLRLAELMLAHREELALLdSLNMGKPVMDAWnIDVPGAAHVFAWYAE---------------SLDKLYDQVAPTA 144
Cdd:cd07128 60 ERAAMLKALAKYLMERKEDLYAL-SAATGATRRDSW-IDIDGGIGTLFAYASlgrrelpnahflvegDVEPLSKDGTFVG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 145 QQALatitrVPL-GV---IGAvvpWNFPldmaAW----KLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGV-PEGVL 215
Cdd:cd07128 138 QHIL-----TPRrGVavhINA---FNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 216 NVVPGlgeQAGKALGLHPEVDALVFTGSTEVGKY------FMQYSAQSNLKQVWLECGGKSPNlVFADCRDLDLAAEKAA 289
Cdd:cd07128 206 QLICG---SVGDLLDHLGEQDVVAFTGSAATAAKlrahpnIVARSIRFNAEADSLNAAILGPD-ATPGTPEFDLFVKEVA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 290 FGIFFNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGG 369
Cdd:cd07128 282 REMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 370 RQLTINGSDN----FIEPTLFGDVRPDMQLAREEI--FGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVA 443
Cdd:cd07128 362 DRFEVVGADAekgaFFPPTLLLCDDPDAATAVHDVeaFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
132-494 |
1.18e-27 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 115.53 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 132 SLDKLYDQVAP-------TAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAEL 204
Cdd:PLN02174 82 ALKQLKNWMAPekaktslTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 205 aLEAGVPEGVLNVVPGLGEQAgKALgLHPEVDALVFTGSTEVGKYFMQYSAQsNLKQVWLECGGKSPNLVFADCrDLDLA 284
Cdd:PLN02174 162 -LEQYLDSSAVRVVEGAVTET-TAL-LEQKWDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDT-DLKVT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 285 AEKAAFGIF-FNQGEVCSANSRLLVERSIHDEFVERLLAKARDWQPGDPLDpASRAGAIVDRRQTAGILAAIERAQGEGA 363
Cdd:PLN02174 237 VRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDK 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 364 TLLGGGRQltingSDNF-IEPTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRV 442
Cdd:PLN02174 316 IVYGGEKD-----RENLkIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERF 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489174509 443 ARRLNAGTVSVNTVdALDVA---VPFGGGKQSGFGRDLSLHSFDKYTQLKTTWFQ 494
Cdd:PLN02174 391 AATVSAGGIVVNDI-AVHLAlhtLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYR 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
153-446 |
1.27e-18 |
|
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: 88.37 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 153 RVPLGVIGAVVPWNFPL-------DMAAwklapALAAGNSVVLKPAEQSPFSALRLAELALEA----GVPEGVLNVVPGL 221
Cdd:cd07129 103 LVPLGPVAVFGASNFPLafsvaggDTAS-----ALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 222 GEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQSNL-KQVWLECGGKSPNLVFADC---RDLDLAAEKAAfGIFFNQG 297
Cdd:cd07129 178 GREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFILPGAlaeRGEAIAQGFVG-SLTLGAG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 298 EVCSANSRLLVERSIH-DEFVERLLAKARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQ--LTI 374
Cdd:cd07129 257 QFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPtlFKV 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489174509 375 NGSDNFIEPTLfgdvrpdmqlaREEIFGPVLAISAFDSEDEAIRLANDSRYGLAASLWSD--DLHRAHRVARRL 446
Cdd:cd07129 337 DAAAFLADPAL-----------QEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEedDLALARELLPVL 399
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
154-455 |
1.05e-15 |
|
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: 79.07 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 154 VPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKP---AEQSPFSALR-LAELALEAGVPEGVLNVVPGLGEQAGKAL 229
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKiMREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 230 GLHPEVDALVFTGSTEVGKyfmqySAQSnlkqvwleCG--------GKSPNLVFADCrDLDLAAEKAAFGIFFNQGEVCS 301
Cdd:cd07122 174 MKHPDVDLILATGGPGMVK-----AAYS--------SGkpaigvgpGNVPAYIDETA-DIKRAVKDIILSKTFDNGTICA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 302 ANSRLLVERSIHDEFVERL------------LAKARD--WQPGDPLDPasragAIVDrrQTAGILAA---IERAqgEGAT 364
Cdd:cd07122 240 SEQSVIVDDEIYDEVRAELkrrgayflneeeKEKLEKalFDDGGTLNP-----DIVG--KSAQKIAElagIEVP--EDTK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 365 LLGGgrqltingsdnfiEPTlfgDVRPDMQLAREEIFgPVLAISAFDSEDEAIRLAND-SRYGLA---ASLWSDDLHRAH 440
Cdd:cd07122 311 VLVA-------------EET---GVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYGGAghtAVIHSNDEEVIE 373
|
330
....*....|....*
gi 489174509 441 RVARRLNAGTVSVNT 455
Cdd:cd07122 374 EFALRMPVSRILVNT 388
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
73-461 |
2.90e-12 |
|
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: 68.66 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 73 WARLAPVERKRVLLRLAELMLAHREELALLDSLNMGKPVMDAWNIDVPGA------AHVFAWYAESldklydQVAPTA-- 144
Cdd:cd07127 100 WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQAGGPHAqdrgleAVAYAWREMS------RIPPTAew 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 145 ------QQALA---TITRVPLGVIGAVVPWNFPldmaAWKLAPA----LAAGNSVVLKPaeqSPFSALRLA-------EL 204
Cdd:cd07127 174 ekpqgkHDPLAmekTFTVVPRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKP---HPAAILPLAitvqvarEV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 205 ALEAGV-PEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYSAQsnlKQVWLECGGKSpNLVFADCRDLDL 283
Cdd:cd07127 247 LAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVN-TVVVDSTDDLKA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 284 AAEKAAFGIFFNQGEVCSANSRLLV---------ERSIHDEfVERLLAKARDWQPGDPldpaSRAGAIVDRRQTAGILAA 354
Cdd:cd07127 323 MLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDE-VAADLAAAIDGLLADP----ARAAALLGAIQSPDTLAR 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 355 IERAQGEGATLLGGGRQLTINGSDNFIE-PTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDS---RYGLAAS 430
Cdd:cd07127 398 IAEARQLGEVLLASEAVAHPEFPDARVRtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvreHGAMTVG 477
|
410 420 430
....*....|....*....|....*....|....
gi 489174509 431 LWSDD---LHRAHRVARRLNAgTVSVNTVDALDV 461
Cdd:cd07127 478 VYSTDpevVERVQEAALDAGV-ALSINLTGGVFV 510
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
134-448 |
1.26e-11 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 66.52 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 134 DKLYDQVAPTAQQALATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEA----G 209
Cdd:cd07081 74 DEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 210 VPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKyfmqySAQSNLKQVwLECGGKSPNLVFADCRDLDLAAEKAA 289
Cdd:cd07081 154 APENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVK-----AAYSSGKPA-IGVGAGNTPVVIDETADIKRAVQSIV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 290 FGIFFNQGEVCSANSRLLVERSIHDEFVERL------LAKARDWQPGDP--LDPASRAGAIVDrrQTAGILAAIeraqge 361
Cdd:cd07081 228 KSKTFDNGVICASEQSVIVVDSVYDEVMRLFegqgayKLTAEELQQVQPviLKNGDVNRDIVG--QDAYKIAAA------ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 362 gatllgGGRQLTINGSDNFIEPTLFGDVRPdmqlAREEIFGPVLAI---SAFDSEDE-AIRLANDSRYGLAASLWSDDLH 437
Cdd:cd07081 300 ------AGLKVPQETRILIGEVTSLAEHEP----FAHEKLSPVLAMyraANFADADAkALALKLEGGCGHTSAMYSDNIK 369
|
330
....*....|.
gi 489174509 438 RAHRVARRLNA 448
Cdd:cd07081 370 AIENMNQFANA 380
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
152-442 |
3.72e-11 |
|
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: 65.21 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 152 TRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALgL 231
Cdd:cd07126 139 YRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL-L 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 232 HPEVDALVFTGSTEVGKYFmqysAQSNLKQVWLECGGKSPNLVFADCRDLDLAAEKAAFGIFFNQGEVCSANSRLLV-ER 310
Cdd:cd07126 218 EANPRMTLFTGSSKVAERL----ALELHGKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAhEN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 311 SIHDEFVERLLAKARDWQPGD-PLDPasragaiVDRRQTAGILAAIER-AQGEGATLLGGGRQLTiNGSdnfiEPTLFGD 388
Cdd:cd07126 294 WVQAGILDKLKALAEQRKLEDlTIGP-------VLTWTTERILDHVDKlLAIPGAKVLFGGKPLT-NHS----IPSIYGA 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 389 VRP--------------DMQLAREEIFGPVLAISAFDSEDEAIRLANDSR--YGLAASLWSDDLHRAHRV 442
Cdd:cd07126 362 YEPtavfvpleeiaieeNFELVTTEVFGPFQVVTEYKDEQLPLVLEALERmhAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
74-325 |
1.02e-10 |
|
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: 63.40 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 74 ARLAPVERKRVLLRLAELMLAHREELALLDslnmgkpVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQ-------- 145
Cdd:cd07077 11 AVNHDEQRDLIINAIANALYDTRQRLASEA-------VSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGitasvghi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 146 ------QALATITR-VPLGVIGAVVPWNFPLdMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAEL---ALEAGVPEGVL 215
Cdd:cd07077 84 qdvllpDNGETYVRaFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLfqaADAAHGPKILV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 216 NVVPGLGEQAGKALGLHPEVDALVFTGSTEVGKYFMQYsaqSNLKQVwLECGGKSPNLVFADCRDLDLAAEKAAFGIFFN 295
Cdd:cd07077 163 LYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKH---SPHIPV-IGFGAGNSPVVVDETADEERASGSVHDSKFFD 238
|
250 260 270
....*....|....*....|....*....|
gi 489174509 296 QGeVCSANSRLLVERSIHDEFVERLLAKAR 325
Cdd:cd07077 239 QN-ACASEQNLYVVDDVLDPLYEEFKLKLV 267
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
6-475 |
4.88e-09 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 58.90 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 6 DWQRRAATQRFIDQALIGGRQRPAASGATFDAIDPASNRLLARVAACDAADVDAAVAAARRAFDEGPWARLAPVERKRVL 85
Cdd:COG0506 475 AAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 86 LRLAELMLAHREELALLDSLNMGKPVMDAWNIDVPGAAHVFAWYAESLDKLYDQVAPTAQQALATITRVPLGVIGAVVPW 165
Cdd:COG0506 555 AAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAA 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 166 NFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLNVVPGLGEQAGKALGLHPEVDALVFTGSTE 245
Cdd:COG0506 635 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAA 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 246 --VGKYFMQYSAQSNLKQVWLECGGKSPNLVFADCRDLDLAAEKAAFGIFFnQGEVCSANSRLLVERSIHDEFVERLLAK 323
Cdd:COG0506 715 aaAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASAS-ASASLLSLLALLLLDADLVILLLALAAA 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 324 ARDWQPGDPLDPASRAGAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTINGSDNFIEPTLFGDVRPDMQLAREEIFGP 403
Cdd:COG0506 794 AAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLAL 873
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489174509 404 VLAISAFDSEDEAIRLANDSRYGLAASLWSDDLHRAHRVARRLNAGTVSVNTVDALDVAVPFGGGKQSGFGR 475
Cdd:COG0506 874 VLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 945
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
148-447 |
3.30e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 55.71 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 LATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAEL----ALEAGVPEGVLNVV--PGL 221
Cdd:cd07121 90 LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELinkaIAEAGGPDNLVVTVeePTI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 222 geQAGKALGLHPEVDALVFTGSTEVGKyfmqySAQSNLKQVwLECGGKSPNLVFADCRDLDLAAEKAAFGIFFNQGEVCS 301
Cdd:cd07121 170 --ETTNELMAHPDINLLVVTGGPAVVK-----AALSSGKKA-IGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 302 ANSRLLVERSIHDEFVERLLakardwqpgdpldpasRAGA-IVDRRQTAGIL---------AAIERA-QGEGATLLggGR 370
Cdd:cd07121 242 AEKEVIAVDSVADYLIAAMQ----------------RNGAyVLNDEQAEQLLevvlltnkgATPNKKwVGKDASKI--LK 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489174509 371 QLTINgSDNFIEpTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGL--AASLWSDDLHRAHRVARRLN 447
Cdd:cd07121 304 AAGIE-VPADIR-LIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARAMQ 380
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
148-447 |
5.70e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 54.91 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 148 LATITRVPLGVIGAVVPWNFPLDMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAEL----ALEAGVPEGVLNVV--PGL 221
Cdd:PRK15398 122 LTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELlneaIVAAGGPENLVVTVaePTI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 222 geQAGKALGLHPEVDALVFTGSTEVGKYFMqysaQSNLKQVwlECGGKSPNLVFADCRDLDLAAEKAAFGIFFNQGEVCS 301
Cdd:PRK15398 202 --ETAQRLMKHPGIALLVVTGGPAVVKAAM----KSGKKAI--GAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 302 ANSRLLVERSIHDEFVERLLakardwqpgdpldpasRAGA-IVDRRQTAGILAAI----ERAQ----GEGATLLggGRQL 372
Cdd:PRK15398 274 AEKEVIVVDSVADELMRLME----------------KNGAvLLTAEQAEKLQKVVlkngGTVNkkwvGKDAAKI--LEAA 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489174509 373 TINGSDNFiePTLFGDVRPDMQLAREEIFGPVLAISAFDSEDEAIRLANDSRYGL--AASLWSDDLHRAHRVARRLN 447
Cdd:PRK15398 336 GINVPKDT--RLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
151-384 |
8.00e-06 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 48.21 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 151 ITRVPLGVIGAVVPWNFPLdMAAWKLAPALAAGNSVVLKPAEQSPFSALR-LAELA-LEAGVP-EGVLNVVPGLGEQAGK 227
Cdd:pfam05893 84 EKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSSDPFTAAAlLASFAdLDPTHPlADSLSVVYWDGGSTQL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 228 ALGLHPEVDALVFTGSTE----VGKYfMQYSAQsnlkqvWLECGGKSPNLVFADCRDLDLAAEKAAFGI-FFNQgEVCSA 302
Cdd:pfam05893 163 EDLIVANADVVIAWGGEDainaIREC-LKPGKQ------WIDFGAKISFAVVDREAALDKAAERAADDIcVFDQ-QACLS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 303 NSRLLVERS---IHDEFVERLLAKARDWQPGDP---LDPASRAgAIVDRRQTAGILAAIERAQGEGATLLGGGRQLTING 376
Cdd:pfam05893 235 PQTVFVESDdkiTPDEFAERLAAALAKRARILPkavLDIDEAA-KISSDRAECKLDYAFAGERGVWSDFHQRWTVIWSDG 313
|
....*...
gi 489174509 377 SDNFIEPT 384
Cdd:pfam05893 314 QEELNSPL 321
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
153-360 |
4.74e-05 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 45.73 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 153 RVPLGVIGAVVPWNFPLdMAAWKLAPALAAGNSVVLKPAEQSPFSALRLAELALEAGVPEGVLN-----VVPGLGEQAGK 227
Cdd:cd07080 110 AQPRGLVVHIIAGNVPL-LPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVDPNHPLTDsisvvYWPGGDAELEE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489174509 228 ALGLHpeVDALVFTGSTEVGKYFMQYsAQSNLKqvWLECGGKSPNLVFADC----RDLDLAAEKAAFGI-FFNQgEVCSA 302
Cdd:cd07080 189 RILAS--ADAVVAWGGEEAVKAIRSL-LPPGCR--LIDFGPKYSFAVIDREalesEKLAEVADALAEDIcRYDQ-QACSS 262
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489174509 303 NSRLLVERSIH---DEFVERLLAKARDWQ---PGDPLDPASRAGAIVDRRqtagiLAAIERAQG 360
Cdd:cd07080 263 PQVVFVEKDDDeelREFAEALAAALERLPrryPALSLSAAESAKIARARL-----EAEFYELKG 321
|
|
| |
