|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
20-498 |
0e+00 |
|
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: 882.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 20 YENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKI 99
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 100 AVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPA 179
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 180 LAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIP 259
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 260 ITLELGGKSPSIFFPDVMDADDAFREKCIEGLAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSV 339
Cdd:cd07559 241 VTLELGGKSPNIFFDDAMDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 340 QMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPT-IFRGNNSMRFFREEIFGPVLAVTTFKTLDE 418
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTlIKGGNNDMRIFQEEIFGPVLAVITFKDEEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 419 ALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLVSY 498
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
20-498 |
0e+00 |
|
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: 876.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 20 YENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKI 99
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 100 AVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPA 179
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 180 LAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIP 259
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 260 ITLELGGKSPSIFFPDVMDADDAFREKCIEGLAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSV 339
Cdd:cd07116 241 VTLELGGKSPNIFFADVMDADDAFFDKALEGFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 340 QMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRGNNSMRFFREEIFGPVLAVTTFKTLDEA 419
Cdd:cd07116 321 MIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFKDEEEA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 420 LEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLVSY 498
Cdd:cd07116 401 LEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY 479
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-498 |
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: 646.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 17 KEQYENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENL 96
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 97 EKIAVAETWENGKAIRETLaADIPLAIDHFRYFAGATRTQEGRISQID-DNTVAYHFHEPLGVVGQIIPWNFPLLMAAWK 175
Cdd:COG1012 83 EELAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 176 IAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVS 254
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 255 DKIIPITLELGGKSPSIFFPDVmDADDAfrekcIEGLAMFA-LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGN 333
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDA-DLDAA-----VEAAVRGAfGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 334 PLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAkleGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTT 412
Cdd:COG1012 316 PLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRP---DGEGGYFVEPTVLADvTPDMRIAREEIFGPVLSVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 413 FKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYP-AHAAFGGYKQSGIGRENHLMMLEHYQET 491
Cdd:COG1012 393 FDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTET 472
|
....*..
gi 896153531 492 KCMLVSY 498
Cdd:COG1012 473 KTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
28-492 |
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: 598.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 28 WTPPvDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWEN 107
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 108 GKAIRETlAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIV 187
Cdd:pfam00171 80 GKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 188 LKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGG 266
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 267 KSPSIFFPdvmDADdafREKCIEGLAMFA-LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQA 345
Cdd:pfam00171 239 KNPLIVLE---DAD---LDAAVEAAVFGAfGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 346 SQEQLDKISGYLESGPKEGAEVLTGGNvaklEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIAN 424
Cdd:pfam00171 313 SKAQLERVLKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANvTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIAN 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 425 DTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYH-SYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:pfam00171 389 DTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTtGDADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
20-497 |
0e+00 |
|
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: 579.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 20 YENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKI 99
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 100 AVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPA 179
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 180 LAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIP 259
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 260 ITLELGGKSPSIFFpdvmdaDDAFREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTS 338
Cdd:cd07117 241 ATLELGGKSANIIF------DDANWDKALEGAQLGILfNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 339 VQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPT-IFRGNNSMRFFREEIFGPVLAVTTFKTLD 417
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTlIVNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 418 EALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLVS 497
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYID 474
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
23-493 |
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: 545.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKD--SWASVPAAERALILHRIADRLEENLEKIA 100
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPAL 180
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 181 AAGNCIVLKPAEQTPASILMLTEIIAD-LLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDK-II 258
Cdd:cd07091 167 AAGNTVVLKPAEQTPLSALYLAELIKEaGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 259 PITLELGGKSPSIFFPDVmDADDAFRekciegLAMFAL--NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLD 336
Cdd:cd07091 247 KVTLELGGKSPNIVFDDA-DLDKAVE------WAAFGIffNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 337 TSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGleggYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKT 415
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKG----YFIQPTVFTDvKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896153531 416 LDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKC 493
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKA 473
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
62-492 |
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: 543.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 62 ALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEG-RI 140
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGeVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 141 SQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIAD-LLPDGVLNIVNG 219
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEaGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 220 LGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDADDAfrekcIEGLAMFA-LNQ 298
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDA-DLDAA-----VKGAVFGAfGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 299 GEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGnvaKLEG 378
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 379 LEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVN 457
Cdd:cd07078 313 GGKGYFVPPTVLTDvDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430
....*....|....*....|....*....|....*.
gi 896153531 458 NYHSYP-AHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07078 393 DYSVGAePSAPFGGVKQSGIGREGGPYGLEEYTEPK 428
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
42-492 |
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: 540.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADIPL 121
Cdd:cd07093 4 PATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILML 201
Cdd:cd07093 84 AAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 202 TEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFpdvmdaD 280
Cdd:cd07093 164 AELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVF------A 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 281 DAFREKCIEG-LAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLES 359
Cdd:cd07093 238 DADLDRAVDAaVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 360 GPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRN 438
Cdd:cd07093 318 ARAEGATILTGGGRPELPDLEGGYFVEPTVITGlDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 896153531 439 QNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELK 451
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
42-496 |
0e+00 |
|
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: 537.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKA--KDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDI 119
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA-QV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 120 PLAIDHFRYFAGATRTQEGRISQID-DNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASI 198
Cdd:cd07114 83 RYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 199 LMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDvm 277
Cdd:cd07114 163 LELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 278 dADdafREKCIEGLA--MFAlNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISG 355
Cdd:cd07114 241 -AD---LDAAVNGVVagIFA-AAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 356 YLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGV 434
Cdd:cd07114 316 YVARAREEGARVLTGGERPSGADLGAGYFFEPTILADvTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896153531 435 WSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLV 496
Cdd:cd07114 396 WTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-492 |
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: 523.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 34 GQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDS--WASVPAAERALILHRIADRLEENLEKIAVAETWENGKAI 111
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 112 RETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPA 191
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 192 EQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSD-KIIPITLELGGKSP 269
Cdd:cd07112 161 EQSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 270 SIFFPDVMDADDAfrekcIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQE 348
Cdd:cd07112 241 NIVFADAPDLDAA-----AEAAAAGIFwNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 349 QLDKISGYLESGPKEGAEVLTGGNVAKLEGleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTI 427
Cdd:cd07112 316 HFDKVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGvTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896153531 428 YGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-506 |
0e+00 |
|
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: 519.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDS--WASVPAAERALILHRIADRLEENLEKIA 100
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETlAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPAL 180
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 181 AAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIP 259
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 260 ITLELGGKSPSIFFPDVmDADDAfrekcIEGlAMFA--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDT 337
Cdd:cd07119 240 VALELGGKNPNIVFADA-DFETA-----VDQ-ALNGvfFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 338 SVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTL 416
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDvDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 417 DEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLV 496
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
490
....*....|
gi 896153531 497 SYDENPTGLF 506
Cdd:cd07119 473 NLSPQPIGWF 482
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
42-496 |
6.04e-170 |
|
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: 487.20 E-value: 6.04e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIrETLAADIPL 121
Cdd:cd07090 4 PATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVDIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILML 201
Cdd:cd07090 83 SADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 202 TEIIADL-LPDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDAD 280
Cdd:cd07090 163 AEILTEAgLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA-DLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 281 DAFREkcieglAMFA--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLE 358
Cdd:cd07090 241 NAVNG------AMMAnfLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 359 SGPKEGAEVLTGGNVAKLE-GLEGGYYVEPTIFRGNN-SMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWS 436
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTdDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 437 RNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLV 496
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
39-497 |
4.48e-169 |
|
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: 485.02 E-value: 4.48e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 39 NSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAAD 118
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 119 IPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASI 198
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 199 LMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVm 277
Cdd:cd07115 161 LRIAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 278 DADDAFREkcieglAMFAL--NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISG 355
Cdd:cd07115 240 DLDAAVRA------AATGIfyNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 356 YLESGPKEGAEVLTGGnvaKLEGlEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGV 434
Cdd:cd07115 314 YVDVGREEGARLLTGG---KRPG-ARGFFVEPTIFAAvPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896153531 435 WSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLVS 497
Cdd:cd07115 390 WTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
14-492 |
4.98e-167 |
|
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: 481.14 E-value: 4.98e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 14 FTYKEQYENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKA-KDSWASVPAAERALILHRIADRL 92
Cdd:cd07144 2 KSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 93 EENLEKIAVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMA 172
Cdd:cd07144 82 EKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 173 AWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINK 251
Cdd:cd07144 162 AWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 252 AVSDKIIPITLELGGKSPSIFFpdvmdaDDAFREKCIEGLA---MFalNQGEVCTCPSRALVHEDIADEFLKLAVERVKQ 328
Cdd:cd07144 242 AAAQNLKAVTLECGGKSPALVF------EDADLDQAVKWAAagiMY--NSGQNCTATSRIYVQESIYDKFVEKFVEHVKQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 329 I-KTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKlEGLEGGYYVEPTIFRG-NNSMRFFREEIFGP 406
Cdd:cd07144 314 NyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAP-EGLGKGYFIPPTIFTDvPQDMRIVKEEIFGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 407 VLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLE 486
Cdd:cd07144 393 VVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLE 472
|
....*.
gi 896153531 487 HYQETK 492
Cdd:cd07144 473 TYTQTK 478
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-492 |
1.26e-164 |
|
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: 473.91 E-value: 1.26e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 22 NFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAV 101
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 102 AETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRiSQIDDNTVAyhfHEPLGVVGQIIPWNFPLLMAAWKIAPALA 181
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFE-ERRGNSLVV---REPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 182 AGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPI 260
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 261 TLELGGKSPSIFFPDVmDADDAFREkcieGLAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQ 340
Cdd:cd07138 237 ALELGGKSANIILDDA-DLEKAVPR----GVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 341 MGAQASQEQLDKISGYLESGPKEGAEVLTGGnVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEA 419
Cdd:cd07138 312 LGPLASAAQFDRVQGYIQKGIEEGARLVAGG-PGRPEGLERGYFVKPTVFADvTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896153531 420 LEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNN-YHSYpaHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGaAFNP--GAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
42-496 |
1.45e-163 |
|
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: 471.07 E-value: 1.45e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADIPL 121
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILML 201
Cdd:cd07108 84 LADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 202 TEIIADLLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDADD 281
Cdd:cd07108 164 AEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA-DLDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 282 AfrekcIEG--LAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLES 359
Cdd:cd07108 243 A-----VDGaiAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 360 GPKE-GAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSR 437
Cdd:cd07108 318 GLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGvDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 438 NQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHL-MMLEHYQETKCMLV 496
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLeGMLEHFTQKKTVNI 457
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
23-497 |
1.58e-163 |
|
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: 471.83 E-value: 1.58e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKA--KDS-WASVPAAERALILHRIADRLEENLEKI 99
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAfkLGSpWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 100 AVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPA 179
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 180 LAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKII 258
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 259 P-ITLELGGKSPSIFFPDVmDADDAFrEKCIEGLamFAlNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDT 337
Cdd:cd07141 250 KrVTLELGGKSPNIVFADA-DLDYAV-EQAHEAL--FF-NMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 338 SVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKleglEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTL 416
Cdd:cd07141 325 KTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHG----DKGYFIQPTVFSDvTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 417 DEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLV 496
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 896153531 497 S 497
Cdd:cd07141 481 K 481
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
23-492 |
1.63e-162 |
|
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: 469.28 E-value: 1.63e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKD--SWASVPAAERALILHRIADRLEENLEKIA 100
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPAL 180
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 181 AAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVS-DKII 258
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAkSNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 259 PITLELGGKSPSIFFPDVmDADDAFRekciegLAMFAL--NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLD 336
Cdd:cd07142 247 PVTLELGGKSPFIVCEDA-DVDKAVE------LAHFALffNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 337 TSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKleglEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKT 415
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIG----SKGYYIQPTIFSDvKDDMKIARDEIFGPVQSILKFKT 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896153531 416 LDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
42-492 |
1.75e-161 |
|
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: 465.65 E-value: 1.75e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADIPL 121
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRIS-QIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILM 200
Cdd:cd07092 84 AVDNFRFFAGAARTLEGPAAgEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 201 LTEIIADLLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFpdvmdaD 280
Cdd:cd07092 164 LAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF------D 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 281 DAFREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLES 359
Cdd:cd07092 238 DADLDAAVAGIATAGYyNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 360 GPKeGAEVLTGGnvAKLEGleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRN 438
Cdd:cd07092 318 APA-HARVLTGG--RRAEG--PGYFYEPTVVAGvAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 896153531 439 QNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
42-492 |
2.54e-159 |
|
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: 459.98 E-value: 2.54e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDIPL 121
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG-EVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRI--SQIDDNTVaYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASIL 199
Cdd:cd07103 83 AASFLEWFAEEARRIYGRTipSPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 200 MLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmD 278
Cdd:cd07103 162 ALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDA-D 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 279 ADDAfrekcIEGlAMFA--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGY 356
Cdd:cd07103 241 LDKA-----VDG-AIASkfRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 357 LESGPKEGAEVLTGGNVAKLegleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVW 435
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGL----GGYFYEPTVLTDvTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 896153531 436 SRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETK 447
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
23-492 |
5.98e-159 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 460.46 E-value: 5.98e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKA-KDSWA-SVPAAERALILHRIADRLEENLEKIA 100
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPAL 180
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 181 AAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLI-NKAVSDKII 258
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVmEAAAKSNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 259 PITLELGGKSPSIFFPDVmDADDAFRekcIEGLAMFaLNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTS 338
Cdd:cd07143 250 KVTLELGGKSPNIVFDDA-DLESAVV---WTAYGIF-FNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 339 VQMGAQASQEQLDKISGYLESGPKEGAEVLTGGnvaKLEGLEgGYYVEPTIFRGNNS-MRFFREEIFGPVLAVTTFKTLD 417
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGG---KRHGNE-GYFIEPTIFTDVTEdMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896153531 418 EALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
18-496 |
1.30e-158 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 459.73 E-value: 1.30e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 18 EQYENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLE 97
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 98 KIAVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIA 177
Cdd:PRK13252 85 ELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 178 PALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGtEAGAALTASDRISKIAFTGSTAVGQLINKAVSDK 256
Cdd:PRK13252 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 257 IIPITLELGGKSPSIFFPDvMDADDAFrekcieGLAMFA--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNP 334
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDD-ADLDRAA------DIAMLAnfYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 335 LDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTF 413
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDcTDDMTIVREEIFGPVMSVLTF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 414 KTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKC 493
Cdd:PRK13252 397 DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
...
gi 896153531 494 MLV 496
Cdd:PRK13252 477 VQV 479
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
42-492 |
6.43e-157 |
|
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: 454.00 E-value: 6.43e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWA-SVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETlAADIP 120
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RADVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 121 LAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILM 200
Cdd:cd07109 83 AAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 201 LTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPdvmDA 279
Cdd:cd07109 163 LAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFA---DA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 280 DdafREKCIEGL--AMFAlNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDtSVQMGAQASQEQLDKISGYL 357
Cdd:cd07109 240 D---LEAALPVVvnAIIQ-NAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 358 ESGPKEGAEVLTGGNVAKlEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWS 436
Cdd:cd07109 315 ARARARGARIVAGGRIAE-GAPAGGYFVAPTLLDDvPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896153531 437 RNQNNAYRAARGIQAGRVWVNNYH-----SYPahaaFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNNYGagggiELP----FGGVKKSGHGREKGLEALYNYTQTK 450
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
40-492 |
9.56e-157 |
|
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: 453.72 E-value: 9.56e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 40 STPVTGEVFCRVPRSNEKDIELALDAAHKAKDS--WASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAa 117
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 118 DIPLAIDHFRYFAGATRTQEGRI-SQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGDSyNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 197 SILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPD 275
Cdd:cd07118 161 TTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 276 VmDADDAfrekcIEGLAM-FALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKIS 354
Cdd:cd07118 241 A-DLDAA-----ADAVVFgVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 355 GYLESGPKEGAEVLTGGNVAkleGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAG 433
Cdd:cd07118 315 DYVDAGRAEGATLLLGGERL---ASAAGLFYQPTIFTDvTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAG 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 434 VWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07118 392 VWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELK 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
42-492 |
3.54e-156 |
|
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: 452.19 E-value: 3.54e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETlAADIPL 121
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAG---ATRTQEGRISQIDDNTV-AYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPAS 197
Cdd:cd07110 83 VAGCFEYYADlaeQLDAKAERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 198 ILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFpdv 276
Cdd:cd07110 163 ELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 277 mdaDDAFREKCIEgLAMFAL--NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKIS 354
Cdd:cd07110 240 ---DDADLEKAVE-WAMFGCfwNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 355 GYLESGPKEGAEVLTGGNVAklEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAG 433
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRP--AHLEKGYFIAPTVFADvPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 434 VWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
19-492 |
9.90e-156 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 451.67 E-value: 9.90e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 19 QYENFIDGKWtPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEK 98
Cdd:PRK13473 2 QTKLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 99 IAVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRIS--QIDDNTvAYHFHEPLGVVGQIIPWNFPLLMAAWKI 176
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAgeYLEGHT-SMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 177 APALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDK 256
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 257 IIPITLELGGKSPSIFFpdvmdaDDAFREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPL 335
Cdd:PRK13473 240 VKRTHLELGGKAPVIVF------DDADLDAVVEGIRTFGYyNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 336 DTSVQMGAQASQEQLDKISGYLESGPKEG-AEVLTGGNVAKLegleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTF 413
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDG----KGYYYEPTLLAGaRQDDEIVQREVFGPVVSVTPF 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 414 KTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:PRK13473 390 DDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
15-479 |
7.85e-154 |
|
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: 447.23 E-value: 7.85e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 15 TYKEQYENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEE 94
Cdd:cd07111 17 AHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 95 NLEKIAVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEgrisqiddntVAYHFHEPLGVVGQIIPWNFPLLMAAW 174
Cdd:cd07111 97 HQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD----------TELAGWKPVGVVGQIVPWNFPLLMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 175 KIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGtEAGAALTASDRISKIAFTGSTAVGQLINKAV 253
Cdd:cd07111 167 KICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 254 SDKIIPITLELGGKSPSIFFpDVMDADDAfrekcIEGL--AMFaLNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKT 331
Cdd:cd07111 246 AGTGKKLSLELGGKSPFIVF-DDADLDSA-----VEGIvdAIW-FNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 332 GNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGleggYYVEPTIFRG-NNSMRFFREEIFGPVLAV 410
Cdd:cd07111 319 GDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKG----PFYPPTLFTNvPPASRIAQEEIFGPVLVV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 411 TTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRE 479
Cdd:cd07111 395 LTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGRE 463
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-496 |
3.73e-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: 445.10 E-value: 3.73e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDS--WASVPAAERALILHRIADRLEENLEKIA 100
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAADIPLAIDHFRYFAGATRT---QEGRISQIDDNTVAYHfhEPLGVVGQIIPWNFPLLMAAWKIA 177
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGHVLVRR--EPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 178 PALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDK 256
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 257 IIPITLELGGKSPSIFFPDvmdADDafrEKCIEGLAM-FALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPL 335
Cdd:cd07139 239 LARVTLELGGKSAAIVLDD---ADL---DAAVPGLVPaSLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 336 DTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGnvAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFK 414
Cdd:cd07139 313 DPATQIGPLASARQRERVEGYIAKGRAEGARLVTGG--GRPAGLDRGWFVEPTLFADvDNDMRIAQEEIFGPVLSVIPYD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 415 TLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPaHAAFGGYKQSGIGRENHLMMLEHYQETKCM 494
Cdd:cd07139 391 DEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDF-GAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
..
gi 896153531 495 LV 496
Cdd:cd07139 470 YL 471
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
42-492 |
9.00e-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: 441.30 E-value: 9.00e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWA-SVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADIP 120
Cdd:cd07089 4 PATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 121 LAIDHFRYFAGATRT---QEGRISQIDDNTVAYHF--HEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTP 195
Cdd:cd07089 84 GPIGHLRYFADLADSfpwEFDLPVPALRGGPGRRVvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 196 ASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFP 274
Cdd:cd07089 164 LSALLLGEIIAETdLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 275 DvmdADdaFREKCIEGLAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKIS 354
Cdd:cd07089 244 D---AD--LAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 355 GYLESGPKEGAEVLTGGnvAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAG 433
Cdd:cd07089 319 GYIARGRDEGARLVTGG--GRPAGLDKGFYVEPTLFADvDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 434 VWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-492 |
2.37e-151 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 440.40 E-value: 2.37e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVA 102
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 103 ETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAA 182
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 183 GNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPIT 261
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 262 LELGGKSPSIFFpdvmdaDDAFREKCIEGlAMFA--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSV 339
Cdd:TIGR01804 241 MELGGKSPLIVF------DDADLESAVDG-AMLGnfFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 340 QMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDE 418
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADcTDDMTIVREEIFGPVMTVLTFSDEDE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896153531 419 ALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:TIGR01804 394 VIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
42-496 |
4.29e-149 |
|
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: 433.88 E-value: 4.29e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETlAADIPL 121
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEgRISQIDDNTVAYHfHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILML 201
Cdd:cd07106 83 AVAWLRYTASLDLPDE-VIEDDDTRRVELR-RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 202 TEIIADLLPDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDADD 281
Cdd:cd07106 161 GELAQEVLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV-DIDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 282 AfrekcIEGLAMFA-LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESG 360
Cdd:cd07106 239 V-----APKLFWGAfINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 361 PKEGAEVLTGGNVAKLEglegGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQ 439
Cdd:cd07106 314 KAKGAKVLAGGEPLDGP----GYFIPPTIVDDpPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 896153531 440 NNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLV 496
Cdd:cd07106 390 ERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
21-499 |
3.99e-148 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 433.08 E-value: 3.99e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 21 ENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIA 100
Cdd:TIGR02299 2 GHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAAdIPLAIDHFRYFAG-ATRTQEGRISQIDDNTvAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPA 179
Cdd:TIGR02299 82 VLECLDCGQPLRQTRQQ-VIRAAENFRFFADkCEEAMDGRTYPVDTHL-NYTVRVPVGPVGLITPWNAPFMLSTWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 180 LAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKII 258
Cdd:TIGR02299 160 LAFGNTVVLKPAEWSPLTAARLAEIAKEAgLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADTLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 259 PITLELGGKSPSIFFpdvmdaDDAFREKCIEGLA--MFALNqGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLD 336
Cdd:TIGR02299 240 RFSMELGGKSPVIVF------DDADLERALDAVVfmIFSFN-GERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 337 TSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAK---LEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTT 412
Cdd:TIGR02299 313 PETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrGEDLGRGNYVLPTVFTGaDNHMRIAQEEIFGPVLTVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 413 FKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:TIGR02299 393 FKDEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETK 472
|
....*..
gi 896153531 493 CMLVSYD 499
Cdd:TIGR02299 473 NVALALG 479
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
20-492 |
6.89e-148 |
|
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: 431.67 E-value: 6.89e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 20 YENFIDGKWTPPVDGQYMDNstPV-TGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEK 98
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRN--PSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 99 IAVAETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEGRISQ-IDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIA 177
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 178 PALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDK 256
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 257 IIPITLELGGKSPSIffpdVM-DAD-DAFREKCIEGlAMFalNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNP 334
Cdd:cd07097 238 GARVQLEMGGKNPLV----VLdDADlDLAVECAVQG-AFF--STGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 335 LDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNvaKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTF 413
Cdd:cd07097 311 LDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGE--RLKRPDEGYYLAPALFAGvTNDMRIAREEIFGPVAAVIRV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 414 KTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHS-YPAHAAFGGYKQSGIG-RENHLMMLEHYQET 491
Cdd:cd07097 389 RDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTI 468
|
.
gi 896153531 492 K 492
Cdd:cd07097 469 K 469
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
42-492 |
2.35e-146 |
|
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: 427.18 E-value: 2.35e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDIPL 121
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILML 201
Cdd:cd07107 83 AAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 202 TEIIADLLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDADD 281
Cdd:cd07107 163 AELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA-DPEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 282 AFREkcieglAMFALN---QGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLE 358
Cdd:cd07107 242 AADA------AVAGMNftwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 359 SGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSR 437
Cdd:cd07107 316 SAKREGARLVTGGGRPEGPALEGGFYVEPTVFADvTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 896153531 438 NQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEK 450
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
23-492 |
1.36e-145 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 426.84 E-value: 1.36e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKA-----KDSWASVPAAERALILHRIADRLEENLE 97
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 98 KIAVAETWENGKAIRETlAADIPLAIDHFRYFAGATR----TQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAA 173
Cdd:PLN02467 91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEaldaKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 174 WKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKA 252
Cdd:PLN02467 170 WKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 253 VSDKIIPITLELGGKSPSIFFpdvmdaDDAFREKCIEgLAMFAL--NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIK 330
Cdd:PLN02467 250 AAQMVKPVSLELGGKSPIIVF------DDVDLDKAVE-WAMFGCfwTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 331 TGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGnvAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLA 409
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG--KRPEHLKKGFFIEPTIITDvTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 410 VTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNyhSYP--AHAAFGGYKQSGIGRENHLMMLEH 487
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINC--SQPcfCQAPWGGIKRSGFGRELGEWGLEN 478
|
....*
gi 896153531 488 YQETK 492
Cdd:PLN02467 479 YLSVK 483
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
23-492 |
4.56e-145 |
|
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: 424.37 E-value: 4.56e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVA 102
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 103 ETWENGKAIRETlAADIPLAIDHFRYFAGATRTQEGRISQID-DNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALA 181
Cdd:cd07088 81 IVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 182 AGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPI 260
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 261 TLELGGKSPSIFFPDVmDADDAFRekcieglAMFA---LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDT 337
Cdd:cd07088 240 SLELGGKAPAIVMKDA-DLDLAVK-------AIVDsriINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 338 SVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGlegGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTL 416
Cdd:cd07088 312 ATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEK---GYFYEPTVLTNvRQDMEIVQEEIFGPVLPVVKFSSL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896153531 417 DEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07088 389 DEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
64-492 |
6.35e-145 |
|
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: 420.10 E-value: 6.35e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 64 DAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEG-RISQ 142
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGpELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 143 IDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIAD-LLPDGVLNIVNGLG 221
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEaGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 222 TEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDADDAfrekcIEGLAMFA-LNQGE 300
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDA-DLDAA-----VEGAVFGAfFNAGQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 301 VCTCPSRALVHEDIADEFlklaVERVKQIKTGNPLDtsvqmgaqasqeqldkisgylesgpkegaevltggnvaklegle 380
Cdd:cd06534 234 ICTAASRLLVHESIYDEF----VEKLVTVLVDVDPD-------------------------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 381 ggyyveptifrgnnsMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYH 460
Cdd:cd06534 266 ---------------MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSS 330
|
410 420 430
....*....|....*....|....*....|...
gi 896153531 461 S-YPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd06534 331 IgVGPEAPFGGVKNSGIGREGGPYGLEEYTRTK 363
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
22-499 |
3.37e-143 |
|
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: 419.83 E-value: 3.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 22 NFIDGKWTPPVDGQYMDNSTPVTG-EVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIA 100
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEGRI--SQIDDNTvAYHFHEPLGVVGQIIPWNFPLLMAAWKIAP 178
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETvpSELPNKD-AMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 179 ALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKI 257
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 258 IPITLELGGKSPSIffpdVMDadDAFREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLD 336
Cdd:cd07131 239 KRVALEMGGKNPII----VMD--DADLDLALEGALWSAFgTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 337 TSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKT 415
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDvTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 416 LDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNyhsyP-----AHAAFGGYKQSGIG-RENHLMMLEHYQ 489
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNA----PtigaeVHLPFGGVKKSGNGhREAGTTALDAFT 468
|
490
....*....|
gi 896153531 490 ETKCMLVSYD 499
Cdd:cd07131 469 EWKAVYVDYS 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
6-505 |
6.68e-143 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 421.52 E-value: 6.68e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 6 NPGTPDAIFTYKEQyenFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDS--WASVPAAERAL 83
Cdd:PLN02466 47 EPITPPVQVSYTQL---LINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 84 ILHRIADRLEENLEKIAVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQII 163
Cdd:PLN02466 124 ILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQII 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 164 PWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGS 242
Cdd:PLN02466 204 PWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 243 TAVGQLINK-AVSDKIIPITLELGGKSPSIFFpdvmdaDDAFREKCIEgLAMFAL--NQGEVCTCPSRALVHEDIADEFL 319
Cdd:PLN02466 284 TDTGKIVLElAAKSNLKPVTLELGGKSPFIVC------EDADVDKAVE-LAHFALffNQGQCCCAGSRTFVHERVYDEFV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 320 KLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEglegGYYVEPTIFRG-NNSMRF 398
Cdd:PLN02466 357 EKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSK----GYYIQPTVFSNvQDDMLI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 399 FREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGR 478
Cdd:PLN02466 433 AQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGR 512
|
490 500
....*....|....*....|....*..
gi 896153531 479 ENHLMMLEHYQETKCMLVSYdENPTGL 505
Cdd:PLN02466 513 EKGIYSLNNYLQVKAVVTPL-KNPAWL 538
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
23-502 |
1.89e-142 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 418.84 E-value: 1.89e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKD--SWASVPAAERALILHRIADRLEENLEKIA 100
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPAL 180
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 181 AAGNCIVLKPAEQTPASILMLTEiIADL--LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVS-DKI 257
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAH-LAKLagVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAtSNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 258 IPITLELGGKSPSIFFpdvmdaDDAFREKCIEgLAMFAL--NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPL 335
Cdd:PLN02766 263 KQVSLELGGKSPLLIF------DDADVDMAVD-LALLGIfyNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 336 DTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKleglEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFK 414
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCG----DKGYYIEPTIFTDvTEDMKIAQDEIFGPVMSLMKFK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 415 TLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCM 494
Cdd:PLN02766 412 TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
....*...
gi 896153531 495 LVSYDENP 502
Cdd:PLN02766 492 VTPLYNSP 499
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
22-498 |
4.84e-132 |
|
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: 391.54 E-value: 4.84e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 22 NFIDGKWTPPvDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAV 101
Cdd:cd07086 1 GVIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 102 AETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEGRI--SQIDDNtVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPA 179
Cdd:cd07086 80 LVSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTipSERPGH-RLMEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 180 LAAGNCIVLKPAEQTPASILMLTEIIADLL-----PDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVS 254
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVLeknglPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 255 DKIIPITLELGGKSPSIffpdVMdaDDAFREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGN 333
Cdd:cd07086 237 RRFGRVLLELGGNNAII----VM--DDADLDLAVRAVLFAAVgTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 334 PLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVakLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTT 412
Cdd:cd07086 311 PLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKR--IDGGEPGNYVEPTIVTGvTDDARIVQEETFAPILYVIK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 413 FKTLDEALEIANDTIYGLGAGVWSRNQNNAYRA--ARGIQAGRVWVNNYHS-YPAHAAFGGYKQSGIGRENHLMMLEHYQ 489
Cdd:cd07086 389 FDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQYM 468
|
....*....
gi 896153531 490 ETKCMLVSY 498
Cdd:cd07086 469 RRSTCTINY 477
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
42-492 |
2.25e-130 |
|
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: 386.31 E-value: 2.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKD--SWASVPAAeRALILHRIADRLEENLEKIAVAETWENGKAIRETlAADI 119
Cdd:cd07120 4 PATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEA-RFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 120 PLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASIL 199
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 200 MLTEIIADL--LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDvm 277
Cdd:cd07120 162 AIIRILAEIpsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 278 dAD-DAFREKCIEGLAMFAlnqGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGY 356
Cdd:cd07120 240 -ADlDAALPKLERALTIFA---GQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 357 LESGPKEGAEV-LTGGNVAklEGLEGGYYVEPTIFR-GNNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGV 434
Cdd:cd07120 316 VERAIAAGAEVvLRGGPVT--EGLAKGAFLRPTLLEvDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 896153531 435 WSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYK 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
23-498 |
1.99e-126 |
|
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: 377.17 E-value: 1.99e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDS-WASVPAAERALILHRIADRLEENLEKIAV 101
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 102 AETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRI------SQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWK 175
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsipSMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 176 IAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGtEAGAALTASDRISKIAFTGSTAVGQLINKAVS 254
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 255 DKIIPITLELGGKSPSIFFPDVmDADDAfrekcIEGL--AMFaLNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTG 332
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDA-DIDWV-----VEGLltAGF-LHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 333 NPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGnvaklEGLEG-GYYVEPTI--FRGNNSmRFFREEIFGPVLA 409
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGG-----EALAGeGYFVQPTLvlARSADS-RLMREETFGPVVS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 410 VTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQ 489
Cdd:cd07113 389 FVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYT 468
|
....*....
gi 896153531 490 ETKCMLVSY 498
Cdd:cd07113 469 ELKSVMIRY 477
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-492 |
1.62e-123 |
|
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: 368.01 E-value: 1.62e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 58 DIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGkAIRETLAADIPLAIDHFRYFAGATRTQE 137
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESG-STRPKAAFEVGAAIAILREAAGLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 138 GRISQID-DNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASI-LMLTEIIADL-LPDGVL 214
Cdd:cd07104 80 GEILPSDvPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAgLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 215 NIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDADDAFRekciegLAMF 294
Cdd:cd07104 160 NVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDA-DLDLAVS------AAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 295 A--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGN 372
Cdd:cd07104 233 GafLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 373 VaklEGLeggyYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQA 451
Cdd:cd07104 313 Y---EGL----FYQPTVLSDvTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLET 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 896153531 452 GRVWVNN---YHSypAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07104 386 GMVHINDqtvNDE--PHVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
23-497 |
1.69e-123 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 370.38 E-value: 1.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDS--WASVPAAERALILHRIADRLEENLEKIA 100
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPAL 180
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 181 AAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVG-QLINKAVSDKII 258
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGkQLLKDAGDSNMK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 259 PITLELGGKSPSIFFPDVMDADDAFREKCieglAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTS 338
Cdd:PRK09847 263 RVWLEAGGKSANIVFADCPDLQQAASATA----AGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 339 VQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEgleggyYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLD 417
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAA------AIGPTIFVDvDPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 418 EALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETKCMLVS 497
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
37-492 |
6.03e-121 |
|
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: 362.03 E-value: 6.03e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 37 MDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENG----KAIR 112
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGstygKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 113 ETLaadipLAIDHFRYFAGATRTQEGRISQIDDN-TVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPA 191
Cdd:cd07150 81 ETT-----FTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 192 EQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPS 270
Cdd:cd07150 156 EETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 271 IFFPDVmDADDAFRekciegLAMFA--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQE 348
Cdd:cd07150 236 IVLADA-DLDYAVR------AAAFGafMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 349 QLDKISGYLESGPKEGAEVLTGGNVAkleglegGYYVEPTIFRGNNS-MRFFREEIFGPVLAVTTFKTLDEALEIANDTI 427
Cdd:cd07150 309 QVERIKRQVEDAVAKGAKLLTGGKYD-------GNFYQPTVLTDVTPdMRIFREETFGPVTSVIPAKDAEEALELANDTE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896153531 428 YGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSY-PAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07150 382 YGLSAAILTNDLQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
42-479 |
9.54e-121 |
|
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: 361.53 E-value: 9.54e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDIPL 121
Cdd:cd07149 6 PYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK-EVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRISQID-----DNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07149 85 AIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 197 SILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKiiPITLELGGKSPSIFFPD 275
Cdd:cd07149 165 SALKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLELGSNAAVIVDAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 276 VmDADDAFrEKCIEGlaMFAlNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISG 355
Cdd:cd07149 243 A-DLEKAV-ERCVSG--AFA-NAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 356 YLESGPKEGAEVLTGGNVAkleglegGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGV 434
Cdd:cd07149 318 WVEEAVEGGARLLTGGKRD-------GAILEPTVLTDvPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 896153531 435 WSRNQNNAYRAARGIQAGRVWVNNYHSYPA-HAAFGGYKQSGIGRE 479
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGRE 436
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
15-498 |
7.19e-120 |
|
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: 360.66 E-value: 7.19e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 15 TYKEQYENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKA--KDSWASVPAAERALILHRIADRL 92
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 93 EENLEKIAVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQEGRISQID----DNTVAYHFHEPLGVVGQIIPWNFP 168
Cdd:cd07140 81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 169 LLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQ 247
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 248 LINKAVSDK-IIPITLELGGKSPSIFFPDVmDADDAFRekciEGLAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERV 326
Cdd:cd07140 241 HIMKSCAVSnLKKVSLELGGKSPLIIFADC-DMDKAVR----MGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 327 KQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEglegGYYVEPTIFRG-NNSMRFFREEIFG 405
Cdd:cd07140 316 KKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP----GFFFEPTVFTDvEDHMFIAKEESFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 406 PVLAVTTFKT--LDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLM 483
Cdd:cd07140 392 PIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEE 471
|
490
....*....|....*
gi 896153531 484 MLEHYQETKCMLVSY 498
Cdd:cd07140 472 ALNEYLKTKTVTIEY 486
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
21-494 |
1.59e-119 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 360.16 E-value: 1.59e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 21 ENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIA 100
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRETLAaDIPLAIDHFRYFAG-ATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPA 179
Cdd:PLN02278 106 QLMTLEQGKPLKEAIG-EVAYGASFLEYFAEeAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 180 LAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKII 258
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 259 PITLELGGKSPSIFFPDVmDADDAFRekciEGLAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTS 338
Cdd:PLN02278 265 RVSLELGGNAPFIVFDDA-DLDVAVK----GALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 339 VQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLegleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLD 417
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSL----GGTFYEPTVLGDvTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 418 EALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQETK--CM 494
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKyvCL 494
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
42-492 |
4.17e-118 |
|
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: 355.12 E-value: 4.17e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETlAADIPL 121
Cdd:cd07145 6 PANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RVEVER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRISQIDD-----NTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07145 85 TIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 197 SILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFpd 275
Cdd:cd07145 165 TAIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVL-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 276 vmdaDDAFREKCIEGLAMFA-LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKIS 354
Cdd:cd07145 243 ----KDADLERAVSIAVRGRfENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 355 GYLESGPKEGAEVLTGGNVakleglEGGYYVEPTIFRGNN-SMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAG 433
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTpDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 434 VWSRNQNNAYRAARGIQAGRVWVNNYHSY-PAHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
44-477 |
5.51e-114 |
|
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: 346.52 E-value: 5.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 44 TGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDIPLAI 123
Cdd:cd07124 56 PSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA-DVAEAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 124 DHFRYFAG-ATRTQEGRISQIDDNTVAYhFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLT 202
Cdd:cd07124 135 DFLEYYAReMLRLRGFPVEMVPGEDNRY-VYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 203 EIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVS------DKIIPITLELGGKSPSIffpd 275
Cdd:cd07124 214 EILEEAgLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgqKWLKRVIAEMGGKNAII---- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 276 vMDADdAFREKCIEGLAMFALN-QGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKIS 354
Cdd:cd07124 290 -VDED-ADLDEAAEGIVRSAFGfQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 355 GYLESGPKEGaEVLTGGNVakLEGLEGGYYVEPTIFRGNNSM-RFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAG 433
Cdd:cd07124 368 RYIEIGKSEG-RLLLGGEV--LELAAEGYFVQPTIFADVPPDhRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGG 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 896153531 434 VWSRNQNNAYRAARGIQAGRVWVN--------NYHSypahaaFGGYKQSGIG 477
Cdd:cd07124 445 VFSRSPEHLERARREFEVGNLYANrkitgalvGRQP------FGGFKMSGTG 490
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
41-478 |
9.58e-112 |
|
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: 338.43 E-value: 9.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 41 TPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAiRETLAADIP 120
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 121 LAIDHFRYFAGAT----RTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07099 81 LALEAIDWAARNAprvlAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 197 SILMLTEIIADL-LPDGVLNIVNGLGtEAGAALTASdRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPD 275
Cdd:cd07099 161 VGELLAEAWAAAgPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 276 VmDADDAfrEKCIEGLAMFalNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISG 355
Cdd:cd07099 239 A-DLERA--AAAAVWGAMV--NAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 356 YLESGPKEGAEVLTGGnvakLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGV 434
Cdd:cd07099 314 HVDDAVAKGAKALTGG----ARSNGGGPFYEPTVLTDvPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 896153531 435 WSRNQNNAYRAARGIQAGRVWVNN---YHSYPAhAAFGGYKQSGIGR 478
Cdd:cd07099 390 FSRDLARAEAIARRLEAGAVSINDvllTAGIPA-LPFGGVKDSGGGR 435
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-492 |
2.43e-111 |
|
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: 338.12 E-value: 2.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 26 GKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIA---VA 102
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVewlIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 103 ETweNGKAIRETLAADIPLAIdhFRYFAGATRTQEGRISQID----DNTVayhFHEPLGVVGQIIPWNFPLLMAAWKIAP 178
Cdd:cd07151 81 ES--GSTRIKANIEWGAAMAI--TREAATFPLRMEGRILPSDvpgkENRV---YREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 179 ALAAGNCIVLKPAEQTPASI-LMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDK 256
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAgLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 257 IIPITLELGGKSPSIFFpdvmdaDDAFREKCIEGLAMFA-LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPL 335
Cdd:cd07151 234 LKKVALELGGNNPFVVL------EDADIDAAVNAAVFGKfLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 336 DTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAkleglegGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFK 414
Cdd:cd07151 308 DPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAE-------GNVLEPTVLSDvTNDMEIAREEIFGPVAPIIKAD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 415 TLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNY--HSYPaHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07151 381 DEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQpvNDEP-HVPFGGEKNSGLGRFNGEWALEEFTTDK 459
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
41-491 |
4.47e-107 |
|
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: 326.57 E-value: 4.47e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 41 TPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGK----AIRETLa 116
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrhAFEEVL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 117 aDIPLAIDHFRYFAGA---TRTQEGRISQIDDNTVAYHfhePLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQ 193
Cdd:cd07101 81 -DVAIVARYYARRAERllkPRRRRGAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 194 TPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTasDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIF 272
Cdd:cd07101 157 TALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 273 fpdvmdADDAFREKCIEGL--AMFAlNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQL 350
Cdd:cd07101 235 ------LEDADLDKAAAGAvrACFS-NAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 351 DKISGYLESGPKEGAEVLTGGN-VAKLegleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIY 428
Cdd:cd07101 308 DRVTAHVDDAVAKGATVLAGGRaRPDL----GPYFYEPTVLTGvTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDY 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896153531 429 GLGAGVWSRNQNNAYRAARGIQAGRVWVNNyhSYPA-----HAAFGGYKQSGIGRENHLMMLEHYQET 491
Cdd:cd07101 384 GLNASVWTRDGARGRRIAARLRAGTVNVNE--GYAAawasiDAPMGGMKDSGLGRRHGAEGLLKYTET 449
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
19-496 |
4.53e-106 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 324.65 E-value: 4.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 19 QYENFIDGKWTPPvDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEK 98
Cdd:TIGR03374 1 QHKLLINGELVSG-EGEKQPVYNPATGEVILEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENAQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 99 IAVAETWENGKAIRETLAADIPLAIDHFRYFAGATRTQ---------EGRISQIDdntvayhfHEPLGVVGQIIPWNFPL 169
Cdd:TIGR03374 80 FAELESRNCGKPLHSVFNDEIPAIVDVFRFFAGAARCLsglaageylEGHTSMIR--------RDPLGVVASIAPWNYPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 170 LMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLI 249
Cdd:TIGR03374 152 MMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGKTVGDPLTGHEKVRMVSLTGSIATGEHI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 250 NKAVSDKIIPITLELGGKSPSIFFpdvmdaDDAFREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERVKQ 328
Cdd:TIGR03374 232 LSHTAPSIKRTHMELGGKAPVIVF------DDADIDAVVEGVRTFGFyNAGQDCTAACRIYAQRGIYDTLVEKLGAAVAT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 329 IKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEG-AEVLTGGNvaKLEGleGGYYVEPTIFRG-NNSMRFFREEIFGP 406
Cdd:TIGR03374 306 LKSGAPDDESTELGPLSSLAHLERVMKAVEEAKALGhIKVITGGE--KRKG--NGYYFAPTLLAGaKQDDAIVQKEVFGP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 407 VLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLE 486
Cdd:TIGR03374 382 VVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLE 461
|
490
....*....|
gi 896153531 487 HYQETKCMLV 496
Cdd:TIGR03374 462 DYTVVRHIMV 471
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
19-479 |
7.39e-106 |
|
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: 324.14 E-value: 7.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 19 QYENFIDGKWTPPvDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKA-KDSWASVPAAERALILHRIADRLEENLE 97
Cdd:cd07082 1 QFKYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 98 KIAVAETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEGRISQID-----DNTVAYHFHEPLGVVGQIIPWNFPLLMA 172
Cdd:cd07082 80 EVANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 173 AWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINK 251
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 252 AVSdkIIPITLELGGKSPSIFFPDVmDADDAFREkCIEGLAMFAlnqGEVCTCPSRALVHEDIADEFLKLAVERVKQIKT 331
Cdd:cd07082 239 QHP--MKRLVLELGGKDPAIVLPDA-DLELAAKE-IVKGALSYS---GQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 332 GNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGnvakleGLEGGYYVEPTIFRGNNS-MRFFREEIFGPVLAV 410
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPdMRLAWEEPFGPVLPI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 411 TTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSY-PAHAAFGGYKQSGIGRE 479
Cdd:cd07082 386 IRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRgPDHFPFLGRKDSGIGTQ 455
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
38-491 |
2.71e-105 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 324.52 E-value: 2.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 38 DNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGK----AIRE 113
Cdd:PRK09407 35 EVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKarrhAFEE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 114 TLaaDIPLAIDHFRYFAG---ATRTQEGRISQIDDNTVAYHfhePLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKP 190
Cdd:PRK09407 115 VL--DVALTARYYARRAPkllAPRRRAGALPVLTKTTELRQ---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 191 AEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTasDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSP 269
Cdd:PRK09407 190 DSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 270 SIFfpdvmdADDAFREKCIEGL--AMFAlNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQ 347
Cdd:PRK09407 268 MIV------LDDADLDKAAAGAvrACFS-NAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 348 EQLDKISGYLESGPKEGAEVLTGGNV-AKLegleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIAND 425
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGATVLAGGKArPDL----GPLFYEPTVLTGvTPDMELAREETFGPVVSVYPVADVDEAVERAND 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 426 TIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYH--SYPAHAA-FGGYKQSGIGRENHLMMLEHYQET 491
Cdd:PRK09407 417 TPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYaaAWGSVDApMGGMKDSGLGRRHGAEGLLKYTES 485
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-479 |
5.52e-105 |
|
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: 320.18 E-value: 5.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 59 IELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDIPLAIDHFRYFA--GATRTQ 136
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAenAEAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 137 EGRISQIDDNtvAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLN 215
Cdd:cd07100 80 DEPIETDAGK--AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPEGVFQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 216 IVNgLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIffpdVM-DAD-DAFREKCIEGlAM 293
Cdd:cd07100 158 NLL-IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFI----VLdDADlDKAVKTAVKG-RL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 294 faLNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNv 373
Cdd:cd07100 232 --QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 374 aKLEGleGGYYVEPTIFRGNNS-MRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAG 452
Cdd:cd07100 309 -RPDG--PGAFYPPTVLTDVTPgMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAG 385
|
410 420
....*....|....*....|....*..
gi 896153531 453 RVWVNNYHSYPAHAAFGGYKQSGIGRE 479
Cdd:cd07100 386 MVFINGMVKSDPRLPFGGVKRSGYGRE 412
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
42-496 |
2.41e-103 |
|
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: 316.88 E-value: 2.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETlAADIPL 121
Cdd:cd07147 6 PYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RGEVAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRISQID-----DNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07147 85 AIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 197 SILMLTEIIAD-LLPDGVLNIVNgLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKiiPITLELGGKSPSIFFPD 275
Cdd:cd07147 165 SALILGEVLAEtGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 276 VmDADDAfrekcIEGLAMFALNQ-GEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKIS 354
Cdd:cd07147 242 A-DLDFA-----AQRIIFGAFYQaGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 355 GYLESGPKEGAEVLTGGNVAkleglegGYYVEPTIF-RGNNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAG 433
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGKRD-------GALLEPTILeDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896153531 434 VWSRNQNNAYRAARGIQAGRVWVNNYHSYPA-HAAFGGYKQSGIGRENHLMMLEHYQETKCMLV 496
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
22-477 |
1.35e-102 |
|
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: 316.00 E-value: 1.35e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 22 NFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAV 101
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 102 AETWENGKAIRETLaADIPLAIDHFRYFAGATRTQEGRISQ-----IDdntvAYHFHEPLGVVGQIIPWNFPLLMAAWKI 176
Cdd:cd07085 83 LITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnvargID----TYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 177 APALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLI------ 249
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIyeraaa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 250 -NKAVsdkiipitLELGG-KSPSIFFPdvmDADdafREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERV 326
Cdd:cd07085 237 nGKRV--------QALGGaKNHAVVMP---DAD---LEQTANALVGAAFgAAGQRCMALSVAVAVGDEADEWIPKLVERA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 327 KQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFG 405
Cdd:cd07085 303 KKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNvTPDMKIYKEEIFG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 406 PVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVN-------NYHSypahaaFGGYKQSGIG 477
Cdd:cd07085 383 PVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpipvplAFFS------FGGWKGSFFG 455
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
37-492 |
6.34e-98 |
|
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: 303.20 E-value: 6.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 37 MDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLA 116
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 117 aDIPLAIDHFRYFAGATRTQEGR-----ISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPA 191
Cdd:cd07094 81 -EVDRAIDTLRLAAEEAERIRGEeipldATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 192 EQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKiiPITLELGGKSPS 270
Cdd:cd07094 160 SKTPLSALELAKILVEAgVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGK--RIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 271 IFFPdvmDAD-DAFREKCIEGLAMFAlnqGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQ 349
Cdd:cd07094 238 IVDR---DADlDAAIEALAKGGFYHA---GQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 350 LDKISGYLESGPKEGAEVLTGGnvaKLEGLeggyYVEPTIFRGN-NSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIY 428
Cdd:cd07094 312 AERVERWVEEAVEAGARLLCGG---ERDGA----LFKPTVLEDVpRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDY 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896153531 429 GLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPA-HAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07094 385 GLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEK 449
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-492 |
1.21e-97 |
|
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: 301.42 E-value: 1.21e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 58 DIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGkAIRETLAADIPLAIDHFRYFAG-ATRTQ 136
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-ATAAWAGFNVDLAAGMLREAASlITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 137 EGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLN 215
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 216 IVNGLGTEAGA---ALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDvmdAD-DAFREKCIEGl 291
Cdd:cd07105 160 VVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLED---ADlDAAANAALFG- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 292 AMfaLNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGnpldtSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGG 371
Cdd:cd07105 236 AF--LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 372 NVaklEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQ 450
Cdd:cd07105 309 LA---DESPSGTSMPPTILDNvTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 896153531 451 AGRVWVN--NYHSYPaHAAFGGYKQSGIGRENHLMMLEHYQETK 492
Cdd:cd07105 386 SGAVHINgmTVHDEP-TLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
44-475 |
4.50e-97 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 303.01 E-value: 4.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 44 TGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETlAADIPLAI 123
Cdd:PRK03137 60 KSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA-DADTAEAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 124 DHFRYFA-GATRTQEGR-ISQIDDNTVAYhFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILML 201
Cdd:PRK03137 139 DFLEYYArQMLKLADGKpVESRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 202 TEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKaVSDKIIP-------ITLELGGKSPSIFF 273
Cdd:PRK03137 218 VEVLEEAgLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE-RAAKVQPgqiwlkrVIAEMGGKDAIVVD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 274 PDVmDADDAfrekcIEGLAMFALN-QGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVqMGAQASQEQLDK 352
Cdd:PRK03137 297 EDA-DLDLA-----AESIVASAFGfSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAY-MGPVINQASFDK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 353 ISGYLESGPKEGaEVLTGGNvaklEGLEGGYYVEPTIFRGNNSM-RFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLG 431
Cdd:PRK03137 370 IMSYIEIGKEEG-RLVLGGE----GDDSKGYFIQPTIFADVDPKaRIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLT 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 896153531 432 AGVWSRNQNNAYRAARGIQAGRVWVN--------NYHsypahaAFGGYKQSG 475
Cdd:PRK03137 445 GAVISNNREHLEKARREFHVGNLYFNrgctgaivGYH------PFGGFNMSG 490
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
85-499 |
1.48e-95 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 295.49 E-value: 1.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 85 LHRIADRLEENLEKIAVAETWENGKaIRETLAADIPLAIDHFRYFAGATRTQEGRISQID-DNTVAYHFHEPLGVVGQII 163
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK-IQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDrPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 164 PWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGS 242
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 243 TAVGQLINKAVSDKIIPITLELGGKSPSIffpdVM-DADDAFREKCIegLAMFALNQGEVCTCPSRALVHEDIADEFLKL 321
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAI----VMdDADLDLAVKAI--VDSRVINSGQVCNCAERVYVQKGIYDQFVNR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 322 AVERVKQIKTGNPLDTS-VQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKleglEGGYYVEPTIFRG-NNSMRFF 399
Cdd:PRK10090 234 LGEAMQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDvRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 400 REEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNyHSYPAHAAF-GGYKQSGIGR 478
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR-ENFEAMQGFhAGWRKSGIGG 388
|
410 420
....*....|....*....|.
gi 896153531 479 ENHLMMLEHYQETKCMLVSYD 499
Cdd:PRK10090 389 ADGKHGLHEYLQTQVVYLQSD 409
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
41-477 |
2.64e-95 |
|
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: 296.08 E-value: 2.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 41 TPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETlAADIP 120
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 121 LAIDHFRYF----AGATRTQEGrisQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07102 81 GMLERARYMisiaEEALADIRV---PEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 197 SILMLTEIIAD-LLPDGVLNIVNgLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPD 275
Cdd:cd07102 158 CGERFAAAFAEaGLPEGVFQVLH-LSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 276 VmDADDAFrEKCIEGlAMFalNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISG 355
Cdd:cd07102 237 A-DLDAAA-ESLVDG-AFF--NSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 356 YLESGPKEGAEVLTGGNVAKlEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGV 434
Cdd:cd07102 312 QIADAIAKGARALIDGALFP-EDKAGGAYLAPTVLTNvDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 896153531 435 WSRNQNNAYRAARGIQAGRVWVN--NYHSyPAhAAFGGYKQSGIG 477
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNrcDYLD-PA-LAWTGVKDSGRG 433
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
45-477 |
2.05e-94 |
|
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: 293.82 E-value: 2.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 45 GEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGkAIRETLAADIPLAID 124
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-SIRPKAGFEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 125 HFRYFAGATRTQEGRISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASI-LMLTE 203
Cdd:cd07152 80 ELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 204 IIADL-LPDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDvmdADDA 282
Cdd:cd07152 160 LFEEAgLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDD---ADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 283 FREKCIEGLAMfaLNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPK 362
Cdd:cd07152 236 LAASNGAWGAF--LHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 363 EGAEVLTGGNVakleglEGGYYvEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNN 441
Cdd:cd07152 314 AGARLEAGGTY------DGLFY-RPTVLSGvKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGR 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 896153531 442 AYRAARGIQAGRVWVNNYH-SYPAHAAFGGYKQSGIG 477
Cdd:cd07152 387 AMALADRLRTGMLHINDQTvNDEPHNPFGGMGASGNG 423
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
42-478 |
3.74e-88 |
|
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: 278.03 E-value: 3.74e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADIPL 121
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAG----ATRTQE---GRISQIDDNTVAYHfhePLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQT 194
Cdd:cd07098 83 TCEKIRWTLKhgekALRPESrpgGLLMFYKRARVEYE---PLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 195 PASILMLTEIIADLL------PDGVLnIVNGLGtEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKS 268
Cdd:cd07098 160 AWSSGFFLSIIRECLaacghdPDLVQ-LVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 269 PSIFFPDVmDADDafrekcIEGLAMFA--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQAS 346
Cdd:cd07098 238 PAIVLDDA-DLDQ------IASIIMRGtfQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 347 QEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIAND 425
Cdd:cd07098 311 PARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDvTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANS 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 896153531 426 TIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNY-HSYPAHA-AFGGYKQSGIGR 478
Cdd:cd07098 391 TEYGLGASVFGKDIKRARRIASQLETGMVAINDFgVNYYVQQlPFGGVKGSGFGR 445
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
42-479 |
1.46e-87 |
|
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: 276.16 E-value: 1.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKdswASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAaDIPL 121
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAASYR---STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY-EVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AIDHFRYFAGATRTQEGRISQIDDNT-----VAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 197 SILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLInkAVSDKIIPITLELGGKSPSIFFPD 275
Cdd:cd07146 162 SAIYLADLLYEAgLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 276 VmDADDAFREKCIEGLAmfalNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISG 355
Cdd:cd07146 240 A-DLERAATLAVAGSYA----NSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 356 YLESGPKEGAEVLTGGnvakleGLEGGYYvEPTIF-RGNNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGV 434
Cdd:cd07146 315 RVEEAIAQGARVLLGN------QRQGALY-APTVLdHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 896153531 435 WSRNQNNAYRAARGIQAGRVWVNNYHSYPA-HAAFGGYKQSGIG-RE 479
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNEVPGFRSeLSPFGGVKDSGLGgKE 434
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
25-479 |
4.13e-84 |
|
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: 267.92 E-value: 4.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 25 DGKWTPPvdGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAET 104
Cdd:cd07130 4 DGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 105 WENGKAIRETLAaDIPLAIDHFRYFAGATRTQEGRI--SQIDDNTVAYHFHePLGVVGQIIPWNFPLLMAAWKIAPALAA 182
Cdd:cd07130 82 LEMGKILPEGLG-EVQEMIDICDFAVGLSRQLYGLTipSERPGHRMMEQWN-PLGVVGVITAFNFPVAVWGWNAAIALVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 183 GNCIVLKPAEQTPASILMLTEIIADLL-----PDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKI 257
Cdd:cd07130 160 GNVVVWKPSPTTPLTAIAVTKIVARVLeknglPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 258 IPITLELGGKSPSIFFPDVmDADDAFREkcieglAMFAL--NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPL 335
Cdd:cd07130 239 GRSLLELGGNNAIIVMEDA-DLDLAVRA------VLFAAvgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 336 DTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVakLEGleGGYYVEPTIFRGNNSMRFFREEIFGPVLAVTTFKT 415
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKV--IDG--PGNYVEPTIVEGLSDAPIVKEETFAPILYVLKFDT 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896153531 416 LDEALEIANDTIYGLGAGVWSRNQNNAYR--AARGIQAGRVWVNNYHSyPAH--AAFGGYKQSGIGRE 479
Cdd:cd07130 388 LEEAIAWNNEVPQGLSSSIFTTDLRNAFRwlGPKGSDCGIVNVNIGTS-GAEigGAFGGEKETGGGRE 454
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
23-497 |
8.53e-84 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 267.54 E-value: 8.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVA 102
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 103 ETWENGKAIRETlAADIPLAIDHFRYFAgatrtQEGRisQIDDNTVAYH--------FHEPLGVVGQIIPWNFPLLMAAW 174
Cdd:PRK11241 94 MTLEQGKPLAEA-KGEISYAASFIEWFA-----EEGK--RIYGDTIPGHqadkrlivIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 175 KIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVG-QLINKA 252
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGrQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 253 VSDkIIPITLELGGKSPSIFFpdvmdaDDAFREKCIEG-LAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKT 331
Cdd:PRK11241 246 AKD-IKKVSLELGGNAPFIVF------DDADLDKAVEGaLASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 332 GNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLegleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAV 410
Cdd:PRK11241 319 GDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL----GGNFFQPTILVDvPANAKVAKEETFGPLAPL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 411 TTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRENHLMMLEHYQE 490
Cdd:PRK11241 395 FRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLE 474
|
....*..
gi 896153531 491 TKCMLVS 497
Cdd:PRK11241 475 IKYMCIG 481
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
12-477 |
9.39e-83 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 265.58 E-value: 9.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 12 AIFTYKEQYenfidGKWTPPV-DGQYMDNSTPV-------TGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERAL 83
Cdd:TIGR01237 21 ALATVKEQL-----GKTYPLViNGERVETENKIvsinpcdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 84 ILHRIADRLEENLEKIAVAETWENGKAIRETlAADIPLAIDHFRYFA---------GATRTQEGRISQiddntvayHFHE 154
Cdd:TIGR01237 96 ILFKAAAIVRRRRHEFSALLVKEVGKPWNEA-DAEVAEAIDFMEYYArqmielakgKPVNSREGETNQ--------YVYT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 155 PLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEI-IADLLPDGVLNIVNGLGTEAGAALTASDR 233
Cdd:TIGR01237 167 PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEIlEEAGLPKGVVQFVPGSGSEVGDYLVDHPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 234 ISKIAFTGSTAVGQLINkAVSDKIIP-------ITLELGGKSPSIffpdvMDaDDAFREKCIEGLAMFALN-QGEVCTCP 305
Cdd:TIGR01237 247 TSLITFTGSREVGTRIF-ERAAKVQPgqkhlkrVIAEMGGKDTVI-----VD-EDADIELAAQSAFTSAFGfAGQKCSAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 306 SRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGaEVLTGGNVAKLEglegGYYV 385
Cdd:TIGR01237 320 SRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSK----GYFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 386 EPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVN------- 457
Cdd:TIGR01237 395 GPTIFADvDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnitgai 474
|
490 500
....*....|....*....|.
gi 896153531 458 -NYHsypahaAFGGYKQSGIG 477
Cdd:TIGR01237 475 vGYQ------PFGGFKMSGTD 489
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
17-485 |
3.15e-79 |
|
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: 256.74 E-value: 3.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 17 KEQYENFIDGKW--TPPVDGQYMDNST--PV-----TGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHR 87
Cdd:cd07125 20 ADALKAFDEKEWeaIPIINGEETETGEgaPVidpadHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 88 IADRLEENLEK---IAVAETwenGKAIRETLAaDIPLAIDHFRYFAGATRTQ--EGRISQIDDNTVAYHFHePLGVVGQI 162
Cdd:cd07125 100 AADLLEANRGEliaLAAAEA---GKTLADADA-EVREAIDFCRYYAAQARELfsDPELPGPTGELNGLELH-GRGVFVCI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 163 IPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTG 241
Cdd:cd07125 175 SPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAgVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 242 STAVGQLINKAVSDK---IIPITLELGGKspsiffpDVMDADD-AFREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIAD 316
Cdd:cd07125 255 STETAKLINRALAERdgpILPLIAETGGK-------NAMIVDStALPEQAVKDVVQSAFgSAGQRCSALRLLYLQEEIAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 317 EFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTggnvAKLEGLEgGYYVEPTIFRGNNSm 396
Cdd:cd07125 328 RFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAP----APLDDGN-GYFVAPGIIEIVGI- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 397 RFFREEIFGPVLAVTTFK--TLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNN------YHSYPahaaF 468
Cdd:cd07125 402 FDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRnitgaiVGRQP----F 477
|
490 500
....*....|....*....|.
gi 896153531 469 GGYKQSGIGRE----NHLMML 485
Cdd:cd07125 478 GGWGLSGTGPKaggpNYLLRF 498
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
42-479 |
3.18e-77 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 249.65 E-value: 3.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADIPL 121
Cdd:PRK09406 8 PATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 122 AiDHFRYFA-----------------GATRtqegrisqiddntvAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGN 184
Cdd:PRK09406 88 A-KGFRYYAehaealladepadaaavGASR--------------AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 185 CIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNgLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPITLE 263
Cdd:PRK09406 153 VGLLKHASNVPQTALYLADLFRRAgFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 264 LGGKSPSIFFPDvmdADdafrekcIEGLAMFAL-----NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTS 338
Cdd:PRK09406 232 LGGSDPFIVMPS---AD-------LDRAAETAVtarvqNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 339 VQMGAQASQEQLDKISGYLESGPKEGAEVLTGGnvaklEGLEG-GYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTL 416
Cdd:PRK09406 302 TDVGPLATEQGRDEVEKQVDDAVAAGATILCGG-----KRPDGpGWFYPPTVITDiTPDMRLYTEEVFGPVASLYRVADI 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896153531 417 DEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYH-SYPAhAAFGGYKQSGIGRE 479
Cdd:PRK09406 377 DEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTvSYPE-LPFGGVKRSGYGRE 439
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
15-477 |
1.03e-70 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 233.62 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 15 TYKEQYENFIDGKWTPPVDGQYMDNSTPvTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEE 94
Cdd:cd07083 14 EFGRAYPLVIGGEWVDTKERMVSVSPFA-PSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 95 NLEKIAVAETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEGRISQI-----DDNTVayhFHEPLGVVGQIIPWNFPL 169
Cdd:cd07083 93 RRRELIATLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPAVEVvpypgEDNES---FYVGLGAGVVISPWNFPV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 170 LMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQL 248
Cdd:cd07083 169 AIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 249 INKAVSDK------IIPITLELGGKSpSIFFPDVMDADDAfrekcIEGLAMFALN-QGEVCTCPSRALVHEDIADEFLKL 321
Cdd:cd07083 249 IYEAAARLapgqtwFKRLYVETGGKN-AIIVDETADFELV-----VEGVVVSAFGfQGQKCSAASRLILTQGAYEPVLER 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 322 AVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGgnvAKLEGLegGYYVEPTIFRGNN-SMRFFR 400
Cdd:cd07083 323 LLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGG---KRLEGE--GYFVAPTVVEEVPpKARIAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 401 EEIFGPVLAVTTFKTLD--EALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYH--SYPAHAAFGGYKQSGI 476
Cdd:cd07083 398 EEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKItgALVGVQPFGGFKLSGT 477
|
.
gi 896153531 477 G 477
Cdd:cd07083 478 N 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
23-480 |
2.51e-68 |
|
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: 227.07 E-value: 2.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVA 102
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 103 ETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEGRIS-QIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALA 181
Cdd:TIGR01722 84 ITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETStQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 182 AGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIIPI 260
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 261 TLELGGKSPSIFFPdvmdadDAFREKCIEGLAMFALNQ-GEVCTCPSRA-LVHEdiADEFLKLAVERVKQIKTGNPLDTS 338
Cdd:TIGR01722 242 QALGGAKNHMVVMP------DADKDAAADALVGAAYGAaGQRCMAISAAvLVGA--ADEWVPEIRERAEKIRIGPGDDPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 339 VQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLD 417
Cdd:TIGR01722 314 AEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERvPPTMKAYQEEIFGPVLCVLEADTLE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 418 EALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVN-------NYHSypahaaFGGYKQSGIGREN 480
Cdd:TIGR01722 394 EAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNvpipvplPYFS------FTGWKDSFFGDHH 457
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
42-479 |
2.53e-68 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 226.28 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLA--ADI 119
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAevAKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 120 PLAIDHFRYFAGATRTQEGRISQIDDNTVAYhfhEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASIL 199
Cdd:PRK13968 94 ANLCDWYAEHGPAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 200 MLTEIIADL-LPDGVLNIVNGlgTEAGAALTASD-RISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVm 277
Cdd:PRK13968 171 LIAQVFKDAgIPQGVYGWLNA--DNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 278 DADDAFREkcieGLAMFALNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYL 357
Cdd:PRK13968 248 DLELAVKA----AVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 358 ESGPKEGAEVLTGGNvaKLEGlEGGYYVePTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWS 436
Cdd:PRK13968 324 EATLAEGARLLLGGE--KIAG-AGNYYA-PTVLANvTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFT 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 896153531 437 RNQNNAYRAARGIQAGRVWVNNYHSYPAHAAFGGYKQSGIGRE 479
Cdd:PRK13968 400 TDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-478 |
2.74e-66 |
|
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: 220.22 E-value: 2.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 58 DIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETL------AADIPLAIDhfryfAG 131
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQtevaamAGKIDISIK-----AY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 132 ATRTQEGRISQIDDNTVAYHfhEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LP 210
Cdd:cd07095 76 HERTGERATPMAQGRAVLRH--RPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 211 DGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVS---DKIipITLELGGKSPSIFFpDVMDADDAFREkC 287
Cdd:cd07095 154 PGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAgrpGKI--LALEMGGNNPLVVW-DVADIDAAAYL-I 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 288 IEGLAMFAlnqGEVCTCPSRALVHED-IADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISgylesgpKEGAE 366
Cdd:cd07095 229 VQSAFLTA---GQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYL-------LAQQD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 367 VLTGGNVAKLE---GLEGGYYVEPTIFRGNNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAY 443
Cdd:cd07095 299 LLALGGEPLLAmerLVAGTAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFE 378
|
410 420 430
....*....|....*....|....*....|....*.
gi 896153531 444 RAARGIQAGRVWVNNYHSYPAHAA-FGGYKQSGIGR 478
Cdd:cd07095 379 RFLARIRAGIVNWNRPTTGASSTApFGGVGLSGNHR 414
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
74-478 |
4.61e-66 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 219.32 E-value: 4.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 74 ASVPAAERALILHRIADRLEENLEKIAVA----------ETWENgkairET--LAADIPLAIDHFRYFAGATRTQEGRIS 141
Cdd:cd07087 15 KTRSLEWRKAQLKALKRMLTENEEEIAAAlyadlgkppaEAYLT-----EIavVLGEIDHALKHLKKWMKPRRVSVPLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 142 QIDDntvAYHFHEPLGVVGQIIPWNFPLLMAawkIAP---ALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVN 218
Cdd:cd07087 90 QPAK---AYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 219 GlGTEAGAALTAsDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDvMDADDAFRE----KCieglamf 294
Cdd:cd07087 164 G-GVEVATALLA-EPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKD-ANLEVAARRiawgKF------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 295 aLNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDtSVQMGAQASQEQLDKISGYLESGpkegaEVLTGGNVA 374
Cdd:cd07087 234 -LNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKE-SPDYGRIINERHFDRLASLLDDG-----KVVIGGQVD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 375 KlegleGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGR 453
Cdd:cd07087 307 K-----EERYIAPTILDDvSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGG 381
|
410 420
....*....|....*....|....*..
gi 896153531 454 VWVN--NYHSYPAHAAFGGYKQSGIGR 478
Cdd:cd07087 382 VCVNdvLLHAAIPNLPFGGVGNSGMGA 408
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
54-457 |
5.95e-64 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 225.20 E-value: 5.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 54 SNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEK---IAVAE---TWENGKA-IREtlaadiplAIDHF 126
Cdd:COG4230 590 ATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAElmaLLVREagkTLPDAIAeVRE--------AVDFC 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 127 RYFAGATRTQEGrisqiddntvAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPasilmlteIIA 206
Cdd:COG4230 662 RYYAAQARRLFA----------APTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTP--------LIA 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 207 ----DLL-----PDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDK---IIPITLELGGKspsiffp 274
Cdd:COG4230 724 aravRLLheagvPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARdgpIVPLIAETGGQ------- 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 275 DVMDAD----------D----AFRekcieglamfalNQGEVCTcpsrAL----VHEDIADEFLKLAVERVKQIKTGNPLD 336
Cdd:COG4230 797 NAMIVDssalpeqvvdDvlasAFD------------SAGQRCS----ALrvlcVQEDIADRVLEMLKGAMAELRVGDPAD 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 337 TSVQMGAQASQEQLDKISGYLESGPKEGAEVltgGNVAKLEGLEGGYYVEPTIFRgNNSMRFFREEIFGPVLAVTTFK-- 414
Cdd:COG4230 861 LSTDVGPVIDAEARANLEAHIERMRAEGRLV---HQLPLPEECANGTFVAPTLIE-IDSISDLEREVFGPVLHVVRYKad 936
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 896153531 415 TLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVN 457
Cdd:COG4230 937 ELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
18-457 |
2.31e-63 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 222.77 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 18 EQYENFIDGKW--TPPVDGQymDNSTPV-----TGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIAD 90
Cdd:PRK11904 541 AAIAAFLEKQWqaGPIINGE--GEARPVvspadRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAAD 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 91 RLEENLEK---IAVAE---TWENGKA-IREtlaadiplAIDHFRYFAGATRTQEGRISQI-----DDNTVAYHfhePLGV 158
Cdd:PRK11904 619 LLEANRAEliaLCVREagkTLQDAIAeVRE--------AVDFCRYYAAQARRLFGAPEKLpgptgESNELRLH---GRGV 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 159 VGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPasilmlteIIADL---------LPDGVLNIVNGLGTEAGAALT 229
Cdd:PRK11904 688 FVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTP--------LIAAEavkllheagIPKDVLQLLPGDGATVGAALT 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 230 ASDRISKIAFTGSTAVGQLINKAVSDK---IIPITLELGGKSPSIffpdvMD--------ADD----AFR---EKCIegl 291
Cdd:PRK11904 760 ADPRIAGVAFTGSTETARIINRTLAARdgpIVPLIAETGGQNAMI-----VDstalpeqvVDDvvtsAFRsagQRCS--- 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 292 amfALnqgevctcpsRAL-VHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGA---QASQEQLDKisgYLESGPKEgAEV 367
Cdd:PRK11904 832 ---AL----------RVLfVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPvidAEAKANLDA---HIERMKRE-ARL 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 368 LTGGNVAklEGLEGGYYVEPTIFRgNNSMRFFREEIFGPVLAVTTFKT--LDEALEIANDTIYGLGAGVWSRNQNNAYRA 445
Cdd:PRK11904 895 LAQLPLP--AGTENGHFVAPTAFE-IDSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRI 971
|
490
....*....|..
gi 896153531 446 ARGIQAGRVWVN 457
Cdd:PRK11904 972 ADRVRVGNVYVN 983
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
78-478 |
2.62e-62 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 209.65 E-value: 2.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 78 AAERALILHRIADRLEENLEKIAVA-ETWENGKAIRETLAADIPLAIDHFRY-------------------FAGATrtqe 137
Cdd:cd07133 19 LEERRDRLDRLKALLLDNQDALAEAiSADFGHRSRHETLLAEILPSIAGIKHarkhlkkwmkpsrrhvgllFLPAK---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 138 grisqiddntvAYHFHEPLGVVGQIIPWNFPLLMAawkIAP---ALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVL 214
Cdd:cd07133 95 -----------AEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 215 NIVNGlGTEAGAALTAS--DrisKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDvMDADDAFRekCIegla 292
Cdd:cd07133 161 AVVTG-GADVAAAFSSLpfD---HLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPD-ADLAKAAE--RI---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 293 MFA--LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQI---KTGNPLDTSVqmgaqASQEQLDKISGYLESGPKEGAEV 367
Cdd:cd07133 230 AFGklLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPDYTSI-----INERHYARLQGLLEDARAKGARV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 368 LTGGNVAklEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAA 446
Cdd:cd07133 305 IELNPAG--EDFAATRKLPPTLVLNvTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVL 382
|
410 420 430
....*....|....*....|....*....|....
gi 896153531 447 RGIQAGRVWVNN--YHSYPAHAAFGGYKQSGIGR 478
Cdd:cd07133 383 RRTHSGGVTINDtlLHVAQDDLPFGGVGASGMGA 416
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
23-479 |
6.46e-61 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 208.15 E-value: 6.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWTppVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVA 102
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 103 ETWENGKAIRETLAaDIPLAIDHFRYFAGATRTQEGRISQID-DNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALA 181
Cdd:PLN02315 102 VSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 182 AGNCIVLKPAEQTPASILMLTEIIADLL-----PDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDK 256
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMTKLVAEVLeknnlPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 257 IIPITLELGGKSPSIffpdVMDADD---AFREkcieglAMFAL--NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKT 331
Cdd:PLN02315 260 FGKCLLELSGNNAII----VMDDADiqlAVRS------VLFAAvgTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 332 GNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGleggYYVEPTIFRGNNSMRFFREEIFGPVLAVT 411
Cdd:PLN02315 330 GDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEG----NFVQPTIVEISPDADVVKEELFGPVLYVM 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896153531 412 TFKTLDEALEIANDTIYGLGAGVWSRNQNNAYR--AARGIQAGRVWVNnyhsYPAH-----AAFGGYKQSGIGRE 479
Cdd:PLN02315 406 KFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKwiGPLGSDCGIVNVN----IPTNgaeigGAFGGEKATGGGRE 476
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
33-457 |
2.51e-60 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 214.73 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 33 DGQYMDNSTPV-----TGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEK---IAVAE- 103
Cdd:PRK11905 561 GGDVDGGTRPVlnpadHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPElfaLAVREa 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 104 --TWENGKA-IREtlaadiplAIDHFRYFA-GATRTQEGRIsqiddntvayhfHEPLGVVGQIIPWNFPLLMAAWKIAPA 179
Cdd:PRK11905 641 gkTLANAIAeVRE--------AVDFLRYYAaQARRLLNGPG------------HKPLGPVVCISPWNFPLAIFTGQIAAA 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 180 LAAGNCIVLKPAEQTPasiLMLTEIIADL----LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSD 255
Cdd:PRK11905 701 LVAGNTVLAKPAEQTP---LIAARAVRLLheagVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAK 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 256 ---KIIPITLELGGKSPSIffpdvMDA--------DD----AFR---EKCIeglamfALnqgevctcpsRAL-VHEDIAD 316
Cdd:PRK11905 778 rsgPPVPLIAETGGQNAMI-----VDSsalpeqvvADviasAFDsagQRCS------AL----------RVLcLQEDVAD 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 317 EFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESGPKEGAEVLTggnVAKLEGLEGGYYVEPTIFRGNNsM 396
Cdd:PRK11905 837 RVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQ---LPLPAETEKGTFVAPTLIEIDS-I 912
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896153531 397 RFFREEIFGPVLAVTTFKT--LDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVN 457
Cdd:PRK11905 913 SDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
42-477 |
7.14e-58 |
|
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: 198.80 E-value: 7.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 42 PVTGEVFCRVPRSNEKDIELALDAA---HKAKDSWasVPAAERALILHRIADRLEENLEKIAVAETWENGK----AIRET 114
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAhalFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKplvdAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 115 LAA--DIPLAIDHFRYFAGA------TRTQEGRIsqiddntvAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCI 186
Cdd:cd07148 84 TRAidGVELAADELGQLGGReipmglTPASAGRI--------AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 187 VLKPAEQTPASILMLTEIIADL-LPDGVLNIVnGLGTEAGAALTASDRISKIAFTGSTAVGQLINKavsdKIIPIT---L 262
Cdd:cd07148 156 IVKPALATPLSCLAFVDLLHEAgLPEGWCQAV-PCENAVAEKLVTDPRVAFFSFIGSARVGWMLRS----KLAPGTrcaL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 263 ELGGKSPSIFfpdvmdADDAFREKCIEGLAMFAL-NQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQM 341
Cdd:cd07148 231 EHGGAAPVIV------DRSADLDAMIPPLVKGGFyHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 342 GAQASQEQLDKISGYLESGPKEGAEVLTGGnvAKLegleGGYYVEPT-IFRGNNSMRFFREEIFGPVLAVTTFKTLDEAL 420
Cdd:cd07148 305 GPLIRPREVDRVEEWVNEAVAAGARLLCGG--KRL----SDTTYAPTvLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAI 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896153531 421 EIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNyhsypaHAA-------FGGYKQSGIG 477
Cdd:cd07148 379 AQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND------HTAfrvdwmpFAGRRQSGYG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
23-481 |
9.83e-58 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 199.03 E-value: 9.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 23 FIDGKWtppVDGQ--YMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIA 100
Cdd:PRK09457 4 WINGDW---IAGQgeAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 101 VAETWENGKAIRET------LAADIPLAIDhfryfAGATRTQEgRISQIDDNTVAYHfHEPLGVVGQIIPWNFPLLMAAW 174
Cdd:PRK09457 81 EVIARETGKPLWEAatevtaMINKIAISIQ-----AYHERTGE-KRSEMADGAAVLR-HRPHGVVAVFGPYNFPGHLPNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 175 KIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGlGTEAGAALTASDRISKIAFTGSTAVGQLINKAV 253
Cdd:PRK09457 154 HIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 254 S---DKIipITLELGGKSPSIfFPDVMDADDAFREkcIEGLAMfaLNQGEVCTCPSRALVHEDI-ADEFLKLAVERVKQI 329
Cdd:PRK09457 233 AgqpEKI--LALEMGGNNPLV-IDEVADIDAAVHL--IIQSAF--ISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 330 KTGNPlDTSVQ--MGAQASQEQLDKI---SGYLESgpkEGAEVLTggnvaKLEGLEGGY-YVEPTIFRGNNSMRFFREEI 403
Cdd:PRK09457 306 TVGRW-DAEPQpfMGAVISEQAAQGLvaaQAQLLA---LGGKSLL-----EMTQLQAGTgLLTPGIIDVTGVAELPDEEY 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896153531 404 FGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRV-WVNNYHSYPAHAAFGGYKQSGigreNH 481
Cdd:PRK09457 377 FGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG----NH 451
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
16-477 |
2.08e-57 |
|
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: 198.60 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 16 YKEQYENFIDGKW--TPPVDGQYMD--NSTPVTG-----EVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILH 86
Cdd:TIGR01238 24 LEAQIHAWADKTWqaAPIIGHSYKAdgEAQPVTNpadrrDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 87 RIADRLEENLEKIAVAETWENGKAIRETLAaDIPLAIDHFRYFAGATRtqegrisqiddNTVAYHFHEPLGVVGQIIPWN 166
Cdd:TIGR01238 104 RLADLLELHMPELMALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 167 FPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAV 245
Cdd:TIGR01238 172 FPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 246 GQLINKAVS---DKIIPITLELGGKSPSIffpdvMDADDAFREKCIEGLAMFALNQGEVCTCPSRALVHEDIADEFLKLA 322
Cdd:TIGR01238 252 AQLINQTLAqreDAPVPLIAETGGQNAMI-----VDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 323 VERVKQIKTGNPLDTSVQMG----AQASQEQLDKISGYLESGpKEGAEVLTGGNVAklegLEGGYYVEPTIFRGNNsMRF 398
Cdd:TIGR01238 327 QGAMQELKVGVPHLLTTDVGpvidAEAKQNLLAHIEHMSQTQ-KKIAQLTLDDSRA----CQHGTFVAPTLFELDD-IAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 399 FREEIFGPVLAVTTFKT--LDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNN--YHSYPAHAAFGGYKQS 474
Cdd:TIGR01238 401 LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRnqVGAVVGVQPFGGQGLS 480
|
...
gi 896153531 475 GIG 477
Cdd:TIGR01238 481 GTG 483
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
65-478 |
2.85e-57 |
|
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: 196.29 E-value: 2.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 65 AAHKAKD-SWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADI-PL------AIDHFRYFA-----G 131
Cdd:cd07134 5 AAQQAHAlALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEIlPVlseinhAIKHLKKWMkpkrvR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 132 ATRTQEGRISQIddntvayhFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADLLPD 211
Cdd:cd07134 85 TPLLLFGTKSKI--------RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 212 GVLNIVNGlGTEAGAALTaSDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFP--DVMDAddafREKCIE 289
Cdd:cd07134 157 DEVAVFEG-DAEVAQALL-ELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDEtaDLKKA----AKKIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 290 GlaMFaLNQGEVCTCPSRALVHEDIADEFLKLAVERVKQI--KTGNPLDTSvQMGAQASQEQLDKISGYLESGPKEGAEV 367
Cdd:cd07134 231 G--KF-LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASP-DLARIVNDRHFDRLKGLLDDAVAKGAKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 368 LTGGNVAkleglEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAA 446
Cdd:cd07134 307 EFGGQFD-----AAQRYIAPTVLTNvTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVL 381
|
410 420 430
....*....|....*....|....*....|....
gi 896153531 447 RGIQAGRVWVNN--YHSYPAHAAFGGYKQSGIGR 478
Cdd:cd07134 382 ARTSSGGVVVNDvvLHFLNPNLPFGGVNNSGIGS 415
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
150-478 |
3.25e-56 |
|
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: 193.87 E-value: 3.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 150 YHFH-------EPLGVVGQIIPWNFPLLMAawkIAP---ALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNG 219
Cdd:cd07136 88 LNFPsksyiyyEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVEG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 220 lGTEAGAALTASdRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPdvmDADdafrekciegLAMFA---- 295
Cdd:cd07136 165 -GVEENQELLDQ-KFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDE---DAN----------LKLAAkriv 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 296 ----LNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDtSVQMGAQASQEQLDKISGYLESGpkegaEVLTGG 371
Cdd:cd07136 230 wgkfLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLDNG-----KIVFGG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 372 NVAKlEGLeggyYVEPTIFRG----NNSMrffREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAAR 447
Cdd:cd07136 304 NTDR-ETL----YIEPTILDNvtwdDPVM---QEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLE 375
|
330 340 350
....*....|....*....|....*....|...
gi 896153531 448 GIQAGRVWVNN--YHSYPAHAAFGGYKQSGIGR 478
Cdd:cd07136 376 NLSFGGGCINDtiMHLANPYLPFGGVGNSGMGS 408
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
22-480 |
3.95e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 197.28 E-value: 3.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 22 NFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAV 101
Cdd:PLN02419 116 NLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 102 AETWENGKAIRETlAADIPLAIDHFRYFAGATRTQEGR-ISQIDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPAL 180
Cdd:PLN02419 196 NITTEQGKTLKDS-HGDIFRGLEVVEHACGMATLQMGEyLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 181 AAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDrISKIAFTGSTAVGQLINKAVSDKIIP 259
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAgLPDGVLNIVHGTNDTVNAICDDED-IRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 260 ITLELGGKSPSIFFPDVmDADDAFREKCIEGLAMfalnQGEVCTCPSRALVHEDiADEFLKLAVERVKQIKTGNPLDTSV 339
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDA-NIDATLNALLAAGFGA----AGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEPDA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 340 QMGAQASQEQLDKISGYLESGPKEGAEVLTGGNVAKLEGLEGGYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDE 418
Cdd:PLN02419 428 DLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGvTPDMECYKEEIFGPVLVCMQANSFDE 507
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896153531 419 ALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNNYHSYP-AHAAFGGYKQSGIGREN 480
Cdd:PLN02419 508 AISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPlPFFSFTGNKASFAGDLN 570
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
154-477 |
9.99e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 193.71 E-value: 9.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 154 EPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGlGTEAGAALTaSDR 233
Cdd:PTZ00381 108 EPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEG-GVEVTTELL-KEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 234 ISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVMDADDAFRekCIEGLamfALNQGEVCTCPSRALVHED 313
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARR--IAWGK---FLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 314 IADEFLK-LAVERVKQIktGNPLDTSVQMGAQASQEQLDKISGYLESgpkEGAEVLTGGNVAKLEgleggYYVEPTIFRg 392
Cdd:PTZ00381 261 IKDKFIEaLKEAIKEFF--GEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVDIEN-----KYVAPTIIV- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 393 NNSM--RFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNN--YHSYPAHAAF 468
Cdd:PTZ00381 330 NPDLdsPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvFHLLNPNLPF 409
|
....*....
gi 896153531 469 GGYKQSGIG 477
Cdd:PTZ00381 410 GGVGNSGMG 418
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
57-478 |
2.04e-53 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 186.27 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 57 KDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADIPLAIDHFRYFagatrtq 136
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHM------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 137 egrISQID---------DNTVAYHFH------EPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILML 201
Cdd:cd07135 78 ---LKNLKkwakdekvkDGPLAFMFGkprirkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 202 TEIIADLLPDGVLNIVNGLGTEAGAALTAsdRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDADD 281
Cdd:cd07135 155 AELVPKYLDPDAFQVVQGGVPETTALLEQ--KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNA-DLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 282 AFREkcieglAMFA--LNQGEVCTCPSRALVHEDIADEFLKlAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLEs 359
Cdd:cd07135 232 AAKR------ILWGkfGNAGQICVAPDYVLVDPSVYDEFVE-ELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLD- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 360 gpKEGAEVLTGGnvaklEGLEGGYYVEPTIFR---GNNSMrfFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWS 436
Cdd:cd07135 304 --TTKGKVVIGG-----EMDEATRFIPPTIVSdvsWDDSL--MSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 896153531 437 RNQNNAYRAARGIQAGRVWVNN--YHSYPAHAAFGGYKQSGIGR 478
Cdd:cd07135 375 DDKSEIDHILTRTRSGGVVINDtlIHVGVDNAPFGGVGDSGYGA 418
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
18-477 |
1.22e-50 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 180.34 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 18 EQYENFIDGKWTPPVDGQYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLE 97
Cdd:PLN00412 14 DVYKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 98 KIAVAETWENGKAIRETLA-----ADIP--LAIDHFRY-----------FAGATRTQEGRISQIddntvayhfhePLGVV 159
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVTevvrsGDLIsyTAEEGVRIlgegkflvsdsFPGNERNKYCLTSKI-----------PLGVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 160 GQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIA 238
Cdd:PLN00412 163 LAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHPGVNCIS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 239 FT-GSTAVgqlinkAVSDK--IIPITLELGGKSPSIFFPdvmDAD-DAFREKCIEGLAMFAlnqGEVCTCPSRALVHEDI 314
Cdd:PLN00412 243 FTgGDTGI------AISKKagMVPLQMELGGKDACIVLE---DADlDLAAANIIKGGFSYS---GQRCTAVKVVLVMESV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 315 ADEFLKLAVERVKQIKTGNPLDTSvQMGAQASQEQLDKISGYLESGPKEGAEVLTggnvaklEGLEGGYYVEPTIF-RGN 393
Cdd:PLN00412 311 ADALVEKVNAKVAKLTVGPPEDDC-DITPVVSESSANFIEGLVMDAKEKGATFCQ-------EWKREGNLIWPLLLdNVR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 394 NSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNnyhSYPA----HAAFG 469
Cdd:PLN00412 383 PDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN---SAPArgpdHFPFQ 459
|
....*...
gi 896153531 470 GYKQSGIG 477
Cdd:PLN00412 460 GLKDSGIG 467
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
51-457 |
2.52e-49 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 182.48 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 51 VPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEK---IAVAE---TWENGKA-IREtlaadiplAI 123
Cdd:PRK11809 676 VREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTlmgLLVREagkTFSNAIAeVRE--------AV 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 124 DHFRYFAGATRtqegriSQIDDNTvayhfHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPasiLMLTE 203
Cdd:PRK11809 748 DFLRYYAGQVR------DDFDNDT-----HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTP---LIAAQ 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 204 IIADLL----PDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKI------IPITLELGGKspsiff 273
Cdd:PRK11809 814 AVRILLeagvPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQ------ 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 274 pDVMDAD-DAFREKCIEGLAMFALNQ-GEVCTcpsrAL----VHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQ 347
Cdd:PRK11809 888 -NAMIVDsSALTEQVVADVLASAFDSaGQRCS----ALrvlcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDA 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 348 EQLDKISGYLESGPKEGAEVlTGGNVAKLEGLEGGYYVEPTIFRGNNSMRFFReEIFGPVLAVTTFK--TLDEALEIAND 425
Cdd:PRK11809 963 EAKANIERHIQAMRAKGRPV-FQAARENSEDWQSGTFVPPTLIELDSFDELKR-EVFGPVLHVVRYNrnQLDELIEQINA 1040
|
410 420 430
....*....|....*....|....*....|..
gi 896153531 426 TIYGLGAGVWSRNQNNAYRAARGIQAGRVWVN 457
Cdd:PRK11809 1041 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1072
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
45-457 |
2.79e-49 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 177.01 E-value: 2.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 45 GEVFCRVPRSNEKDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENL-EKIAVAETWENGKAIREtlaADIPLA- 122
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNVWQ---AEIDAAc 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 123 --IDHFR---YFAGATRTQEGRISQIDD-NTVAYhfhEPL-GVVGQIIPWNFPLLMAAWKIAPALAaGNCIVLKPAEQTP 195
Cdd:cd07123 134 elIDFLRfnvKYAEELYAQQPLSSPAGVwNRLEY---RPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 196 ASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKI-----IP-ITLELGGKS 268
Cdd:cd07123 210 LSNYLVYKILEEAgLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLdryrtYPrIVGETGGKN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 269 -----PSiffpdvmdAD-DAFREKCIEGLAMFalnQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMG 342
Cdd:cd07123 290 fhlvhPS--------ADvDSLVTATVRGAFEY---QGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 343 AQASQEQLDKISGYLESGPKE-GAEVLTGGNVAKLEglegGYYVEPTIFRGNNSM-RFFREEIFGPVLAVTTF--KTLDE 418
Cdd:cd07123 359 AVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSV----GYFVEPTVIETTDPKhKLMTEEIFGPVLTVYVYpdSDFEE 434
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 896153531 419 ALEIANDT-IYGLGAGVWSRNQNNAYRAARGIQ--AGRVWVN 457
Cdd:cd07123 435 TLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYIN 476
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
64-478 |
2.36e-44 |
|
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: 162.01 E-value: 2.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 64 DAAHKAKDSWAS---VPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAA-------DIPLAIDHFRYFAGAT 133
Cdd:cd07132 2 EAVRRAREAFSSgktRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSeillvknEIKYAISNLPEWMKPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 134 RTQEGRISQIDDntvAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASilmlTEIIADLLPDGV 213
Cdd:cd07132 82 PVKKNLATLLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPAT----AKLLAELIPKYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 214 LN----IVNGlGTEAGAALTAsDRISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPsIFFPDVMDADDAFRE---- 285
Cdd:cd07132 155 DKecypVVLG-GVEETTELLK-QRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSP-CYVDKSCDIDVAARRiawg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 286 KCIeglamfalNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDtSVQMGAQASQEQLDKISGYLESGpkega 365
Cdd:cd07132 232 KFI--------NAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKE-SPDYGRIINDRHFQRLKKLLSGG----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 366 EVLTGGNVAKLEgleggYYVEPTIFRG-NNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYR 444
Cdd:cd07132 298 KVAIGGQTDEKE-----RYIAPTVLTDvKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINK 372
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 896153531 445 AARGIQAGRVWVNN------YHSYPahaaFGGYKQSGIGR 478
Cdd:cd07132 373 ILSNTSSGGVCVNDtimhytLDSLP----FGGVGNSGMGA 408
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
154-478 |
2.77e-42 |
|
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: 156.03 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 154 EPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGLGTEAGAALtaSDR 233
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVPETTALL--EQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 234 ISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFFPDVmDADDAFReKCIEGlaMFALNQGEVCTCPSRALVHED 313
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTV-DLKVAVR-RIAGG--KWGCNNGQACIAPDYVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 314 IADEFLKLAVERVKQIKTGNPLdTSVQMGAQASQEQLDKISGYLESgPKEGAEVLTGGNVAkleglEGGYYVEPTIFRgN 393
Cdd:cd07137 254 FAPTLIDALKNTLEKFFGENPK-ESKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERD-----EKNLYIEPTILL-D 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 394 NSMR--FFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNN--YHSYPAHAAFG 469
Cdd:cd07137 326 PPLDssIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDtvVQYAIDTLPFG 405
|
....*....
gi 896153531 470 GYKQSGIGR 478
Cdd:cd07137 406 GVGESGFGA 414
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
60-470 |
5.06e-36 |
|
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: 138.91 E-value: 5.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 60 ELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAirETLAADIPLAIDHFRYFAGATRTqeGR 139
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG--WMFAENICGDQVQLRARAFVIYS--YR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 140 ISQIDDNTV-------AYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIAD--LLP 210
Cdd:cd07084 78 IPHEPGNHLgqglkqqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 211 DGVLNIVNGLGtEAGAALTASDRISKIAFTGSTAVGQ-LINKAvsdKIIPITLELGGKSPSIFFPDVmDADDAFREKCIE 289
Cdd:cd07084 158 PEDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEkLALDA---KQARIYLELAGFNWKVLGPDA-QAVDYVAWQCVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 290 GLAMFAlnqGEVCTCPSRALVHEDIADE-FLKLAVERVKQIKTGNPLDTSVQmgaqasqeQLDKISGYLESGPKEGAEVL 368
Cdd:cd07084 233 DMTACS---GQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLLLGPVQ--------TFTTLAMIAHMENLLGSVLL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 369 TGGNVAKLEGLEGGY--YVEPTIF----RGNNSMRFFREEIFGPVLAVTTFKTLDEA--LEIANDTIYGLGAGVWS---- 436
Cdd:cd07084 302 FSGKELKNHSIPSIYgaCVASALFvpidEILKTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSndpi 381
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 896153531 437 ---RNQNNAYRAAR----GIQAGRVWVNNYHSYPAHAAFGG 470
Cdd:cd07084 382 flqELIGNLWVAGRtyaiLRGRTGVAPNQNHGGGPAADPRG 422
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-458 |
4.12e-35 |
|
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: 137.40 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 21 ENFIDGKW-TPPVDGQYMDNstPVTGEVFCRVpRSNEKDIELALDAAHKAkdswaSVPA------AERALILHRIADRLE 93
Cdd:cd07128 2 QSYVAGQWhAGTGDGRTLHD--AVTGEVVARV-SSEGLDFAAAVAYAREK-----GGPAlraltfHERAAMLKALAKYLM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 94 ENLEK-IAVAETweNGkAIRETLAADIPLAIDHFRYFAGATRTQ--------EGRISQI--DDNTVAYHFHEPL-GVVGQ 161
Cdd:cd07128 74 ERKEDlYALSAA--TG-ATRRDSWIDIDGGIGTLFAYASLGRRElpnahflvEGDVEPLskDGTFVGQHILTPRrGVAVH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 162 IIPWNFPllmaAW----KIAPALAAGNCIVLKPAEQTPASILMLTEIIAD--LLPDGVLNIVNGLGTEAGAALTASDris 235
Cdd:cd07128 151 INAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICGSVGDLLDHLGEQD--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 236 KIAFTGSTAVGQLI--NKAVSDKIIPITLELGGKSPSIFFPDVMDADDAFrekcieglAMFA--------LNQGEVCTCP 305
Cdd:cd07128 224 VVAFTGSAATAAKLraHPNIVARSIRFNAEADSLNAAILGPDATPGTPEF--------DLFVkevaremtVKAGQKCTAI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 306 SRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLESgPKEGAEVLTGGNV---AKLEGLEGG 382
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDrfeVVGADAEKG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 383 YYVEPTIFRGNNSMR---FFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQA--GRVWVN 457
Cdd:cd07128 375 AFFPPTLLLCDDPDAataVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVL 454
|
.
gi 896153531 458 N 458
Cdd:cd07128 455 N 455
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
154-495 |
3.29e-34 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 134.79 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 154 EPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGLGTEAGAALtaSDR 233
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 234 ISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSiffpdVMDADDAFR---EKCIEGlaMFALNQGEVCTCPSRALV 310
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPV-----VVDSDTDLKvtvRRIIAG--KWGCNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 311 HEDIADEFLKLAVERVKQIKTGNPLDtSVQMGAQASQEQLDKISGYLESgpKEGAEVLTGGNVAKLEGLEggyyVEPTIF 390
Cdd:PLN02174 262 TKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGEKDRENLK----IAPTIL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 391 RGN--NSMrFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNN------YHSY 462
Cdd:PLN02174 335 LDVplDSL-IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDiavhlaLHTL 413
|
330 340 350
....*....|....*....|....*....|...
gi 896153531 463 PahaaFGGYKQSGIGRENHLMMLEHYQETKCML 495
Cdd:PLN02174 414 P----FGGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
154-478 |
1.14e-32 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 130.23 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 154 EPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLNIVNGlGTEAGAALTaSDR 233
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEG-GPAVGEQLL-QHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 234 ISKIAFTGSTAVGQLINKAVSDKIIPITLELGGKSPSIFfpdvmDADDAFRE-----KCIEGlAMFALNQGEVCTCPSRA 308
Cdd:PLN02203 185 WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV-----DSLSSSRDtkvavNRIVG-GKWGSCAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 309 LVHEDIADEFLKLAVERVKQIKTGNPLDTSvQMGAQASQEQLDKISGYLESgPKEGAEVLTGGNVAkleglEGGYYVEPT 388
Cdd:PLN02203 259 LVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKD-PRVAASIVHGGSID-----EKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 389 IFRgNNSM--RFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQAGRVWVNN-YHSYPAH 465
Cdd:PLN02203 332 ILL-NPPLdsDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDaIIQYACD 410
|
330
....*....|....
gi 896153531 466 A-AFGGYKQSGIGR 478
Cdd:PLN02203 411 SlPFGGVGESGFGR 424
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-424 |
5.58e-31 |
|
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: 124.96 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 59 IELALDAAHKAKDSWASVPAAERALILHRIADRLEEN---LEKIAVAETwenGKAIREtLAADIPLAIDHFRYFAGATRT 135
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALgdeLVARAHAET---GLPEAR-LQGELGRTTGQLRLFADLVRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 136 QEGRISQIDDNTVAYH---------FHEPLGVVGQIIPWNFPLlmaAWKI-----APALAAGNCIVLKPAEQTPAsilmL 201
Cdd:cd07129 77 GSWLDARIDPADPDRQplprpdlrrMLVPLGPVAVFGASNFPL---AFSVaggdtASALAAGCPVVVKAHPAHPG----T 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 202 TEIIADL---------LPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKI--IPITLELGGKSPS 270
Cdd:cd07129 150 SELVARAiraalratgLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPepIPFYAELGSVNPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 271 IFFPDVMDADdafREKCIEGLA-MFALNQGEVCTCPSRALVHEDIA-DEFLKLAVERVKQIKTGNPLDTSVQMGAQASQE 348
Cdd:cd07129 230 FILPGALAER---GEAIAQGFVgSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 349 QldkisgyLESGPkeGAEVLTGGNVAkleglEGGYYVEPTI-------FRGNNSmrfFREEIFGPVLAVTTFKTLDEALE 421
Cdd:cd07129 307 A-------LAAAP--GVRVLAGGAAA-----EGGNQAAPTLfkvdaaaFLADPA---LQEEVFGPASLVVRYDDAAELLA 369
|
...
gi 896153531 422 IAN 424
Cdd:cd07129 370 VAE 372
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
18-456 |
1.16e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 122.12 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 18 EQYENFIDGKW-------TPPVDgqymdnstPVTGEVFCRVprsNEKDIELALDAAHKAKDSWASVPA---AERALILHR 87
Cdd:PRK11903 3 ELLANYVAGRWqagsgagTPLFD--------PVTGEELVRV---SATGLDLAAAFAFAREQGGAALRAltyAQRAALLAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 88 IADRLEENLEK---IAVAetweNGKAIRETLAADIPLAIDHFRYFA--GAT-----------RTQEGRisqiDDNTVAYH 151
Cdd:PRK11903 72 IVKVLQANRDAyydIATA----NSGTTRNDSAVDIDGGIFTLGYYAklGAAlgdarllrdgeAVQLGK----DPAFQGQH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 152 FHEPL-GVVGQIIPWNFPllmaAW----KIAPALAAGNCIVLKPAeqTPASIL---MLTEII-ADLLPDGVLNIVNGLGT 222
Cdd:PRK11903 144 VLVPTrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPA--TATAWLtqrMVKDVVaAGILPAGALSVVCGSSA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 223 EAGAALTASDRISkiaFTGSTAVGQLI--NKAVSDKIIPITLELGGKSPSIFFPDVMDADDAFREKCIEGLAMFALNQGE 300
Cdd:PRK11903 218 GLLDHLQPFDVVS---FTGSAETAAVLrsHPAVVQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 301 VCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLDTSVQMGAQASQEQLDKISGYLEsGPKEGAEVLTGGNVAKLEGLE 380
Cdd:PRK11903 295 KCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDAD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 381 --GGYYVEPTIFRGN---NSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGAGVWSRNQNNAYRAARGIQA--GR 453
Cdd:PRK11903 374 paVAACVGPTLLGASdpdAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGR 453
|
...
gi 896153531 454 VWV 456
Cdd:PRK11903 454 VHV 456
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
22-440 |
1.87e-12 |
|
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: 69.45 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 22 NFIDGKWTPPVDgqYMDNSTPVTGEVFCRVPRSNEKDIELALDAAHKAKDSWASVP--AAERALILHRIADRLEENLEKI 99
Cdd:cd07126 1 NLVAGKWKGASN--YTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPlkNPERYLLYGDVSHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 100 AVAETWenGKAIRETL-------AADIPLAIDHFRYFAGATRTQEGRISQIDDNTVAYHFHE---PLGVVGQIIPWNFPL 169
Cdd:cd07126 79 EVEDFF--ARLIQRVApksdaqaLGEVVVTRKFLENFAGDQVRFLARSFNVPGDHQGQQSSGyrwPYGPVAIITPFNFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 170 LMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-LPDGVLNIVNGLGTEAGAALTASDRISkIAFTGSTAVGQL 248
Cdd:cd07126 157 EIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCgMPATDVDLIHSDGPTMNKILLEANPRM-TLFTGSSKVAER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 249 INKAVSDKiipITLELGGKSPSIFFPDVMDAD--------DAFreKCieglamfalnQGEVCTCPSRALVHED-----IA 315
Cdd:cd07126 236 LALELHGK---VKLEDAGFDWKILGPDVSDVDyvawqcdqDAY--AC----------SGQKCSAQSILFAHENwvqagIL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 316 DEFLKLAVERVKQIKTGNPLDTsvqMGAQASQEQLDKISGYlesgpkEGAEVLTGGNVAKLEGLEGGY-YVEPT-IF--- 390
Cdd:cd07126 301 DKLKALAEQRKLEDLTIGPVLT---WTTERILDHVDKLLAI------PGAKVLFGGKPLTNHSIPSIYgAYEPTaVFvpl 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 896153531 391 ---RGNNSMRFFREEIFGPVLAVTTFK--TLDEALEIANDTIYGLGAGVWSRNQN 440
Cdd:cd07126 372 eeiAIEENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSNDIR 426
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
64-433 |
4.03e-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: 61.47 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 64 DAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENGKAIRETLAADIPLA----------IDHFRYFAGAt 133
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMgcsesklyknIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 134 rtqEGRISQI--DDNTVAYHFHEPLGVVGQIIPWNFPLLmAAWKIAPALAAGNCIVLKPAEQTPAS----ILMLTEIIAD 207
Cdd:cd07077 80 ---VGHIQDVllPDNGETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTnralALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 208 LLPDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVsdKIIPITLELGGKSPSiffpdVMDaDDAFREKC 287
Cdd:cd07077 156 HGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPV-----VVD-ETADEERA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 288 IEGLAMFALNQGEVCTCPSRALVHEDIADEF-----LKLAVERVK-----QIKTGNPLDTSVQ------MGAQASQEQLD 351
Cdd:cd07077 228 SGSVHDSKFFDQNACASEQNLYVVDDVLDPLyeefkLKLVVEGLKvpqetKPLSKETTPSFDDealesmTPLECQFRVLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 352 KISG------YLESGPKEGAEVLTGGNVAKLEGLegGYYVEPTIFRGNNSMRFFREEIFGPVLAVTtfktldeaLEIAND 425
Cdd:cd07077 308 VISAvenawmIIESGGGPHTRCVYTHKINKVDDF--VQYIDTASFYPNESSKKGRGAFAGKGVERI--------VTSGMN 377
|
....*...
gi 896153531 426 TIYGLGAG 433
Cdd:cd07077 378 NIFGAGVG 385
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
29-475 |
1.63e-09 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 60.18 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 29 TPPVDGQYMDNSTPVTGEVFCRVPRSnekDIELALDAAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWENG 108
Cdd:cd07127 59 QPGASGWVGGEVSPYGVELGVTYPQC---DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 109 KAIRETLAADIPLAIDH----FRYFAGA-TRT--------QEGRISQIddnTVAYHFH-EPLGV-----VGQIIPWN-FP 168
Cdd:cd07127 136 QAFMMAFQAGGPHAQDRgleaVAYAWREmSRIpptaewekPQGKHDPL---AMEKTFTvVPRGValvigCSTFPTWNgYP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 169 LLMAAwkiapaLAAGNCIVLKPAeqtPASIL---MLTEIIADLL------PDGVLNIVNGLGTEAGAALTASDRISKIAF 239
Cdd:cd07127 213 GLFAS------LATGNPVIVKPH---PAAILplaITVQVAREVLaeagfdPNLVTLAADTPEEPIAQTLATRPEVRIIDF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 240 TGSTAVGQLINKAVSDKIIpiTLELGGKSPSIffpdvMDADDAFREKCiEGLAM-FALNQGEVCTCPSRALVHED----- 313
Cdd:cd07127 284 TGSNAFGDWLEANARQAQV--YTEKAGVNTVV-----VDSTDDLKAML-RNLAFsLSLYSGQMCTTPQNIYVPRDgiqtd 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 314 ------------IADEFLKLAvervkqiktGNPLDTSVQMGAQASQEQLDKISgylESGpkEGAEVLTGGNVAKLEGLEG 381
Cdd:cd07127 356 dgrksfdevaadLAAAIDGLL---------ADPARAAALLGAIQSPDTLARIA---EAR--QLGEVLLASEAVAHPEFPD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 382 GYYVEPTIFRGNNSMR-FFREEIFGPVLAVTTFKTLDEALEIANDTIYGLGA---GVWSRNQNNAYR-----AARGIQ-- 450
Cdd:cd07127 422 ARVRTPLLLKLDASDEaAYAEERFGPIAFVVATDSTDHSIELARESVREHGAmtvGVYSTDPEVVERvqeaaLDAGVAls 501
|
490 500
....*....|....*....|....*...
gi 896153531 451 ---AGRVWVNNyhsypaHAAFGGYKQSG 475
Cdd:cd07127 502 inlTGGVFVNQ------SAAFSDFHGTG 523
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
62-457 |
7.56e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 48.42 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 62 ALDAAHKAKDSWASVPAAERALILHRIADRLEE---NLEKIAVAETwenGKAIRETlaadiPLAIDHF--RYFAGATRTQ 136
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDariDLAKLAVSET---GMGRVED-----KVIKNHFaaEYIYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 137 E--GRISQiDDNTVAYHFHEPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTP-----ASILMLTEIIADLL 209
Cdd:cd07081 76 KtcGVLTG-DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKkvtqrAATLLLQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 210 PDGVLNIVNGLGTEAGAALTASDRISKIAFTGSTAVGQLINKAVSDKIipitlELGGKSPsiffPDVMD--ADDAFREKC 287
Cdd:cd07081 155 PENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAI-----GVGAGNT----PVVIDetADIKRAVQS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 288 IEGLAMFalNQGEVCTCPSRALVHEDIADEFLKLAVERVKQIKTGNPLdtsvqmgaQASQEQLdkisgyLESGPKEGAEV 367
Cdd:cd07081 226 IVKSKTF--DNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEEL--------QQVQPVI------LKNGDVNRDIV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 368 -LTGGNVAKLEGLEGG-----YYVEPTIFrgnNSMRFFREEIFGPVLAVTTFKTLDEALEIANDTIY--GLG--AGVWSR 437
Cdd:cd07081 290 gQDAYKIAAAAGLKVPqetriLIGEVTSL---AEHEPFAHEKLSPVLAMYRAANFADADAKALALKLegGCGhtSAMYSD 366
|
410 420
....*....|....*....|...
gi 896153531 438 NQN---NAYRAARGIQAGRVWVN 457
Cdd:cd07081 367 NIKaieNMNQFANAMKTSRFVKN 389
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
65-260 |
1.58e-04 |
|
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130164 [Multi-domain] Cd Length: 715 Bit Score: 44.51 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 65 AAHKAKDSWASVPAAERALILHRIADRLEENLEKIAVAETWE----NGKAIRETLAADIPLAIDHFRYFAGATR----TQ 136
Cdd:TIGR01092 294 AARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDvaaaQGAGYAASLVARLSMSPSKISSLAISLRqlaaME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 137 E--GRI---SQIDDNTVAYHFHEPLGVVgQIIPWNFP--LLMAAwkiAPALAAGNCIVLKPAEQTPASILMLTEIIADLL 209
Cdd:TIGR01092 374 DpiGRVlkrTRIADNLILEKTSVPIGVL-LIVFESRPdaLVQIA---SLAIRSGNGLLLKGGKEAARSNAILHKVITEAI 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 896153531 210 PDGVLNIVNGLGT---EAGAALTASDRISKIAFTGSTAVGQLINKAVSdkiIPI 260
Cdd:TIGR01092 450 PIHVGKKLIGLVTsreEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTK---IPV 500
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
154-457 |
1.14e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 41.32 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 154 EPLGVVGQIIPWNFPLLMAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADL-----LPDGVLNIVNGLGTEAGAAL 228
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaagAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 229 TASDRISKIAFTGSTA--------------VGQ-----------LINKAVSDKIIpitlelgGKSpsiffpdvmdaddaf 283
Cdd:cd07122 174 MKHPDVDLILATGGPGmvkaayssgkpaigVGPgnvpayidetaDIKRAVKDIIL-------SKT--------------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 284 rekcieglamfaLNQGEVCTCPSRALVHEDIADEFLKLAVERvkqiktgnpldtsvqmGAQ-ASQEQLDKISGYL-ESGP 361
Cdd:cd07122 232 ------------FDNGTICASEQSVIVDDEIYDEVRAELKRR----------------GAYfLNEEEKEKLEKALfDDGG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 362 KEGAEVlTGGNVAKLEGLEGGYYVEPT-IFRGNNSM-----RFFREEIFgPVLAVTTFKTLDEALEIAND--TIYGLG-- 431
Cdd:cd07122 284 TLNPDI-VGKSAQKIAELAGIEVPEDTkVLVAEETGvgpeePLSREKLS-PVLAFYRAEDFEEALEKAREllEYGGAGht 361
|
330 340
....*....|....*....|....*.
gi 896153531 432 AGVWSRNQNNAYRAARGIQAGRVWVN 457
Cdd:cd07122 362 AVIHSNDEEVIEEFALRMPVSRILVN 387
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
155-258 |
2.91e-03 |
|
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: 40.12 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153531 155 PLGVVGQIIPWNFPLLmAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLnivnglgteagaaltaSDRI 234
Cdd:pfam05893 88 PPGLVFHVLSGNVPLL-PVMSILMGLLVKNVNLLKVSSSDPFTAAALLASFADLDPTHPL----------------ADSL 150
|
90 100
....*....|....*....|....*
gi 896153531 235 SKIAF-TGSTAVGQLINKAvSDKII 258
Cdd:pfam05893 151 SVVYWdGGSTQLEDLIVAN-ADVVI 174
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
155-349 |
9.95e-03 |
|
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: 38.41 E-value: 9.95e-03
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gi 896153531 155 PLGVVGQIIPWNFPLLmAAWKIAPALAAGNCIVLKPAEQTPASILMLTEIIADLLPDGVLnivnglgTEAGAAL------ 228
Cdd:cd07080 112 PRGLVVHIIAGNVPLL-PVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVDPNHPL-------TDSISVVywpggd 183
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90 100 110 120 130 140 150 160
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gi 896153531 229 -TASDRISK-----IAFTGSTAVgqlinKAVSDKIIP--ITLELGGK-SPSIFFPDVMDADDAfrEKCIEGLAM--FALN 297
Cdd:cd07080 184 aELEERILAsadavVAWGGEEAV-----KAIRSLLPPgcRLIDFGPKySFAVIDREALESEKL--AEVADALAEdiCRYD 256
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170 180 190 200 210 220
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gi 896153531 298 QgEVCTCPSRALVHEDIA---DEF---LKLAVERV--KQIKTGNPLDTSVQMgAQASQEQ 349
Cdd:cd07080 257 Q-QACSSPQVVFVEKDDDeelREFaeaLAAALERLprRYPALSLSAAESAKI-ARARLEA 314
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