|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
20-499 |
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: 937.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELL 99
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 100 AVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPA 179
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 180 LAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIP 259
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 260 VTLELGGKSPNIFFEDVASSKDAYYEKAQEGFTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNT 339
Cdd:cd07559 241 VTLELGGKSPNIFFDDAMDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 340 MMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGDLSGGYYVQPTVFEGKNSMRIFQEEIFGPVLSVTSFKDYDE 419
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 420 AISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY 499
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
20-499 |
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: 931.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELL 99
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 100 AVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPA 179
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 180 LAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIP 259
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 260 VTLELGGKSPNIFFEDVASSKDAYYEKAQEGFTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNT 339
Cdd:cd07116 241 VTLELGGKSPNIFFADVMDADDAFFDKALEGFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 340 MMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGDLSGGYYVQPTVFeGKNSMRIFQEEIFGPVLSVTSFKDYDE 419
Cdd:cd07116 321 MIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFK-GGNKMRIFQEEIFGPVLAVTTFKDEEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 420 AISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY 499
Cdd:cd07116 400 ALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY 479
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
14-499 |
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: 636.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 14 MSYKgRYDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRME 93
Cdd:COG1012 1 MTTP-EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 94 ANLELLAVAETWDNGKAVRETMaADIPLAIDHFRYFAGAIRAQEGSIGELD-DNTVAYHFHEPLGVVGQIIPWNFPILMA 172
Cdd:COG1012 80 ERREELAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 173 VWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQ 251
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 252 YASENLIPVTLELGGKSPNIFFEDVasskDayYEKAQEG--FTMFaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKI 329
Cdd:COG1012 239 AAAENLKRVTLELGGKNPAIVLDDA----D--LDAAVEAavRGAF-GNAGQRCTAASRLLVHESIYDEFVERLVAAAKAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 330 IQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGgdlsGGYYVQPTVFEG-KNSMRIFQEEIFGPV 408
Cdd:COG1012 312 KVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGE----GGYFVEPTVLADvTPDMRIAREEIFGPV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 409 LSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYP-AHAAFGGYKQSGIGRENHKMMLD 487
Cdd:COG1012 388 LSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLE 467
|
490
....*....|..
gi 2498343516 488 HYQQTKNLLVSY 499
Cdd:COG1012 468 EYTETKTVTIRL 479
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
20-498 |
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: 604.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELL 99
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 100 AVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPA 179
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 180 LAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIP 259
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 260 VTLELGGKSPNIFFEdvasskDAYYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTN 338
Cdd:cd07117 241 ATLELGGKSANIIFD------DANWDKALEGAQLGILfNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 339 TMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERAdLGGDLSGGYYVQPTVFEGK-NSMRIFQEEIFGPVLSVTSFKDY 417
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRL-TENGLDKGFFIEPTLIVNVtNDMRVAQEEIFGPVATVIKFKTE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 418 DEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07117 394 DEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
.
gi 2498343516 498 S 498
Cdd:cd07117 474 D 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
31-494 |
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: 586.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 31 PSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKA 110
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 111 VRETMAaDIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKP 190
Cdd:pfam00171 83 LAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 191 AEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSP 269
Cdd:pfam00171 162 SELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 270 NIFFEdvasskDAYYEKAQEGfTMFA--LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASN 347
Cdd:pfam00171 242 LIVLE------DADLDAAVEA-AVFGafGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 348 DQLEKILSYIDIGKQEGAKLLCGGERadlggDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIAND 426
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEA-----GLDNGYFVEPTVLANvTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIAND 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2498343516 427 TLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQY-PAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 494
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGdADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| 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: 564.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFE--SWGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPAL 180
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 181 AAGNCIVLKPAEQTPASIHVLLELI-EDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE-NLI 258
Cdd:cd07091 167 AAGNTVVLKPAEQTPLSALYLAELIkEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 259 PVTLELGGKSPNIFFEDvasskdAYYEKAQEgFTMFAL--NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLD 336
Cdd:cd07091 247 KVTLELGGKSPNIVFDD------ADLDKAVE-WAAFGIffNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 337 TNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlggdlSGGYYVQPTVF-EGKNSMRIFQEEIFGPVLSVTSFK 415
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHG-----SKGYFIQPTVFtDVKDDMKIAKEEIFGPVVTILKFK 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2498343516 416 DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
39-497 |
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: 550.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 39 NITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAAD 118
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 119 IPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASI 198
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 199 HVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEdva 277
Cdd:cd07093 161 WLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFA--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 278 sskDAYYEKAQEGfTMFA--LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILS 355
Cdd:cd07093 238 ---DADLDRAVDA-AVRSsfSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 356 YIDIGKQEGAKLLCGGERADLgGDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAG 434
Cdd:cd07093 314 YVELARAEGATILTGGGRPEL-PDLEGGYFVEPTVITGlDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 435 VWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-507 |
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: 544.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES--WGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETmAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPAL 180
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 181 AAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIP 259
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 260 VTLELGGKSPNIFFedvassKDAYYEKAQEGfTMFA--LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDT 337
Cdd:cd07119 240 VALELGGKNPNIVF------ADADFETAVDQ-ALNGvfFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 338 NTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlGGDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKD 416
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPT-GDELAKGYFVEPTIFDDvDRTMRIVQEEIFGPVLTVERFDT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 417 YDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 496
Cdd:cd07119 392 EEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
490
....*....|.
gi 2498343516 497 VSYAEGPMGFF 507
Cdd:cd07119 472 INLSPQPIGWF 482
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
40-497 |
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: 539.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES--WGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVREtMAA 117
Cdd:cd07114 2 INPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRE-TRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 118 DIPLAIDHFRYFAGAIRAQEGSIGELD-DNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 197 SIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFED 275
Cdd:cd07114 161 STLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 276 vasskdAYYEKAQEG--FTMFAlNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKI 353
Cdd:cd07114 241 ------ADLDAAVNGvvAGIFA-AAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 354 LSYIDIGKQEGAKLLCGGERADlGGDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLG 432
Cdd:cd07114 314 ERYVARAREEGARVLTGGERPS-GADLGAGYFFEPTILADvTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2498343516 433 AGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-493 |
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: 533.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 34 GEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES--WGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAV 111
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 112 RETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPA 191
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 192 EQTPASIHVLLEL-IEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE-NLIPVTLELGGKSP 269
Cdd:cd07112 161 EQSPLTALRLAELaLEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 270 NIFFEDVASSkDAYYEKAQEGftMFAlNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQ 349
Cdd:cd07112 241 NIVFADAPDL-DAAAEAAAAG--IFW-NQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 350 LEKILSYIDIGKQEGAKLLCGGERADLGGdlsGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTL 428
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGKRVLTET---GGFFVEPTVFDGvTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2498343516 429 YGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
60-497 |
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: 524.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 60 DMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKaVRETMAADIPLAIDHFRYFAGAIRAQEG- 138
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGK-PIEEALGEVARAADTFRYYAGLARRLHGe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 139 SIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIED-LLPAGVLNIV 217
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEaGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 218 NGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEG--FTMFa 295
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFD------DADLDAAVKGavFGAF- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 296 LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERAD 375
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 376 LGgdlsGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGR 454
Cdd:cd07078 313 GG----KGYFVPPTVLTDvDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGT 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2498343516 455 VWTNTYHQYP-AHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07078 389 VWINDYSVGAePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
23-493 |
7.23e-174 |
|
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: 498.17 E-value: 7.23e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFE--SWGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPAL 180
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 181 AAGNCIVLKPAEQTPASIHVLLELI-EDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE-NLI 258
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAaEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 259 PVTLELGGKSPNIFFEDVasSKDAYYEKAQegFTMFaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTN 338
Cdd:cd07142 247 PVTLELGGKSPFIVCEDA--DVDKAVELAH--FALF-FNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 339 TMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERadLGgdlSGGYYVQPTVF-EGKNSMRIFQEEIFGPVLSVTSFKDY 417
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDR--IG---SKGYYIQPTIFsDVKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2498343516 418 DEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
23-493 |
7.28e-171 |
|
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: 490.77 E-value: 7.28e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES-WGKTSVTERAIILNKIADRMEANLELLAV 101
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 102 AETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALA 181
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 182 AGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPV 260
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 261 TLELGGKSPNIFFEDVASSKDAYYekAQEGFtMFalNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKI-IQGNPLDTNT 339
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKW--AAAGI-MY--NSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 340 MMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGgdLSGGYYVQPTVF-EGKNSMRIFQEEIFGPVLSVTSFKDYD 418
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEG--LGKGYFIPPTIFtDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2498343516 419 EAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
39-498 |
1.51e-170 |
|
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: 488.87 E-value: 1.51e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 39 NITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAAD 118
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 119 IPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASI 198
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 199 HVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEdva 277
Cdd:cd07115 161 LRIAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFA--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 278 sskDAYYEKAQEG--FTMFaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILS 355
Cdd:cd07115 238 ---DADLDAAVRAaaTGIF-YNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 356 YIDIGKQEGAKLLCGGERADlggdlSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAG 434
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPG-----ARGFFVEPTIFAAvPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2498343516 435 VWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVS 498
Cdd:cd07115 389 VWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
23-498 |
4.13e-170 |
|
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: 488.78 E-value: 4.13e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFE---SWGKTSVTERAIILNKIADRMEANLELL 99
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 100 AVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPA 179
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 180 LAAGNCIVLKPAEQTPASIHVLLELI-EDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE-NL 257
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIkEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsNL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 258 IPVTLELGGKSPNIFFEDvaSSKDAYYEKAQEGftMFAlNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDT 337
Cdd:cd07141 250 KRVTLELGGKSPNIVFAD--ADLDYAVEQAHEA--LFF-NMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 338 NTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERAdlgGDLsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKD 416
Cdd:cd07141 325 KTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRH---GDK--GYFIQPTVFSDvTDDMRIAKEEIFGPVQQIFKFKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 417 YDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 496
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
..
gi 2498343516 497 VS 498
Cdd:cd07141 480 IK 481
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
14-497 |
7.93e-165 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 475.52 E-value: 7.93e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 14 MSYKGRYDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRME 93
Cdd:PRK13252 1 MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 94 ANLELLAVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAV 173
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 174 WKLAPALAAGNCIVLKPAEQTPASIHVLLE-LIEDLLPAGVLNIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIMQY 252
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEiYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 253 ASENLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEGfTMFA--LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKII 330
Cdd:PRK13252 240 AAASLKEVTMELGGKSPLIVFD------DADLDRAADI-AMLAnfYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 331 QGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlGGDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVL 409
Cdd:PRK13252 313 IGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLT-EGGFANGAFVAPTVFTDcTDDMTIVREEIFGPVM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 410 SVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHY 489
Cdd:PRK13252 392 SVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHY 471
|
....*...
gi 2498343516 490 QQTKNLLV 497
Cdd:PRK13252 472 TQIKSVQV 479
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
39-497 |
4.16e-163 |
|
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: 469.86 E-value: 4.16e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 39 NITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVrETMAAD 118
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 119 IPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASI 198
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 199 HVLLE-LIEDLLPAGVLNIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDva 277
Cdd:cd07090 160 LLLAEiLTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 278 sskdAYYEKAQEGfTMFA--LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILS 355
Cdd:cd07090 237 ----ADLENAVNG-AMMAnfLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 356 YIDIGKQEGAKLLCGGERADLGGDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAG 434
Cdd:cd07090 312 YIESAKQEGAKVLCGGERVVPEDGLENGFYVSPCVLTDcTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 435 VWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07090 392 VFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
40-496 |
4.37e-160 |
|
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: 462.21 E-value: 4.37e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETmAADI 119
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAIDHFRYFAG---AIRAQEGSIGELDDNTV-AYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTP 195
Cdd:cd07110 81 DDVAGCFEYYADlaeQLDAKAERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 196 ASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFE 274
Cdd:cd07110 161 LTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 275 dvasskDAYYEKAQEgFTMFAL--NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEK 352
Cdd:cd07110 241 ------DADLEKAVE-WAMFGCfwNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 353 ILSYIDIGKQEGAKLLCGGERADLGGDlsgGYYVQPTVF-EGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGL 431
Cdd:cd07110 314 VLSFIARGKEEGARLLCGGRRPAHLEK---GYFIAPTVFaDVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2498343516 432 GAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 496
Cdd:cd07110 391 AAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-493 |
1.67e-159 |
|
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: 461.20 E-value: 1.67e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 22 NYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAV 101
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 102 AETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIgELDDNTVAyhfHEPLGVVGQIIPWNFPILMAVWKLAPALA 181
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEE-RRGNSLVV---REPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 182 AGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPV 260
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 261 TLELGGKSPNIFFEdvasskDAYYEKA-QEGFTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNT 339
Cdd:cd07138 237 ALELGGKSANIILD------DADLEKAvPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 340 MMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGgdLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYD 418
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEG--LERGYFVKPTVFADvTPDMTIAREEIFGPVLSIIPYDDED 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2498343516 419 EAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNtYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
23-493 |
4.95e-158 |
|
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: 458.15 E-value: 4.95e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFE-SWG-KTSVTERAIILNKIADRMEANLELLA 100
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPAL 180
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 181 AAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE-NLI 258
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 259 PVTLELGGKSPNIFFEDVASSKDAYYekaqEGFTMFaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTN 338
Cdd:cd07143 250 KVTLELGGKSPNIVFDDADLESAVVW----TAYGIF-FNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 339 TMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERAdlgGDLsgGYYVQPTVFEGKNS-MRIFQEEIFGPVLSVTSFKDY 417
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRH---GNE--GYFIEPTIFTDVTEdMKIVKEEIFGPVVAVIKFKTE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2498343516 418 DEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07143 400 EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
6-493 |
7.29e-158 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 459.66 E-value: 7.29e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 6 NPGTPGAVMSYKgryDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES--WGKTSVTERAI 83
Cdd:PLN02466 47 EPITPPVQVSYT---QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 84 ILNKIADRMEANLELLAVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQII 163
Cdd:PLN02466 124 ILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQII 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 164 PWNFPILMAVWKLAPALAAGNCIVLKPAEQTPAS-IHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGE 242
Cdd:PLN02466 204 PWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSaLYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 243 TTTGRLIMQYASE-NLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEgFTMFAL--NQGEVCTCPSRALVAKPIYDGFM 319
Cdd:PLN02466 284 TDTGKIVLELAAKsNLKPVTLELGGKSPFIVCE------DADVDKAVE-LAHFALffNQGQCCCAGSRTFVHERVYDEFV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 320 SDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlggdlSGGYYVQPTVFEG-KNSMR 398
Cdd:PLN02466 357 EKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG-----SKGYYIQPTVFSNvQDDML 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 399 IFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIG 478
Cdd:PLN02466 432 IAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIG 511
|
490
....*....|....*
gi 2498343516 479 RENHKMMLDHYQQTK 493
Cdd:PLN02466 512 REKGIYSLNNYLQVK 526
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
42-497 |
2.22e-155 |
|
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: 450.15 E-value: 2.22e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 42 PVTGQVFCEVARGNAKDVDMAVAAGWKAFES-WGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAaDIP 120
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA-DVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 121 LAIDHFRYFAGAIRAQEG-SIGELDDNTVaYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIH 199
Cdd:cd07109 83 AAARYFEYYGGAADKLHGeTIPLGPGYFV-YTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 200 VLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEdvas 278
Cdd:cd07109 162 RLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFA---- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 279 skDAYYEKAQEGF--TMFAlNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDtNTMMGAQASNDQLEKILSY 356
Cdd:cd07109 238 --DADLEAALPVVvnAIIQ-NAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 357 IDIGKQEGAKLLCGGERAdlGGDLSGGYYVQPTVFEGKNS-MRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGV 435
Cdd:cd07109 314 VARARARGARIVAGGRIA--EGAPAGGYFVAPTLLDDVPPdSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2498343516 436 WSRSGDTAYRAGRAIQAGRVWTNTYH-----QYPahaaFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGagggiELP----FGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
42-497 |
2.17e-154 |
|
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: 447.54 E-value: 2.17e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 42 PVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAADIPL 121
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 122 AIDHFRYFAGAIRAQEG-SIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHV 200
Cdd:cd07092 84 AVDNFRFFAGAARTLEGpAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 201 LLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEdvassk 280
Cdd:cd07092 164 LAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 281 DAYYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDi 359
Cdd:cd07092 238 DADLDAAVAGIATAGYyNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 360 GKQEGAKLLCGGERADlgGDlsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSR 438
Cdd:cd07092 317 RAPAHARVLTGGRRAE--GP---GYFYEPTVVAGvAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2498343516 439 SGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-497 |
2.39e-153 |
|
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: 445.27 E-value: 2.39e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAADI 119
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIH 199
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 200 VLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvaSS 279
Cdd:cd07108 162 LLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD--AD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 280 KDAYYEKAQEG--FTmfalNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYI 357
Cdd:cd07108 240 LDDAVDGAIAGmrFT----RQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 358 DIGKQE-GAKLLCGGErADLGGDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGV 435
Cdd:cd07108 316 DLGLSTsGATVLRGGP-LPGEGPLADGFFVQPTIFSGvDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 436 WSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRE-NHKMMLDHYQQTKNLLV 497
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREaSLEGMLEHFTQKKTVNI 457
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-493 |
2.27e-152 |
|
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: 443.10 E-value: 2.27e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVA 102
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 103 ETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAA 182
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 183 GNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVT 261
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 262 LELGGKSPNIFFedvassKDAYYEKAQEGftmfALN-----QGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLD 336
Cdd:TIGR01804 241 MELGGKSPLIVF------DDADLESAVDG----AMLgnffsAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 337 TNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlGGDLSGGYYVQPTVFEGKN-SMRIFQEEIFGPVLSVTSFK 415
Cdd:TIGR01804 311 EATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPE-NVGLQNGFFVEPTVFADCTdDMTIVREEIFGPVMTVLTFS 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2498343516 416 DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:TIGR01804 390 DEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
22-497 |
8.57e-150 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 436.65 E-value: 8.57e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 22 NYIGGKYVApSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAV 101
Cdd:PRK13473 5 LLINGELVA-GEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 102 AETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSI-GE-LDDNTvAYHFHEPLGVVGQIIPWNFPILMAVWKLAPA 179
Cdd:PRK13473 84 LESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAaGEyLEGHT-SMIRRDPVGVVASIAPWNYPLMMAAWKLAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 180 LAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIP 259
Cdd:PRK13473 163 LAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 260 VTLELGGKSPNIFFEdvasskDAYYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTN 338
Cdd:PRK13473 243 THLELGGKAPVIVFD------DADLDAVVEGIRTFGYyNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 339 TMMGAQASNDQLEKILSYIDIGKQEG-AKLLCGGERADLggdlsGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKD 416
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDG-----KGYYYEPTLLAGaRQDDEIVQREVFGPVVSVTPFDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 417 YDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 496
Cdd:PRK13473 392 EDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVM 471
|
.
gi 2498343516 497 V 497
Cdd:PRK13473 472 V 472
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
39-493 |
1.60e-149 |
|
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: 435.52 E-value: 1.60e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 39 NITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWG-KTSVTERAIILNKIADRMEANLELLA---VAETwdnGKAVRET 114
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRallVAEV---GAPVMTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 115 MAADIPLAIDHFRYFAGAIRAQEGSIgELDDNTVAYHF------HEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVL 188
Cdd:cd07089 78 RAMQVDGPIGHLRYFADLADSFPWEF-DLPVPALRGGPgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 189 KPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGK 267
Cdd:cd07089 157 KPAPDTPLSALLLGEIIAETdLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 268 SPNIFFEDvasskdAYYEKAQ-EGFTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQAS 346
Cdd:cd07089 237 SANIVLDD------ADLAAAApAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 347 NDQLEKILSYIDIGKQEGAKLLCGGERADlggDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIAN 425
Cdd:cd07089 311 AAQRDRVEGYIARGRDEGARLVTGGGRPA---GLDKGFYVEPTLFADvDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIAN 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2498343516 426 DTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07089 388 DSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-497 |
1.15e-148 |
|
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: 433.54 E-value: 1.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES--WGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRA------QEGSIGelddNTVAYHfHEPLGVVGQIIPWNFPILMAVW 174
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfeerRPGSGG----GHVLVR-REPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 175 KLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYA 253
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 254 SENLIPVTLELGGKSPNIFFEDvasskdAYYEKAQEG-FTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQG 332
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDD------ADLDAAVPGlVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 333 NPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlggDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSV 411
Cdd:cd07139 310 DPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPA---GLDRGWFVEPTLFADvDNDMRIAQEEIFGPVLSV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 412 TSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPaHAAFGGYKQSGIGRENHKMMLDHYQQ 491
Cdd:cd07139 387 IPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDF-GAPFGGFKQSGIGREGGPEGLDAYLE 465
|
....*.
gi 2498343516 492 TKNLLV 497
Cdd:cd07139 466 TKSIYL 471
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
40-497 |
1.68e-148 |
|
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: 432.53 E-value: 1.68e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES--WGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAa 117
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 118 DIPLAIDHFRYFAGAIRAQEG-SIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGdSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 197 SIHVLLEL-IEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFed 275
Cdd:cd07118 161 TTLMLAELlIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVF-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 276 vassKDAYYEKAQEGFTM-FALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKIL 354
Cdd:cd07118 239 ----ADADLDAAADAVVFgVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 355 SYIDIGKQEGAKLLCGGERADLGGdlsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGA 433
Cdd:cd07118 315 DYVDAGRAEGATLLLGGERLASAA----GLFYQPTIFTDvTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2498343516 434 GVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07118 391 GVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
23-503 |
1.38e-145 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 426.93 E-value: 1.38e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFE--SWGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPAL 180
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 181 AAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE-NLI 258
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 259 PVTLELGGKSPNIFFEDvasskdAYYEKAQEgFTMFAL--NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLD 336
Cdd:PLN02766 264 QVSLELGGKSPLLIFDD------ADVDMAVD-LALLGIfyNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 337 TNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERAdlgGDlsGGYYVQPTVF-EGKNSMRIFQEEIFGPVLSVTSFK 415
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPC---GD--KGYYIEPTIFtDVTEDMKIAQDEIFGPVMSLMKFK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 416 DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 495
Cdd:PLN02766 412 TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
....*...
gi 2498343516 496 LVSYAEGP 503
Cdd:PLN02766 492 VTPLYNSP 499
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-493 |
6.69e-144 |
|
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: 420.69 E-value: 6.69e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAaDI 119
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG-EV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAIDHFRYFAGAIRAQEGSIGELDDNTVAYH-FHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASI 198
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILvIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 199 HVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDva 277
Cdd:cd07103 161 LALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 278 sskdAYYEKAQEGfTMFA--LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILS 355
Cdd:cd07103 239 ----ADLDKAVDG-AIASkfRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 356 YIDIGKQEGAKLLCGGERADLGGdlsggYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAG 434
Cdd:cd07103 314 LVEDAVAKGAKVLTGGKRLGLGG-----YFYEPTVLTDvTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2498343516 435 VWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07103 389 VFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETK 447
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-493 |
8.29e-141 |
|
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: 412.69 E-value: 8.29e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAaDI 119
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAIDHFRYFAGAIRAQEgsIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIH 199
Cdd:cd07106 81 GGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 200 VLLELIEDLLPAGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDVass 279
Cdd:cd07106 159 KLGELAQEVLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 280 kDayYEKAQEGFTMFA-LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYID 358
Cdd:cd07106 235 -D--IDAVAPKLFWGAfINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 359 IGKQEGAKLLCGGERADlggdlSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWS 437
Cdd:cd07106 312 DAKAKGAKVLAGGEPLD-----GPGYFIPPTIVDDpPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2498343516 438 RSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
40-499 |
8.09e-140 |
|
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: 410.61 E-value: 8.09e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAaDI 119
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIH 199
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 200 VLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDVASS 279
Cdd:cd07107 161 RLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 280 KDAYYEKAQEGFTMfalnQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDI 359
Cdd:cd07107 241 AAADAAVAGMNFTW----CGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 360 GKQEGAKLLCGGERADlGGDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSR 438
Cdd:cd07107 317 AKREGARLVTGGGRPE-GPALEGGFYVEPTVFADvTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2498343516 439 SGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY 499
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
23-507 |
1.35e-139 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 411.82 E-value: 1.35e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAF-----ESWGKTSVTERAIILNKIADRMEANLE 97
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 98 LLAVAETWDNGKAVRETmAADIPLAIDHFRYFAG---AIRAQEGSIGELDDNTVAYHF-HEPLGVVGQIIPWNFPILMAV 173
Cdd:PLN02467 91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADlaeALDAKQKAPVSLPMETFKGYVlKEPLGVVGLITPWNYPLLMAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 174 WKLAPALAAGNCIVLKPAEQtpASIhVLLEL----IEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLI 249
Cdd:PLN02467 170 WKVAPALAAGCTAVLKPSEL--ASV-TCLELadicREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 250 MQYASENLIPVTLELGGKSPNIFFEDVAsskdayYEKAQEgFTMFAL--NQGEVCTCPSRALVAKPIYDGFMSDGIARVG 327
Cdd:PLN02467 247 MTAAAQMVKPVSLELGGKSPIIVFDDVD------LDKAVE-WAMFGCfwTNGQICSATSRLLVHERIASEFLEKLVKWAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 328 KIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERadlGGDLSGGYYVQPTVFEG-KNSMRIFQEEIFG 406
Cdd:PLN02467 320 NIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR---PEHLKKGFFIEPTIITDvTTSMQIWREEVFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 407 PVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMML 486
Cdd:PLN02467 397 PVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGL 476
|
490 500
....*....|....*....|.
gi 2498343516 487 DHYQQTKNLLVSYAEGPMGFF 507
Cdd:PLN02467 477 ENYLSVKQVTKYISDEPWGWY 497
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
20-493 |
3.26e-139 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 409.72 E-value: 3.26e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVAPSSGEyfENITPV-TGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLEL 98
Cdd:cd07097 1 YRNYIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 99 LAVAETWDNGKAVRETMAaDIPLAIDHFRYFAGAIRAQEG-SIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLA 177
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGeTLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 178 PALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASEN 256
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 257 LIPVTLELGGKSPNIFfedvasSKDAYYEKAQEGFTMFA-LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPL 335
Cdd:cd07097 238 GARVQLEMGGKNPLVV------LDDADLDLAVECAVQGAfFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 336 DTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGgdlSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSF 414
Cdd:cd07097 312 DEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRP---DEGYYLAPALFAGvTNDMRIAREEIFGPVAAVIRV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 415 KDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN--TYHqYPAHAAFGGYKQSGIG-RENHKMMLDHYQQ 491
Cdd:cd07097 389 RDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAG-VDYHVPFGGRKGSSYGpREQGEAALEFYTT 467
|
..
gi 2498343516 492 TK 493
Cdd:cd07097 468 IK 469
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
64-497 |
4.14e-139 |
|
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: 405.46 E-value: 4.14e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 64 AAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKaVRETMAADIPLAIDHFRYFAGAIRAQEGS-IGE 142
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGK-PIEEALGEVARAIDTFRYAAGLADKLGGPeLPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 143 LDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIED-LLPAGVLNIVNGFG 221
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEaGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 222 IEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEG--FTMFaLNQG 299
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDE------DADLDAAVEGavFGAF-FNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 300 EVCTCPSRALVAKPIYDGFMsdgiarvgkiiqgnpldtntmmgaqasnDQLEKILSYIDigkqegakllcggeradlggd 379
Cdd:cd06534 233 QICTAASRLLVHESIYDEFV----------------------------EKLVTVLVDVD--------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 380 lsggyyvqptvfegkNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNT 459
Cdd:cd06534 264 ---------------PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYIND 328
|
410 420 430
....*....|....*....|....*....|....*....
gi 2498343516 460 YH-QYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd06534 329 SSiGVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
15-489 |
1.15e-138 |
|
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: 408.71 E-value: 1.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 15 SYKGRYDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEA 94
Cdd:cd07111 17 AHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 95 NLELLAVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEgsigelddntVAYHFHEPLGVVGQIIPWNFPILMAVW 174
Cdd:cd07111 97 HQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD----------TELAGWKPVGVVGQIVPWNFPLLMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 175 KLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIMQYA 253
Cdd:cd07111 167 KICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 254 SENLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEGFTMFA-LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQG 332
Cdd:cd07111 246 AGTGKKLSLELGGKSPFIVFD------DADLDSAVEGIVDAIwFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 333 NPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAkllcggERADLGGDLSG-GYYVQPTVFEGKN-SMRIFQEEIFGPVLS 410
Cdd:cd07111 320 DPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGA------DVFQPGADLPSkGPFYPPTLFTNVPpASRIAQEEIFGPVLV 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2498343516 411 VTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHY 489
Cdd:cd07111 394 VLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
23-494 |
1.18e-134 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 397.79 E-value: 1.18e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVA 102
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 103 ETWDNGKAVRETmAADIPLAIDHFRYFAGAIRAQEGSIGELD-DNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALA 181
Cdd:cd07088 81 IVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 182 AGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPV 260
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 261 TLELGGKSPNIFFedvassKDAYYEKAQEG-FTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNT 339
Cdd:cd07088 240 SLELGGKAPAIVM------KDADLDLAVKAiVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 340 MMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGdlsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYD 418
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEK----GYFYEPTVLTNvRQDMEIVQEEIFGPVLPVVKFSSLD 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2498343516 419 EAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 494
Cdd:cd07088 390 EAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKV 465
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
22-499 |
6.65e-130 |
|
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: 385.93 E-value: 6.65e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 22 NYIGGKYVAPSSGEYFENITPVTG-QVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAaDIPLAIDHFRYFAGAIRAQEGSI--GELDDNTvAYHFHEPLGVVGQIIPWNFPILMAVWKLAP 178
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETvpSELPNKD-AMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 179 ALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENL 257
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 258 IPVTLELGGKSPNIFFEDvasskdAYYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLD 336
Cdd:cd07131 239 KRVALEMGGKNPIIVMDD------ADLDLALEGALWSAFgTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 337 TNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlGGDLSGGYYVQPTVFEGKN-SMRIFQEEIFGPVLSVTSFK 415
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLT-GGGYEKGYFVEPTVFTDVTpDMRIAQEEIFGPVVALIEVS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 416 DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTyhqyP-----AHAAFGGYKQSGIG-RENHKMMLDHY 489
Cdd:cd07131 392 SLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNA----PtigaeVHLPFGGVKKSGNGhREAGTTALDAF 467
|
490
....*....|
gi 2498343516 490 QQTKNLLVSY 499
Cdd:cd07131 468 TEWKAVYVDY 477
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
23-498 |
1.71e-127 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 380.40 E-value: 1.71e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES--WGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPAL 180
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 181 AAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE-NLI 258
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 259 PVTLELGGKSPNIFFEDVASSKDAYYEKAQEGFtmfaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTN 338
Cdd:PRK09847 263 RVWLEAGGKSANIVFADCPDLQQAASATAAGIF----YNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 339 TMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGgdlsggyYVQPTVF-EGKNSMRIFQEEIFGPVLSVTSFKDY 417
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAA-------AIGPTIFvDVDPNASLSREEIFGPVLVVTRFTSE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 418 DEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:PRK09847 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
.
gi 2498343516 498 S 498
Cdd:PRK09847 492 S 492
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
23-499 |
1.26e-124 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 372.54 E-value: 1.26e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVApSSGEYFENIT-PVTGQVFCEVARGNAKDVDMAVAAGWKAFES-WGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:cd07113 3 FIDGRPVA-GQSEKRLDITnPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEG-----SI----GElddNTVAYHFHEPLGVVGQIIPWNFPILM 171
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGetlapSIpsmqGE---RYTAFTRREPVGVVAGIVPWNFSVMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 172 AVWKLAPALAAGNCIVLKPAEQTPASIHVLLEL-IEDLLPAGVLNIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIM 250
Cdd:cd07113 159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAELaKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 251 QYASENLIPVTLELGGKSPNIFFedvassKDAYYEKAQEG-FTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKI 329
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFL------KDADIDWVVEGlLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 330 IQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlgGDlsgGYYVQPTVFEGKNS-MRIFQEEIFGPV 408
Cdd:cd07113 312 QVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA--GE---GYFVQPTLVLARSAdSRLMREETFGPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 409 LSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDH 488
Cdd:cd07113 387 VSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDD 466
|
490
....*....|.
gi 2498343516 489 YQQTKNLLVSY 499
Cdd:cd07113 467 YTELKSVMIRY 477
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
40-493 |
1.91e-124 |
|
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: 371.29 E-value: 1.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFE--SWgKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAa 117
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 118 DIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPAS 197
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 198 IHVLLELIEDL--LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFED 275
Cdd:cd07120 160 NAAIIRILAEIpsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 276 vaSSKDAYYEKAQEGFTMFAlnqGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILS 355
Cdd:cd07120 240 --ADLDAALPKLERALTIFA---GQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 356 YIDIGKQEGAKLLCGGERadLGGDLSGGYYVQPTVFE-GKNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAG 434
Cdd:cd07120 315 MVERAIAAGAEVVLRGGP--VTEGLAKGAFLRPTLLEvDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAAS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2498343516 435 VWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07120 393 VWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYK 451
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
20-499 |
1.01e-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: 362.97 E-value: 1.01e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFES--WGKTSVTERAIILNKIADRMEANLE 97
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 98 LLAVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELD----DNTVAYHFHEPLGVVGQIIPWNFPILMAV 173
Cdd:cd07140 86 ELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 174 WKLAPALAAGNCIVLKPAEQTPASIHVLLEL-IEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQY 252
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 253 ASE-NLIPVTLELGGKSPNIFFedvassKDAYYEKA-QEGFTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKII 330
Cdd:cd07140 246 CAVsNLKKVSLELGGKSPLIIF------ADCDMDKAvRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 331 QGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLggdlsGGYYVQPTVFEG-KNSMRIFQEEIFGPVL 409
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR-----PGFFFEPTVFTDvEDHMFIAKEESFGPIM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 410 SVTSFK--DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLD 487
Cdd:cd07140 395 IISKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALN 474
|
490
....*....|..
gi 2498343516 488 HYQQTKNLLVSY 499
Cdd:cd07140 475 EYLKTKTVTIEY 486
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
24-497 |
2.35e-114 |
|
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: 346.22 E-value: 2.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 24 IGGKYVApSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAE 103
Cdd:TIGR03374 6 INGELVS-GEGEKQPVYNPATGEVILEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENAQVFAELE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 104 TWDNGKAVRETMAADIPLAIDHFRYFAGAIRAQEGSI-GELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAA 182
Cdd:TIGR03374 85 SRNCGKPLHSVFNDEIPAIVDVFRFFAGAARCLSGLAaGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 183 GNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTL 262
Cdd:TIGR03374 165 GNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGKTVGDPLTGHEKVRMVSLTGSIATGEHILSHTAPSIKRTHM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 263 ELGGKSPNIFFEdvasskDAYYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMM 341
Cdd:TIGR03374 245 ELGGKAPVIVFD------DADIDAVVEGVRTFGFyNAGQDCTAACRIYAQRGIYDTLVEKLGAAVATLKSGAPDDESTEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 342 GAQASNDQLEKILSYIDIGKQEG-AKLLCGGERADlggdlSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDE 419
Cdd:TIGR03374 319 GPLSSLAHLERVMKAVEEAKALGhIKVITGGEKRK-----GNGYYFAPTLLAGaKQDDAIVQKEVFGPVVSITSFDDEEQ 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2498343516 420 AISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:TIGR03374 394 VVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHIMV 471
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
20-478 |
1.64e-113 |
|
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: 345.36 E-value: 1.64e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVapSSGEYFENITPV-TGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLEL 98
Cdd:cd07124 33 YPLVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 99 LAVAETWDNGKAVRETMAaDIPLAIDHFRYFAG-AIRAQEGSIGELDDNTVAYhFHEPLGVVGQIIPWNFPILMAVWKLA 177
Cdd:cd07124 111 LAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAReMLRLRGFPVEMVPGEDNRY-VYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 178 PALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYAS-- 254
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 255 ----ENLIPVTLELGGKSPNIFfedvasSKDAYYEKAQEGFTMFALN-QGEVCTCPSRALVAKPIYDGFMSDGIARVGKI 329
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIV------DEDADLDEAAEGIVRSAFGfQGQKCSACSRVIVHESVYDEFLERLVERTKAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 330 IQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGaKLLCGGERADLGgdlSGGYYVQPTVFEGKNSM-RIFQEEIFGPV 408
Cdd:cd07124 343 KVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA---AEGYFVQPTIFADVPPDhRLAQEEIFGPV 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2498343516 409 LSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGrvwtNTYHQYPAHAA------FGGYKQSGIG 478
Cdd:cd07124 419 LAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVG----NLYANRKITGAlvgrqpFGGFKMSGTG 490
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-493 |
2.28e-112 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 339.51 E-value: 2.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 58 DVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEAN---LELLAVAETwdnG----KAVRETMAAdiplaIDHFRYFA 130
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERrdeIADWLIRES---GstrpKAAFEVGAA-----IAILREAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 131 GAIRAQEGSIGELD-DNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLL-ELIEDL 208
Cdd:cd07104 73 GLPRRPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 209 -LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvasskdAYYEKA 287
Cdd:cd07104 153 gLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDD------ADLDLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 288 QE--GFTMFaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGA 365
Cdd:cd07104 227 VSaaAFGAF-LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 366 KLLCGGERADLggdlsggyYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAY 444
Cdd:cd07104 306 RLLTGGTYEGL--------FYQPTVLSDvTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAM 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2498343516 445 RAGRAIQAGRVWTN--TYHQYPaHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07104 378 AFAERLETGMVHINdqTVNDEP-HVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
37-480 |
1.11e-111 |
|
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: 338.54 E-value: 1.11e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 37 FENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNG----KAVR 112
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGstygKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 113 ETMaadipLAIDHFRYFAGAIRAQEGSIGELDDN-TVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPA 191
Cdd:cd07150 81 ETT-----FTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 192 EQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPN 270
Cdd:cd07150 156 EETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 271 IFFEDVasskDAYYEKAQEGFTMFaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQL 350
Cdd:cd07150 236 IVLADA----DLDYAVRAAAFGAF-MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 351 EKILSYIDIGKQEGAKLLCGGERAdlggdlsgGYYVQPTVFEGKNS-MRIFQEEIFGPVLSVTSFKDYDEAISIANDTLY 429
Cdd:cd07150 311 ERIKRQVEDAVAKGAKLLTGGKYD--------GNFYQPTVLTDVTPdMRIFREETFGPVTSVIPAKDAEEALELANDTEY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 430 GLGAGVWSRSGDTAYRAGRAIQAGRVWTN--TYHQyPAHAAFGGYKQSGIGRE 480
Cdd:cd07150 383 GLSAAILTNDLQRAFKLAERLESGMVHINdpTILD-EAHVPFGGVKASGFGRE 434
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
22-480 |
1.11e-103 |
|
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: 318.74 E-value: 1.11e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 22 NYIGGKYVApSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAV 101
Cdd:cd07086 1 GVIGGEWVG-SGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 102 AETWDNGKAVRETMAaDIPLAIDHFRYFAGAIRAQEGSI--GELDDNtVAYHFHEPLGVVGQIIPWNFPilMAV--WKLA 177
Cdd:cd07086 80 LVSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTipSERPGH-RLMEQWNPLGVVGVITAFNFP--VAVpgWNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 178 PALAAGNCIVLKPAEQTPASIHVLLELIEDLL-----PAGVLNIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIMQY 252
Cdd:cd07086 156 IALVCGNTVVWKPSETTPLTAIAVTKILAEVLeknglPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 253 ASENLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQ 331
Cdd:cd07086 235 VARRFGRVLLELGGNNAIIVMD------DADLDLAVRAVLFAAVgTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 332 GNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlggDLSGGYYVQPTVFEGKN-SMRIFQEEIFGPVLS 410
Cdd:cd07086 309 GDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRID---GGEPGNYVEPTIVTGVTdDARIVQEETFAPILY 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2498343516 411 VTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRA--IQAGRVWTNTyhqyP-----AHAAFGGYKQSGIGRE 480
Cdd:cd07086 386 VIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNI----PtsgaeIGGAFGGEKETGGGRE 458
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
19-493 |
2.72e-103 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 318.56 E-value: 2.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 19 RYDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLEL 98
Cdd:PLN02278 24 RTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 99 LAVAETWDNGKAVRETMAaDIPLAIDHFRYFAG-AIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLA 177
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAIG-EVAYGASFLEYFAEeAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 178 PALAAGNCIVLKPAEQTPASIHVLLEL-IEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASEN 256
Cdd:PLN02278 183 PALAAGCTVVVKPSELTPLTALAAAELaLQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 257 LIPVTLELGGKSPNIFFEDV---ASSKDAYYEKAQegftmfalNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGN 333
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDAdldVAVKGALASKFR--------NSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 334 PLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGDlsggYYvQPTVF-EGKNSMRIFQEEIFGPVLSVT 412
Cdd:PLN02278 335 GFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGT----FY-EPTVLgDVTEDMLIFREEVFGPVAPLT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 413 SFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQT 492
Cdd:PLN02278 410 RFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEI 489
|
.
gi 2498343516 493 K 493
Cdd:PLN02278 490 K 490
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-479 |
1.05e-102 |
|
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: 315.31 E-value: 1.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAvRETMAADI 119
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAIDHFRYFAG----AIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTP 195
Cdd:cd07099 80 LLALEAIDWAARnaprVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 196 ASIHVLLELIEDL-LPAGVLNIVNGFGiEAGAPLAShNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFE 274
Cdd:cd07099 160 LVGELLAEAWAAAgPPQGVLQVVTGDG-ATGAALID-AGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 275 DvASSKDAYYEKAQEGFTmfalNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKIL 354
Cdd:cd07099 238 D-ADLERAAAAAVWGAMV----NAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 355 SYIDIGKQEGAKLLCGGERADlggdlSGGYYVQPTVFEGKN-SMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGA 433
Cdd:cd07099 313 RHVDDAVAKGAKALTGGARSN-----GGGPFYEPTVLTDVPhDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2498343516 434 GVWSRSGDTAYRAGRAIQAGRVWTN---TYHQYPAhAAFGGYKQSGIGR 479
Cdd:cd07099 388 SVFSRDLARAEAIARRLEAGAVSINdvlLTAGIPA-LPFGGVKDSGGGR 435
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-480 |
7.85e-102 |
|
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: 313.13 E-value: 7.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 37 FENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMA 116
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 117 aDIPLAIDHFRYFAGAIRAQEGSIGELDD-----NTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPA 191
Cdd:cd07145 81 -EVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 192 EQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPN 270
Cdd:cd07145 160 SNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 271 IFFedvassKDAYYEKAQEGFTMFA-LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQ 349
Cdd:cd07145 240 IVL------KDADLERAVSIAVRGRfENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 350 LEKILSYIDIGKQEGAKLLCGGERADlggdlsgGYYVQPTVFEGKN-SMRIFQEEIFGPVLSVTSFKDYDEAISIANDTL 428
Cdd:cd07145 314 VERMENLVNDAVEKGGKILYGGKRDE-------GSFFPPTVLENDTpDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 429 YGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQY-PAHAAFGGYKQSGIGRE 480
Cdd:cd07145 387 YGLQASVFTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGRE 439
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-480 |
4.27e-101 |
|
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: 311.07 E-value: 4.27e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 37 FENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMA 116
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 117 aDIPLAIDHFRYFAGAIRAQEGSIGELD-----DNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPA 191
Cdd:cd07149 81 -EVDRAIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 192 EQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASenLIPVTLELGGKSPN 270
Cdd:cd07149 160 SQTPLSALKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 271 IFFEDVAsskdayYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQ 349
Cdd:cd07149 238 IVDADAD------LEKAVERCVSGAFaNAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 350 LEKILSYIDIGKQEGAKLLCGGERAdlggdlsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTL 428
Cdd:cd07149 312 AERIEEWVEEAVEGGARLLTGGKRD--------GAILEPTVLTDvPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSP 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 429 YGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPA-HAAFGGYKQSGIGRE 480
Cdd:cd07149 384 YGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGRE 436
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-493 |
5.55e-101 |
|
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: 311.55 E-value: 5.55e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 26 GKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLEL---LAVA 102
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEiveWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 103 ET----------WDNGKAV-REtmAADIPLAIDhfryfaGAIRAqegSIGELDDNTVayhFHEPLGVVGQIIPWNFPILM 171
Cdd:cd07151 81 ESgstrikanieWGAAMAItRE--AATFPLRME------GRILP---SDVPGKENRV---YREPLGVVGVISPWNFPLHL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 172 AVWKLAPALAAGNCIVLKPAEQTPASIHVLL-ELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLI 249
Cdd:cd07151 147 SMRSVAPALALGNAVVLKPASDTPITGGLLLaKIFEEAgLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 250 MQYASENLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEG--FTMFaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVG 327
Cdd:cd07151 227 GELAGRHLKKVALELGGNNPFVVLE------DADIDAAVNAavFGKF-LHQGQICMAINRIIVHEDVYDEFVEKFVERVK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 328 KIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLggdlsggyYVQPTVFEG-KNSMRIFQEEIFG 406
Cdd:cd07151 300 ALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN--------VLEPTVLSDvTNDMEIAREEIFG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 407 PVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN--TYHQYPaHAAFGGYKQSGIGRENHKM 484
Cdd:cd07151 372 PVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDEP-HVPFGGEKNSGLGRFNGEW 450
|
....*....
gi 2498343516 485 MLDHYQQTK 493
Cdd:cd07151 451 ALEEFTTDK 459
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
13-476 |
2.37e-100 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 311.48 E-value: 2.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 13 VMSYKGR-YDNYIGGKYVapSSGEYFENITPV-TGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIAD 90
Cdd:PRK03137 29 VEKELGQdYPLIIGGERI--TTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 91 RM-EANLELLAVaETWDNGKAVRETmAADIPLAIDHFRYFA-GAIRAQEGSI-----GEldDNTvayHFHEPLGVVGQII 163
Cdd:PRK03137 107 IIrRRKHEFSAW-LVKEAGKPWAEA-DADTAEAIDFLEYYArQMLKLADGKPvesrpGE--HNR---YFYIPLGVGVVIS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 164 PWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGE 242
Cdd:PRK03137 180 PWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 243 TTTGRLIMQYASEN------LIPVTLELGGKSPNIFfedvasSKDAYYEKAQEGFTMFALN-QGEVCTCPSRALVAKPIY 315
Cdd:PRK03137 260 REVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVV------DEDADLDLAAESIVASAFGfSGQKCSACSRAIVHEDVY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 316 DGFMSDGIARVGKIIQGNPLDtNTMMGAQASNDQLEKILSYIDIGKQEGaKLLCGGERADlggdlSGGYYVQPTVFEGKN 395
Cdd:PRK03137 334 DEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDD-----SKGYFIQPTIFADVD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 396 SM-RIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNT--------YHqypah 466
Cdd:PRK03137 407 PKaRIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRgctgaivgYH----- 481
|
490
....*....|
gi 2498343516 467 aAFGGYKQSG 476
Cdd:PRK03137 482 -PFGGFNMSG 490
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
40-495 |
7.63e-97 |
|
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: 300.38 E-value: 7.63e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVR----ETM 115
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRhafeEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 116 aaDIPLAIDHFRYFAGAI---RAQEGSIGELDDNTVAYHfhePLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAE 192
Cdd:cd07101 81 --DVAIVARYYARRAERLlkpRRRRGAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 193 QTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIrkIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNI 271
Cdd:cd07101 156 QTALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 272 FFEDvasskdAYYEKAQEG--FTMFAlNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQ 349
Cdd:cd07101 234 VLED------ADLDKAAAGavRACFS-NAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 350 LEKILSYIDIGKQEGAKLLCGGE-RADLGGdlsggYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDT 427
Cdd:cd07101 307 LDRVTAHVDDAVAKGATVLAGGRaRPDLGP-----YFYEPTVLTGvTEDMELFAEETFGPVVSIYRVADDDEAIELANDT 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 428 LYGLGAGVWSRSGDTAYRAGRAIQAGRVwtNTYHQYPA-----HAAFGGYKQSGIGRENHKMMLDHYQQTKNL 495
Cdd:cd07101 382 DYGLNASVWTRDGARGRRIAARLRAGTV--NVNEGYAAawasiDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
29-479 |
5.80e-96 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 300.26 E-value: 5.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 29 VAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNG 108
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 109 K----AVRETMaaDIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGN 184
Cdd:PRK09407 106 KarrhAFEEVL--DVALTARYYARRAPKLLAPRRRAGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 185 CIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLAshNNIRKIAFTGETTTGRLIMQYASENLIPVTLE 263
Cdd:PRK09407 184 AVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLIGFSLE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 264 LGGKSPNIFFEDvasskdAYYEKAQEG--FTMFAlNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMM 341
Cdd:PRK09407 262 LGGKNPMIVLDD------ADLDKAAAGavRACFS-NAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 342 GAQASNDQLEKILSYIDIGKQEGAKLLCGGE-RADLGGdlsggYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDE 419
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKaRPDLGP-----LFYEPTVLTGvTPDMELAREETFGPVVSVYPVADVDE 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2498343516 420 AISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVwtNTYHQY-PAHAAF----GGYKQSGIGR 479
Cdd:PRK09407 410 AVERANDTPYGLNASVWTGDTARGRAIAARIRAGTV--NVNEGYaAAWGSVdapmGGMKDSGLGR 472
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-493 |
3.16e-92 |
|
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: 287.55 E-value: 3.16e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 58 DVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAvaetwdngKAVRETMAAD-------IPLAIDHFRYFA 130
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFI--------EAMMEETGATaawagfnVDLAAGMLREAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 131 GAI-RAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASiHVLLE--LIED 207
Cdd:cd07105 73 SLItQIIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRT-HWLIGrvFHEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 208 LLPAGVLNIVngFGIEAGAP-----LASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvasskdA 282
Cdd:cd07105 152 GLPKGVLNVV--THSPEDAPevveaLIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLED------A 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 283 YYEKAQEGFTMFA-LNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDtntmmGAQASNDQLEKILSYIDIGK 361
Cdd:cd07105 224 DLDAAANAALFGAfLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 362 QEGAKLLCGGERADLGGDLSggyyVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSG 440
Cdd:cd07105 299 SKGAKLVVGGLADESPSGTS----MPPTILDNvTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2498343516 441 DTAYRAGRAIQAGRVWTN--TYHQYPaHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07105 375 ARALAVAKRIESGAVHINgmTVHDEP-TLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-480 |
4.49e-91 |
|
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: 284.74 E-value: 4.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 59 VDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAaDIPLAIDHFRYFAG---AIRA 135
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAEnaeAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 136 QEGSIGELDDNTVAYhfhEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVL 214
Cdd:cd07100 80 DEPIETDAGKAYVRY---EPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 215 NIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvasskdAYYEKAQEGFT-- 292
Cdd:cd07100 157 QNLLI-DSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDD------ADLDKAVKTAVkg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 293 -MfaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGG 371
Cdd:cd07100 230 rL--QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 372 ERADlggdlSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAI 450
Cdd:cd07100 308 KRPD-----GPGAFYPPTVLTDvTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL 382
|
410 420 430
....*....|....*....|....*....|
gi 2498343516 451 QAGRVWTNTYHQYPAHAAFGGYKQSGIGRE 480
Cdd:cd07100 383 EAGMVFINGMVKSDPRLPFGGVKRSGYGRE 412
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
85-493 |
3.16e-86 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 271.61 E-value: 3.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 85 LNKIADRMEANLELLAVAETWDNGKaVRETMAADIPLAIDHFRYFAGAIRAQEGSIGELD-DNTVAYHFHEPLGVVGQII 163
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK-IQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDrPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 164 PWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGE 242
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 243 TTTGRLIMQYASENLIPVTLELGGKSPNIFFED------VASSKDAYyekaqegftmfALNQGEVCTCPSRALVAKPIYD 316
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDadldlaVKAIVDSR-----------VINSGQVCNCAERVYVQKGIYD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 317 GFMSDGIARVGKIIQGNPLDTNTM-MGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlggdlSGGYYVQPTVF-EGK 394
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVE-----GKGYYYPPTLLlDVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 395 NSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTyHQYPAHAAF-GGYK 473
Cdd:PRK10090 304 QEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR-ENFEAMQGFhAGWR 382
|
410 420
....*....|....*....|
gi 2498343516 474 QSGIGRENHKMMLDHYQQTK 493
Cdd:PRK10090 383 KSGIGGADGKHGLHEYLQTQ 402
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
22-478 |
3.24e-86 |
|
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: 273.62 E-value: 3.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 22 NYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAV 101
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 102 AETWDNGKAVRETMaADIPLAIDHFRyFAGAI------RAQEGSIGELDdntvAYHFHEPLGVVGQIIPWNFPILMAVWK 175
Cdd:cd07085 83 LITLEHGKTLADAR-GDVLRGLEVVE-FACSIphllkgEYLENVARGID----TYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 176 LAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYAS 254
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 255 ENLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGN 333
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMP------DADLEQTANALVGAAFgAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 334 PLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGeRADLGGDLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVT 412
Cdd:cd07085 310 GDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDG-RGVKVPGYENGNFVGPTILDNvTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2498343516 413 SFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYP-AHAAFGGYKQSGIG 478
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPlAFFSFGGWKGSFFG 455
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
20-480 |
5.05e-86 |
|
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: 272.91 E-value: 5.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVApSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKT-SVTERAIILNKIADRMEANLEL 98
Cdd:cd07082 2 FKYLINGEWKE-SSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 99 LAVAETWDNGKAVRETMAaDIPLAIDHFRYFAGAIRAQEG--SIGEL---DDNTVAYHFHEPLGVVGQIIPWNFPILMAV 173
Cdd:cd07082 81 VANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGdsLPGDWfpgTKGKIAQVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 174 WKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQY 252
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 253 ASenLIPVTLELGGKSPNIFFEDvASSKDAYYEKAQEGFTmFAlnqGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQG 332
Cdd:cd07082 240 HP--MKRLVLELGGKDPAIVLPD-ADLELAAKEIVKGALS-YS---GQRCTAIKRVLVHESVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 333 NPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERAdlggdlsGGYYVQPTVFEGKNS-MRIFQEEIFGPVLSV 411
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGRE-------GGNLIYPTLLDPVTPdMRLAWEEPFGPVLPI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 412 TSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQY-PAHAAFGGYKQSGIGRE 480
Cdd:cd07082 386 IRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRgPDHFPFLGRKDSGIGTQ 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-497 |
5.31e-85 |
|
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: 269.50 E-value: 5.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 37 FENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETmA 116
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 117 ADIPLAIDHFRYFAGAIRAQEGSIGELD-----DNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPA 191
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 192 EQTPASIHVLLE-LIEDLLPAGVLNIVNgFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENliPVTLELGGKSPn 270
Cdd:cd07147 160 SRTPLSALILGEvLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 271 iffedVASSKDAYYEKAQEGFTMFALNQ-GEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQ 349
Cdd:cd07147 236 -----VIVDSDADLDFAAQRIIFGAFYQaGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 350 LEKILSYIDIGKQEGAKLLCGGERAdlggdlsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTL 428
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGKRD--------GALLEPTILEDvPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSK 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 429 YGLGAGVWSRSGDTAYRAGRAIQAGRVWTNtyhQYPA----HAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07147 383 FGLQAGVFTRDLEKALRAWDELEVGGVVIN---DVPTfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
42-479 |
2.85e-84 |
|
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: 268.01 E-value: 2.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 42 PVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAADIPL 121
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 122 AIDHFRYFAG----AIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPAS 197
Cdd:cd07098 83 TCEKIRWTLKhgekALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 198 IHVLLELIEDLL-----PAGVLNIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIF 272
Cdd:cd07098 163 SGFFLSIIRECLaacghDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 273 FEDvaSSKDAYYEKAQEG-FtmfaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLE 351
Cdd:cd07098 242 LDD--ADLDQIASIIMRGtF----QSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 352 KILSYIDIGKQEGAKLLCGGERADLGGDLSGGYYvQPTVF-EGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYG 430
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKRYPHPEYPQGHYF-PPTLLvDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2498343516 431 LGAGVWSRSGDTAYRAGRAIQAGRV----WTNTYH--QYPahaaFGGYKQSGIGR 479
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVaindFGVNYYvqQLP----FGGVKGSGFGR 445
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
45-478 |
1.15e-83 |
|
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: 265.70 E-value: 1.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 45 GQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEAN---LELLAVAETwdngKAVRETMAADIPL 121
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHadeIADWIVRES----GSIRPKAGFEVGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 122 AIDHFRYFAGAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVL 201
Cdd:cd07152 77 AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 202 L-ELIEDL-LPAGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFED---- 275
Cdd:cd07152 157 IaRLFEEAgLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDadld 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 276 VASSKDAyyekaqegFTMFaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILS 355
Cdd:cd07152 236 LAASNGA--------WGAF-LHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 356 YIDIGKQEGAKLLCGGERADLggdlsggyYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAG 434
Cdd:cd07152 307 IVDDSVAAGARLEAGGTYDGL--------FYRPTVLSGvKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAG 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2498343516 435 VWSRSGDTAYRAGRAIQAGRVWTN--TYHQYPaHAAFGGYKQSGIG 478
Cdd:cd07152 379 IISRDVGRAMALADRLRTGMLHINdqTVNDEP-HNPFGGMGASGNG 423
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-493 |
9.69e-81 |
|
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: 258.52 E-value: 9.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAaDI 119
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-EV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAIDHFRYFAGAIRAQEGSIGELDDNT-----VAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQT 194
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIPLDATQgsdnrLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 195 PASIHVLLELI-EDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASenLIPVTLELGGKSPNIFF 273
Cdd:cd07094 163 PLSALELAKILvEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 274 EDVasSKDAYYEKAQEGFTMFAlnqGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKI 353
Cdd:cd07094 241 RDA--DLDAAIEALAKGGFYHA---GQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 354 LSYIDIGKQEGAKLLCGGERAdlggdlsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLG 432
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGERD--------GALFKPTVLEDvPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2498343516 433 AGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPA-HAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEK 449
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
20-478 |
6.23e-80 |
|
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: 258.26 E-value: 6.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVapSSGEYFENITPV-TGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLEL 98
Cdd:TIGR01237 33 YPLVINGERV--ETENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 99 LAVAETWDNGKAVRETmAADIPLAIDHFRYFA-GAIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLA 177
Cdd:TIGR01237 111 FSALLVKEVGKPWNEA-DAEVAEAIDFMEYYArQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 178 PALAAGNCIVLKPAEQTPASIHVLLE-LIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYAS-- 254
Cdd:TIGR01237 190 APIVTGNCVVLKPAEAAPVIAAKFVEiLEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkv 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 255 ----ENLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEGFTMFALN-QGEVCTCPSRALVAKPIYDGFMSDGIARVGKI 329
Cdd:TIGR01237 270 qpgqKHLKRVIAEMGGKDTVIVDE------DADIELAAQSAFTSAFGfAGQKCSAGSRAVVHEKVYDEVVERFVEITESL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 330 IQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGaKLLCGGEradlgGDLSGGYYVQPTVFEGKN-SMRIFQEEIFGPV 408
Cdd:TIGR01237 344 KVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGC-----GDDSKGYFIGPTIFADVDrKARLAQEEIFGPV 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2498343516 409 LSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN--------TYHqypahaAFGGYKQSGIG 478
Cdd:TIGR01237 418 VAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnitgaivGYQ------PFGGFKMSGTD 489
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-478 |
7.46e-80 |
|
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: 256.40 E-value: 7.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETmAADI 119
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAIDHFRYFAG-AIRAQEGSIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASI 198
Cdd:cd07102 80 RGMLERARYMISiAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 199 HVLLE-LIEDLLPAGVLNIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvA 277
Cdd:cd07102 160 ERFAAaFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPD-A 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 278 SSKDAYYEKAQEGFtmfaLNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYI 357
Cdd:cd07102 238 DLDAAAESLVDGAF----FNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 358 DIGKQEGAKLLCGGERADLGGDlsGGYYVQPTVFEGKN-SMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVW 436
Cdd:cd07102 314 ADAIAKGARALIDGALFPEDKA--GGAYLAPTVLTNVDhSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2498343516 437 SRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIG 478
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRG 433
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
19-498 |
4.69e-79 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 255.22 E-value: 4.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 19 RYDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLEL 98
Cdd:PRK11241 10 RQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 99 LAVAETWDNGKAVRETmAADIPLAIDHFRYFAGAIRAQEGSI--GELDDNTVAYhFHEPLGVVGQIIPWNFPILMAVWKL 176
Cdd:PRK11241 90 LARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTipGHQADKRLIV-IKQPIGVTAAITPWNFPAAMITRKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 177 APALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE 255
Cdd:PRK11241 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 256 NLIPVTLELGGKSPNIFFEdvasskDAYYEKAQEGFTMFAL-NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNP 334
Cdd:PRK11241 248 DIKKVSLELGGNAPFIVFD------DADLDKAVEGALASKFrNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 335 LDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGDlsggyYVQPTVF-EGKNSMRIFQEEIFGPVLSVTS 413
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGN-----FFQPTILvDVPANAKVAKEETFGPLAPLFR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 414 FKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 493
Cdd:PRK11241 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
....*
gi 2498343516 494 NLLVS 498
Cdd:PRK11241 477 YMCIG 481
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
42-480 |
1.10e-76 |
|
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: 248.04 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 42 PVTGQVFCEVARGNAKDVDMAVAAgwkAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAaDIPL 121
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALAL---AASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY-EVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 122 AIDHFRYFAGAIRAQEGSIGELDDNT-----VAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPA 196
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 197 SIHVLLELI-EDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMqyASENLIPVTLELGGKSPNIFFED 275
Cdd:cd07146 162 SAIYLADLLyEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIA--ATAGYKRQLLELGGNDPLIVMDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 276 vaSSKDAYYEKAQEGftMFAlNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGA---QASNDQLEK 352
Cdd:cd07146 240 --ADLERAATLAVAG--SYA-NSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTvidEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 353 -ILSYIDigkqEGAKLLCGGERAdlggdlsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYG 430
Cdd:cd07146 315 rVEEAIA----QGARVLLGNQRQ--------GALYAPTVLDHvPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2498343516 431 LGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPA-HAAFGGYKQSG-IGRE 480
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSeLSPFGGVKDSGlGGKE 434
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
23-478 |
1.94e-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: 233.24 E-value: 1.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVapSSGEYFENITPV-TGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAV 101
Cdd:cd07083 22 VIGGEWV--DTKERMVSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 102 AETWDNGKAVRETMaADIPLAIDHFRYFAGAIRAQEGSIGEL-----DDNTVayhFHEPLGVVGQIIPWNFPILMAVWKL 176
Cdd:cd07083 100 TLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYPAVEVvpypgEDNES---FYVGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 177 APALAAGNCIVLKPAEQTP-ASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASE 255
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVvVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 256 NL------IPVTLELGGKSPNIffedVASSKDayYEKAQEGFTMFALN-QGEVCTCPSRALVAKPIYDGFMSDGIARVGK 328
Cdd:cd07083 256 LApgqtwfKRLYVETGGKNAII----VDETAD--FELVVEGVVVSAFGfQGQKCSAASRLILTQGAYEPVLERLLKRAER 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 329 IIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGaKLLCGGERADlggdlSGGYYVQPTVFEGKN-SMRIFQEEIFGP 407
Cdd:cd07083 330 LSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE-----GEGYFVAPTVVEEVPpKARIAQEEIFGP 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2498343516 408 VLSVTSFK--DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN------TYHQYPahaaFGGYKQSGIG 478
Cdd:cd07083 404 VLSVIRYKddDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkitgaLVGVQP----FGGFKLSGTN 478
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-479 |
2.84e-67 |
|
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: 222.92 E-value: 2.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 58 DVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRET------MAADIPLAIDHFRYFAG 131
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAqtevaaMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 132 aIRAQEGsigeldDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL-LP 210
Cdd:cd07095 81 -ERATPM------AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 211 AGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLI-MQYASENLIPVTLELGGKSPNIFFeDVASSKDAYYEKAQE 289
Cdd:cd07095 154 PGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPGKILALEMGGNNPLVVW-DVADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 290 GFtmfaLNQGEVCTCPSRALVA-KPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLL 368
Cdd:cd07095 232 AF----LTAGQRCTCARRLIVPdGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 369 CGGERADLGGdlsggYYVQPTVFEGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGR 448
Cdd:cd07095 308 LAMERLVAGT-----AFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLA 382
|
410 420 430
....*....|....*....|....*....|..
gi 2498343516 449 AIQAGRV-WTNTYHQYPAHAAFGGYKQSGIGR 479
Cdd:cd07095 383 RIRAGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
44-478 |
2.27e-66 |
|
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: 222.84 E-value: 2.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 44 TGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANL-EL--LAVAETwdnGKAVRETMAaDIP 120
Cdd:cd07125 56 HERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRgELiaLAAAEA---GKTLADADA-EVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 121 LAIDHFRYFAGAIRAQ------EGSIGELDDntvaYHFHePLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQT 194
Cdd:cd07125 132 EAIDFCRYYAAQARELfsdpelPGPTGELNG----LELH-GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 195 PASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASEN---LIPVTLELGGKSPN 270
Cdd:cd07125 207 PLIAARAVELLHEAgVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 271 IffedVASSKDayYEKA-----QEGFTmfalNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQA 345
Cdd:cd07125 287 I----VDSTAL--PEQAvkdvvQSAFG----SAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 346 SNDQLEKILSYIDIGKQEgAKLLcggERADLggDLSGGYYVQPTVFEGKNSMRIfQEEIFGPVLSVTSFK--DYDEAISI 423
Cdd:cd07125 357 DKPAGKLLRAHTELMRGE-AWLI---APAPL--DDGNGYFVAPGIIEIVGIFDL-TTEVFGPILHVIRFKaeDLDEAIED 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2498343516 424 ANDTLYGLGAGVWSRSGDTAYRAGRAIQAGrvwtNTYHQYPAHAA------FGGYKQSGIG 478
Cdd:cd07125 430 INATGYGLTLGIHSRDEREIEYWRERVEAG----NLYINRNITGAivgrqpFGGWGLSGTG 486
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
40-480 |
3.33e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 218.07 E-value: 3.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 40 ITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAADI 119
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 120 PLAiDHFRYFAG---AIRAQE----GSIGElddnTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAE 192
Cdd:PRK09406 86 KCA-KGFRYYAEhaeALLADEpadaAAVGA----SRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 193 QTPASIHVLLELIEDL-LPAGVLN--IVNGFGIEAgapLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSP 269
Cdd:PRK09406 161 NVPQTALYLADLFRRAgFPDGCFQtlLVGSGAVEA---ILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 270 NIffedVASSKDAyyEKAQE-GFTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASND 348
Cdd:PRK09406 238 FI----VMPSADL--DRAAEtAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 349 QLEKILSYIDIGKQEGAKLLCGGERADlgGDlsgGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDT 427
Cdd:PRK09406 312 GRDEVEKQVDDAVAAGATILCGGKRPD--GP---GWFYPPTVITDiTPDMRLYTEEVFGPVASLYRVADIDEAIEIANAT 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2498343516 428 LYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN----TYHQYPahaaFGGYKQSGIGRE 480
Cdd:PRK09406 387 TFGLGSNAWTRDEAEQERFIDDLEAGQVFINgmtvSYPELP----FGGVKRSGYGRE 439
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
23-483 |
1.47e-62 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 211.74 E-value: 1.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVApSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVA 102
Cdd:PRK09457 4 WINGDWIA-GQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 103 ETWDNGKAVRET------MAADIPLAIDHFRYFAGAIRaqegsiGELDDNTVAYHfHEPLGVVGQIIPWNFPILMAVWKL 176
Cdd:PRK09457 83 IARETGKPLWEAatevtaMINKIAISIQAYHERTGEKR------SEMADGAAVLR-HRPHGVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 177 APALAAGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLI-MQYAS 254
Cdd:PRK09457 156 VPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQFAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 255 ENLIPVTLELGGKSPnIFFEDVASSKDAYYEKAQEGFtmfaLNQGEVCTCPSRALVAKPIY-DGFMSDGIARVGKIIQGN 333
Cdd:PRK09457 235 QPEKILALEMGGNNP-LVIDEVADIDAAVHLIIQSAF----ISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 334 PLDTNT-MMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGDLsggyyVQPTVFEGKNSMRIFQEEIFGPVLSVT 412
Cdd:PRK09457 310 WDAEPQpFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGL-----LTPGIIDVTGVAELPDEEYFGPLLQVV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2498343516 413 SFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRV-WTNTYHQYPAHAAFGGYKQSGigreNHK 483
Cdd:PRK09457 385 RYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG----NHR 452
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
149-479 |
8.05e-59 |
|
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: 200.44 E-value: 8.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 149 AYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPL 228
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVEGGVEVATALL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 229 A---SHnnirkIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvASSKDAyyekAQEGFTMFALNQGEVCTCP 305
Cdd:cd07087 174 AepfDH-----IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKD-ANLEVA----ARRIAWGKFLNAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 306 SRALVAKPIYDGFmsdgIARVGKIIQ---GNPLDTNTMMGAQASNDQLEKILSYIDigkqeGAKLLCGGERADlggdlsG 382
Cdd:cd07087 244 DYVLVHESIKDEL----IEELKKAIKefyGEDPKESPDYGRIINERHFDRLASLLD-----DGKVVIGGQVDK------E 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 383 GYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIAND-----TLYglgagVWSRSGDTAYRAGRAIQAGRVW 456
Cdd:cd07087 309 ERYIAPTILDDvSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSrpkplALY-----LFSEDKAVQERVLAETSSGGVC 383
|
330 340
....*....|....*....|....*
gi 2498343516 457 TN--TYHQYPAHAAFGGYKQSGIGR 479
Cdd:cd07087 384 VNdvLLHAAIPNLPFGGVGNSGMGA 408
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
32-480 |
3.45e-57 |
|
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: 197.43 E-value: 3.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 32 SSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAV 111
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 112 RETMAA-----DI-PLAIDHFRYFAGAIRAQEGSigelddNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNC 185
Cdd:cd07130 89 PEGLGEvqemiDIcDFAVGLSRQLYGLTIPSERP------GHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 186 IVLKPAEQTP----ASIHVLLELIEDL-LPAGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPV 260
Cdd:cd07130 163 VVWKPSPTTPltaiAVTKIVARVLEKNgLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 261 TLELGGKSPNIFFEDvasskdAYYEKAQEGfTMFAL--NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTN 338
Cdd:cd07130 242 LLELGGNNAIIVMED------ADLDLAVRA-VLFAAvgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 339 TMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlggdlSGGYYVQPTVFEGKNSMRIFQEEIFGPVLSVTSFKDYD 418
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVID-----GPGNYVEPTIVEGLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2498343516 419 EAISIANDTLYGLGAGVWSRSgdtAYRAGRAIQA-----GRVWTNTyhqYPAHA----AFGGYKQSGIGRE 480
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTD---LRNAFRWLGPkgsdcGIVNVNI---GTSGAeiggAFGGEKETGGGRE 454
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
68-479 |
2.08e-56 |
|
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: 194.24 E-value: 2.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 68 KAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWD-NGKAVRETMAADIPLAIDHFRY----FAGAIRAQEGSIGE 142
Cdd:cd07133 9 AAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADfGHRSRHETLLAEILPSIAGIKHarkhLKKWMKPSRRHVGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 143 LDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGfGI 222
Cdd:cd07133 89 LFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVTG-GA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 223 EAGAPLAS----HnnirkIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvASSKDAyyekAQEgfTMFA--L 296
Cdd:cd07133 168 DVAAAFSSlpfdH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPD-ADLAKA----AER--IAFGklL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 297 NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKI---IQGNPLDTntmmgAQASNDQLEKILSYIDIGKQEGAKLLcggER 373
Cdd:cd07133 236 NAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPDYT-----SIINERHYARLQGLLEDARAKGARVI---EL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 374 ADLGGDLSGGYYVQPT-VFEGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIAND-----TLYglgagVWSRSGDTAYRAG 447
Cdd:cd07133 308 NPAGEDFAATRKLPPTlVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINArprplALY-----YFGEDKAEQDRVL 382
|
410 420 430
....*....|....*....|....*....|....
gi 2498343516 448 RAIQAGRVWTN--TYHQYPAHAAFGGYKQSGIGR 479
Cdd:cd07133 383 RRTHSGGVTINdtLLHVAQDDLPFGGVGASGMGA 416
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
23-493 |
2.25e-56 |
|
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: 195.10 E-value: 2.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVA 102
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 103 ETWDNGKaVRETMAADIPLAIDHFRYFAGAIRAQEGSIGE-LDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALA 181
Cdd:TIGR01722 84 ITAEHGK-THSDALGDVARGLEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 182 AGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPV 260
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 261 TLELGGKSPNIFFEDvaSSKDAYYEKAQEGFTMFAlnqGEVCTCPSRALVAKPIyDGFMSDGIARVGKIIQGNPLDTNTM 340
Cdd:TIGR01722 242 QALGGAKNHMVVMPD--ADKDAAADALVGAAYGAA---GQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 341 MGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGdLSGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDE 419
Cdd:TIGR01722 316 MGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDG-YEEGNWVGPTLLERvPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2498343516 420 AISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYP-AHAAFGGYKQSGIGRENH--KMMLDHYQQTK 493
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPlPYFSFTGWKDSFFGDHHIygKQGTHFYTRGK 471
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
39-480 |
6.76e-55 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 190.84 E-value: 6.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 39 NITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMA-- 116
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAev 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 117 ADIPLAIDHFRYFAGAIRAQEGSIGELDDNTVAYhfhEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPA 196
Cdd:PRK13968 91 AKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 197 SIHVLLELIEDL-LPAGVLNIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFED 275
Cdd:PRK13968 168 CAQLIAQVFKDAgIPQGVYGWLNADN-DGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 276 V---ASSKDAYYEKAQegftmfalNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEK 352
Cdd:PRK13968 247 AdleLAVKAAVAGRYQ--------NTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 353 ILSYIDIGKQEGAKLLCGGERadLGGdlSGGYYVqPTVFEGKN-SMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGL 431
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEK--IAG--AGNYYA-PTVLANVTpEMTAFREELFGPVAAITVAKDAEHALELANDSEFGL 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2498343516 432 GAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYPAHAAFGGYKQSGIGRE 480
Cdd:PRK13968 394 SATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
19-503 |
1.20e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 190.73 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 19 RYDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLEL 98
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 99 LAVAETWDNGKAVRETMAaDIPLAIDHFRYFAGAIRAQEGS-IGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLA 177
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEyLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 178 PALAAGNCIVLKPAEQTPASIHVLLEL-IEDLLPAGVLNIVNGFGIEAGApLASHNNIRKIAFTGETTTGRLIMQYASEN 256
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 257 LIPVTLELGGKSPNIFFEDvaSSKDAYYEK-AQEGFTMfalnQGEVCTCPSRALV---AKPIYDGFMSDgiARVGKIIQG 332
Cdd:PLN02419 351 GKRIQSNMGAKNHGLVLPD--ANIDATLNAlLAAGFGA----AGQRCMALSTVVFvgdAKSWEDKLVER--AKALKVTCG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 333 NPLDTNtmMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGdLSGGYYVQPTVFEGKN-SMRIFQEEIFGPVLSV 411
Cdd:PLN02419 423 SEPDAD--LGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPG-YEKGNFIGPTILSGVTpDMECYKEEIFGPVLVC 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 412 TSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTYHQYP-AHAAFGGYKQSGIGRENH--KMMLDH 488
Cdd:PLN02419 500 MQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPlPFFSFTGNKASFAGDLNFygKAGVDF 579
|
490
....*....|....*
gi 2498343516 489 YQQTKNLLVSYAEGP 503
Cdd:PLN02419 580 FTQIKLVTQKQKDIH 594
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
57-479 |
4.12e-52 |
|
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: 182.80 E-value: 4.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 57 KDVDMAVAAGWKAFESwGKT-SVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAADIPLAIDHFRYFAGAIR- 134
Cdd:cd07135 5 DEIDSIHSRLRATFRS-GKTkDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 135 -AQEGSIGeldDNTVAYHFH------EPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIED 207
Cdd:cd07135 84 wAKDEKVK---DGPLAFMFGkprirkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 208 LLPAGVLNIVNGfGI-EAGAPLASHNNirKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDV---ASSKDAY 283
Cdd:cd07135 161 YLDPDAFQVVQG-GVpETTALLEQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNAdleLAAKRIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 284 YEKaqegftmfALNQGEVCTCPSRALVAKPIYDGFmsdgIARVGKIIQ---GNPLDTNTMMGAQASNDQLEKILSYIDig 360
Cdd:cd07135 238 WGK--------FGNAGQICVAPDYVLVDPSVYDEF----VEELKKVLDefyPGGANASPDYTRIVNPRHFNRLKSLLD-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 361 kQEGAKLLCGGERADlgGDLsggyYVQPTVF---EGKNSMriFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWS 437
Cdd:cd07135 304 -TTKGKVVIGGEMDE--ATR----FIPPTIVsdvSWDDSL--MSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2498343516 438 RSGD------TAYRAGraiqaGRVWTNTYHQYPAH-AAFGGYKQSGIGR 479
Cdd:cd07135 375 DDKSeidhilTRTRSG-----GVVINDTLIHVGVDnAPFGGVGDSGYGA 418
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
68-479 |
8.63e-51 |
|
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: 178.96 E-value: 8.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 68 KAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAADI-PL------AIDHFRYFAGA--IRAQEG 138
Cdd:cd07134 9 AHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEIlPVlseinhAIKHLKKWMKPkrVRTPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 139 SIGelddnTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVN 218
Cdd:cd07134 89 LFG-----TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 219 GfGIE-AGAPLA---SHnnirkIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIfFEDVASSKDAYYEKAQEGFtmf 294
Cdd:cd07134 164 G-DAEvAQALLElpfDH-----IFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTI-VDETADLKKAAKKIAWGKF--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 295 aLNQGEVCTCPSRALVAKPIYDGF---MSDGIARV---GKIIQGNPlDTNTMMGAQASNdqleKILSYIDIGKQEGAKLL 368
Cdd:cd07134 234 -LNAGQTCIAPDYVFVHESVKDAFvehLKAEIEKFygkDAARKASP-DLARIVNDRHFD----RLKGLLDDAVAKGAKVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 369 CGGERADlggdlsGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIAND-----TLYglgagVWSRSGDT 442
Cdd:cd07134 308 FGGQFDA------AQRYIAPTVLTNvTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAkpkplALY-----VFSKDKAN 376
|
410 420 430
....*....|....*....|....*....|....*....
gi 2498343516 443 AYRAGRAIQAGRVWTNTYHQYPAHA--AFGGYKQSGIGR 479
Cdd:cd07134 377 VNKVLARTSSGGVVVNDVVLHFLNPnlPFGGVNNSGIGS 415
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-460 |
2.59e-50 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 185.53 E-value: 2.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 50 EVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANL-EL--LAVAE---TWDNGKA-VREtmaadiplA 122
Cdd:COG4230 586 TVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRaELmaLLVREagkTLPDAIAeVRE--------A 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 123 IDHFRYFAGAIRAQEGsigelddntvAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTP--ASIHV 200
Cdd:COG4230 658 VDFCRYYAAQARRLFA----------APTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPliAARAV 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 201 LLeLIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLI-MQYASENLIPVTL--ELGGKSPNIffedVA 277
Cdd:COG4230 728 RL-LHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMI----VD 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 278 SSkdAYYEKA-----QEGFtmfaLNQGEVCTcpsrAL----VAKPIYDgfmsdgiaRVGKIIQ--------GNPLDTNTM 340
Cdd:COG4230 803 SS--ALPEQVvddvlASAF----DSAGQRCS----ALrvlcVQEDIAD--------RVLEMLKgamaelrvGDPADLSTD 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 341 MGAQASNDQLEKILSYIDIGKQEGAKLlcggERADLGGDLSGGYYVQPTVFEgKNSMRIFQEEIFGPVLSVTSFK--DYD 418
Cdd:COG4230 865 VGPVIDAEARANLEAHIERMRAEGRLV----HQLPLPEECANGTFVAPTLIE-IDSISDLEREVFGPVLHVVRYKadELD 939
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2498343516 419 EAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGrvwtNTY 460
Cdd:COG4230 940 KVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVY 977
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
44-458 |
2.83e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 185.02 E-value: 2.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 44 TGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANL-ELLA--VAE---TWDNGKA-VREtma 116
Cdd:PRK11904 572 RRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRaELIAlcVREagkTLQDAIAeVRE--- 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 117 adiplAIDHFRYFAGAIRAQ-------EGSIGEldDNTVAYHfhePLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLK 189
Cdd:PRK11904 649 -----AVDFCRYYAAQARRLfgapeklPGPTGE--SNELRLH---GRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAK 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 190 PAEQTPASIHVLLELI-EDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQ-YASENLIPVTL--ELG 265
Cdd:PRK11904 719 PAEQTPLIAAEAVKLLhEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRtLAARDGPIVPLiaETG 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 266 GKspNIFF-------EDVAssKDAyyekAQEGFTmfalNQGEVCtcpS--RALvakpiydgFMSDGIA-RVGKIIQ---- 331
Cdd:PRK11904 799 GQ--NAMIvdstalpEQVV--DDV----VTSAFR----SAGQRC---SalRVL--------FVQEDIAdRVIEMLKgama 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 332 ----GNPLDTNTMMG----AQAsndqLEKILSYIDIGKQEgAKLLCggeRADLGGDLSGGYYVQPTVFEgKNSMRIFQEE 403
Cdd:PRK11904 856 elkvGDPRLLSTDVGpvidAEA----KANLDAHIERMKRE-ARLLA---QLPLPAGTENGHFVAPTAFE-IDSISQLERE 926
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2498343516 404 IFGPVLSVTSFK--DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN 458
Cdd:PRK11904 927 VFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
56-458 |
5.95e-50 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 184.30 E-value: 5.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 56 AKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANL-ELLAVA-----ETWDNGKA-VREtmaadiplAIDHFRY 128
Cdd:PRK11905 589 AEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMpELFALAvreagKTLANAIAeVRE--------AVDFLRY 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 129 FAGAIRaqegsigELDDNTVayhfHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDL 208
Cdd:PRK11905 661 YAAQAR-------RLLNGPG----HKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEA 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 209 -LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENL---IPVTLELGGKSPNIffedVASSkdayy 284
Cdd:PRK11905 730 gVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSgppVPLIAETGGQNAMI----VDSS----- 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 285 ekaqegftmfALnqgevctcPSRAlVAKPIYDGFMSDG--------------IA-RVGKIIQG--------NPLDTNTMM 341
Cdd:PRK11905 801 ----------AL--------PEQV-VADVIASAFDSAGqrcsalrvlclqedVAdRVLTMLKGamdelrigDPWRLSTDV 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 342 GAQASNDQLEKILSYIDIGKQEGAKLlcggERADLGGDLSGGYYVQPTVFEGKNsMRIFQEEIFGPVLSVTSFK--DYDE 419
Cdd:PRK11905 862 GPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLPAETEKGTFVAPTLIEIDS-ISDLEREVFGPVLHVVRFKadELDR 936
|
410 420 430
....*....|....*....|....*....|....*....
gi 2498343516 420 AISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN 458
Cdd:PRK11905 937 VIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
150-479 |
1.14e-48 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 173.84 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 150 YHFH-------EPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGFGI 222
Cdd:cd07136 88 LNFPsksyiyyEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVEGGVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 223 EAGAPLASHNNirKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvASSKDAyyekAQE-GFTMFaLNQGEV 301
Cdd:cd07136 168 ENQELLDQKFD--YIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDED-ANLKLA----AKRiVWGKF-LNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 302 CTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMmgAQASNDQ-LEKILSYIDIGkqegaKLLCGGE--RADLgg 378
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDY--GRIINEKhFDRLAGLLDNG-----KIVFGGNtdRETL-- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 379 dlsggyYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIAND-----TLYglgagVWSRSGDTAYRAGRAIQA 452
Cdd:cd07136 311 ------YIEPTILDNvTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSrpkplALY-----LFSEDKKVEKKVLENLSF 379
|
330 340
....*....|....*....|....*....
gi 2498343516 453 GRVWTN--TYHQYPAHAAFGGYKQSGIGR 479
Cdd:cd07136 380 GGGCINdtIMHLANPYLPFGGVGNSGMGS 408
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
154-496 |
2.20e-47 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 171.37 E-value: 2.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 154 EPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGfgieaGAPLAshNN 233
Cdd:PTZ00381 108 EPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEG-----GVEVT--TE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 234 IRK-----IAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFFEDvASSKDAYYEKAQEGFtmfaLNQGEVCTCPSRA 308
Cdd:PTZ00381 181 LLKepfdhIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKS-CNLKVAARRIAWGKF----LNAGQTCVAPDYV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 309 LVAKPIYDGFMSDGIARVGKIIQGNPLDTNTmMGAQASNDQLEKILSYIdigKQEGAKLLCGGErADLGGDlsggyYVQP 388
Cdd:PTZ00381 256 LVHRSIKDKFIEALKEAIKEFFGEDPKKSED-YSRIVNEFHTKRLAELI---KDHGGKVVYGGE-VDIENK-----YVAP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 389 TVF-EGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIAND-----TLYglgagVWSRSGDTAYRAGRAIQAGRVWTN--TY 460
Cdd:PTZ00381 326 TIIvNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSrpkplALY-----YFGEDKRHKELVLENTSSGAVVINdcVF 400
|
330 340 350
....*....|....*....|....*....|....*.
gi 2498343516 461 HQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 496
Cdd:PTZ00381 401 HLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
23-480 |
9.59e-47 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 170.01 E-value: 9.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVApsSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVA 102
Cdd:PLN02315 24 YVGGEWRA--NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 103 ETWDNGKAVRETMAaDIPLAIDHFRYFAGAIRAQEGSIGELD-DNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALA 181
Cdd:PLN02315 102 VSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 182 AGNCIVLKPAEQTP----ASIHVLLELIE-DLLPAGVLNIVNGfGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASEN 256
Cdd:PLN02315 181 CGNCVVWKGAPTTPlitiAMTKLVAEVLEkNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 257 LIPVTLELGGKSPNIFFEDvasskdAYYEKAQEGfTMFAL--NQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNP 334
Cdd:PLN02315 260 FGKCLLELSGNNAIIVMDD------ADIQLAVRS-VLFAAvgTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 335 LDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlggdlSGGYYVQPTVFEGKNSMRIFQEEIFGPVLSVTSF 414
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE-----SEGNFVQPTIVEISPDADVVKEELFGPVLYVMKF 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2498343516 415 KDYDEAISIANDTLYGLGAGVWSRSGDTAYR--AGRAIQAGRVWTNTyhqyPAH-----AAFGGYKQSGIGRE 480
Cdd:PLN02315 408 KTLEEAIEINNSVPQGLSSSIFTRNPETIFKwiGPLGSDCGIVNVNI----PTNgaeigGAFGGEKATGGGRE 476
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-478 |
1.27e-43 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 161.23 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 24 IGGKYVAPSSGEYFENITP---VTGQVFcevaRGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLA 100
Cdd:TIGR01238 42 IGHSYKADGEAQPVTNPADrrdIVGQVF----HANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 101 VAETWDNGKAVRETMAaDIPLAIDHFRYFAGAIRaqegsiGELDDNTvayhfHEPLGVVGQIIPWNFPILMAVWKLAPAL 180
Cdd:TIGR01238 118 ALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVR------DVLGEFS-----VESRGVFVCISPWNFPLAIFTGQISAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 181 AAGNCIVLKPAEQTPASIHVLLELI-EDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENL-- 257
Cdd:TIGR01238 186 AAGNTVIAKPAEQTSLIAYRAVELMqEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREda 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 258 -IPVTLELGGKSPNIffedVASSKDAYYEKAQEGFTMFAlNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLD 336
Cdd:TIGR01238 266 pVPLIAETGGQNAMI----VDSTALPEQVVRDVLRSAFD-SAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 337 TNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLggDLSGGYYVQPTVFEgKNSMRIFQEEIFGPVLSVTSFK- 415
Cdd:TIGR01238 341 LTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSR--ACQHGTFVAPTLFE-LDDIAELSEEVFGPVLHVVRYKa 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2498343516 416 -DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTyHQYPAHAA---FGGYKQSGIG 478
Cdd:TIGR01238 418 rELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNR-NQVGAVVGvqpFGGQGLSGTG 483
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
80-478 |
7.91e-43 |
|
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: 157.97 E-value: 7.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 80 ERAIILNKIADRMEANLELLAVAETWDNGKA-----VRETMAAD-IPLAIDHFRYFAGairaQEGSIG--ELDDNTVAYH 151
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKPlvdakVEVTRAIDgVELAADELGQLGG----REIPMGltPASAGRIAFT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 152 FHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELI-EDLLPAGVLNIVNGfGIEAGAPLAS 230
Cdd:cd07148 121 TREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLhEAGLPEGWCQAVPC-ENAVAEKLVT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 231 HNNIRKIAFTGETTTGrlimQYASENLIPVT---LELGGKSPNIFFEDVasSKDAYYEK-AQEGFtmfaLNQGEVCTCPS 306
Cdd:cd07148 200 DPRVAFFSFIGSARVG----WMLRSKLAPGTrcaLEHGGAAPVIVDRSA--DLDAMIPPlVKGGF----YHAGQVCVSVQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 307 RALVAKPIYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERadlggdLSGGYYv 386
Cdd:cd07148 270 RVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKR------LSDTTY- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 387 QPTV-FEGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTyhqypa 465
Cdd:cd07148 343 APTVlLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND------ 416
|
410 420
....*....|....*....|
gi 2498343516 466 HAA-------FGGYKQSGIG 478
Cdd:cd07148 417 HTAfrvdwmpFAGRRQSGYG 436
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
20-478 |
9.37e-43 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 158.77 E-value: 9.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 20 YDNYIGGKYVAPSSGEYFENITPVTGQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELL 99
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 100 A---VAETWDNGK-AVRETM-AADIplaIDHfryfagaiRAQEG--SIGE-----------LDDNTVAYHFHEPLGVVGQ 161
Cdd:PLN00412 96 AeclVKEIAKPAKdAVTEVVrSGDL---ISY--------TAEEGvrILGEgkflvsdsfpgNERNKYCLTSKIPLGVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 162 IIPWNFPILMAVWKLAPALAAGNCIVLKPAEQ-TPASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFT 240
Cdd:PLN00412 165 IPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQgAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 241 GeTTTGRLIMQYASenLIPVTLELGGKSPNIFFEDvASSKDAYYEKAQEGFTMfalnQGEVCTCPSRALVAKPIYDGFMS 320
Cdd:PLN00412 245 G-GDTGIAISKKAG--MVPLQMELGGKDACIVLED-ADLDLAAANIIKGGFSY----SGQRCTAVKVVLVMESVADALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 321 DGIARVGKIIQGNPLD--TNTMMGAQASNDQLEkilSYIDIGKQEGAKLLCGGERAdlggdlsgGYYVQPTVFEG-KNSM 397
Cdd:PLN00412 317 KVNAKVAKLTVGPPEDdcDITPVVSESSANFIE---GLVMDAKEKGATFCQEWKRE--------GNLIWPLLLDNvRPDM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 398 RIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTNTY-HQYPAHAAFGGYKQSG 476
Cdd:PLN00412 386 RIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSG 465
|
..
gi 2498343516 477 IG 478
Cdd:PLN00412 466 IG 467
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
23-476 |
3.06e-42 |
|
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: 157.75 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 23 YIGGKYVAPSSGEYFENitPVT-GQVFCEVARGNAKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANL--ELL 99
Cdd:cd07123 36 VIGGKEVRTGNTGKQVM--PHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYryELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 100 AvAETWDNGKAVREtmaADIPLA---IDHFR---YFAGAIRAQE---GSIGELddNTVAYhfhEPL-GVVGQIIPWNFPI 169
Cdd:cd07123 114 A-ATMLGQGKNVWQ---AEIDAAcelIDFLRfnvKYAEELYAQQplsSPAGVW--NRLEY---RPLeGFVYAVSPFNFTA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 170 LMAVWKLAPALAaGNCIVLKPAEQTPASIHVLLELIEDL-LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRL 248
Cdd:cd07123 185 IGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAgLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 249 IMQYASENL-----IP-VTLELGGKSpnifFEDVASSKDAyyekaqegfTMFALN--------QGEVCTCPSRALVAKPI 314
Cdd:cd07123 264 LWKQIGENLdryrtYPrIVGETGGKN----FHLVHPSADV---------DSLVTAtvrgafeyQGQKCSAASRAYVPESL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 315 YDGFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQE-GAKLLCGGEradlgGDLSGGYYVQPTVFEG 393
Cdd:cd07123 331 WPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK-----CDDSVGYFVEPTVIET 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 394 KNSM-RIFQEEIFGPVLSVTSFKD--YDEAISIANDT-LYGLGAGVWSRSGDTAYRAGRAIQ--AGRVWTNT------YH 461
Cdd:cd07123 406 TDPKhKLMTEEIFGPVLTVYVYPDsdFEETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDkptgavVG 485
|
490
....*....|....*
gi 2498343516 462 QYPahaaFGGYKQSG 476
Cdd:cd07123 486 QQP----FGGARASG 496
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
154-497 |
1.79e-40 |
|
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: 151.02 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 154 EPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGfGIEAGAPLASHnN 233
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEG-GVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 234 IRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIFfeDVASSKDAYYEKAQEGftMFALNQGEVCTCPSRALVAKp 313
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIV--DSTVDLKVAVRRIAGG--KWGCNNGQACIAPDYVLVEE- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 314 iydGFMSDGIARVGKIIQG----NPLDTNTMmgAQASNDQLEKILSYIDIGKQEGAKLLCGGERADlggdlsGGYYVQPT 389
Cdd:cd07137 253 ---SFAPTLIDALKNTLEKffgeNPKESKDL--SRIVNSHHFQRLSRLLDDPSVADKIVHGGERDE------KNLYIEPT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 390 -VFEGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN-TYHQYPAHA 467
Cdd:cd07137 322 iLLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDT 401
|
330 340 350
....*....|....*....|....*....|.
gi 2498343516 468 -AFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07137 402 lPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
56-458 |
2.17e-39 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 153.21 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 56 AKDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELL--------------AVAEtwdngkaVREtmaadipl 121
Cdd:PRK11809 681 PAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLmgllvreagktfsnAIAE-------VRE-------- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 122 AIDHFRYFAGAIRAqegsigELDDNTvayhfHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTP--ASIH 199
Cdd:PRK11809 746 AVDFLRYYAGQVRD------DFDNDT-----HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPliAAQA 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 200 VLLeLIEDLLPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENL------IPVTLELGGKSPNI-- 271
Cdd:PRK11809 815 VRI-LLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIvd 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 272 --------FFEDVASSKDAyyekaqegftmfalnQGEVCTcpsrALVAKPIYDgfmsDGIARVGKIIQ--------GNPL 335
Cdd:PRK11809 894 ssalteqvVADVLASAFDS---------------AGQRCS----ALRVLCLQD----DVADRTLKMLRgamaecrmGNPD 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 336 DTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLcGGERADlGGDLSGGYYVQPTVFEgKNSMRIFQEEIFGPVLSVTSFK 415
Cdd:PRK11809 951 RLSTDIGPVIDAEAKANIERHIQAMRAKGRPVF-QAAREN-SEDWQSGTFVPPTLIE-LDSFDELKREVFGPVLHVVRYN 1027
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2498343516 416 --DYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN 458
Cdd:PRK11809 1028 rnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1072
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
68-497 |
6.00e-35 |
|
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: 135.81 E-value: 6.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 68 KAFESwGKT-SVTERAIILNKIADRMEANLELLAVAETWDNGKAVRET-------MAADIPLAIDHFRYFAGAIRAQEGS 139
Cdd:cd07132 9 EAFSS-GKTrPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvlseillVKNEIKYAISNLPEWMKPEPVKKNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 140 IGELDDntvAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNG 219
Cdd:cd07132 88 ATLLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 220 fGIEAGAPLAShNNIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSP-------NIffeDVASSKDAYyekaqeGFT 292
Cdd:cd07132 165 -GVEETTELLK-QRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPcyvdkscDI---DVAARRIAW------GKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 293 MfalNQGEVCTCPSRALVAKPIYDGFmsdgIARVGKIIQ---GNPldtntmmgAQASNDqLEKILSyiDIGKQEGAKLLC 369
Cdd:cd07132 234 I---NAGQTCIAPDYVLCTPEVQEKF----VEALKKTLKefyGED--------PKESPD-YGRIIN--DRHFQRLKKLLS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 370 GGERAdLGGDL-SGGYYVQPTVFEG-KNSMRIFQEEIFGPVLSVTSFKDYDEAISIAND-----TLYglgagVWSRSGDT 442
Cdd:cd07132 296 GGKVA-IGGQTdEKERYIAPTVLTDvKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSrekplALY-----VFSNNKKV 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2498343516 443 AYRAGRAIQAGRVWTN------TYHQYPahaaFGGYKQSGIGRENHKMMLDHYQQTKNLLV 497
Cdd:cd07132 370 INKILSNTSSGGVCVNdtimhyTLDSLP----FGGVGNSGMGAYHGKYSFDTFSHKRSCLV 426
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
154-496 |
1.26e-32 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 130.17 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 154 EPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGFGIEAGAPLASHNN 233
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 234 irKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIffedVASSKDAYYEKAQEGFTMFALNQGEVCTCPSRALVAKP 313
Cdd:PLN02174 191 --KIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVV----VDSDTDLKVTVRRIIAGKWGCNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 314 IYDGFMSDGIARVGKIIQGNPLDTNTMMGAQASN--DQLEKILSYidigKQEGAKLLCGGE--RADLGgdlsggyyVQPT 389
Cdd:PLN02174 265 YAPKVIDAMKKELETFYGKNPMESKDMSRIVNSThfDRLSKLLDE----KEVSDKIVYGGEkdRENLK--------IAPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 390 V-FEGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN------TYHQ 462
Cdd:PLN02174 333 IlLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiavhlALHT 412
|
330 340 350
....*....|....*....|....*....|....
gi 2498343516 463 YPahaaFGGYKQSGIGRENHKMMLDHYQQTKNLL 496
Cdd:PLN02174 413 LP----FGGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-425 |
3.66e-31 |
|
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: 126.23 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 21 DNYIGGKYVAPSsGEYFENITPVTGQVfceVARGNAKDVDMAVAAGW---KAFESWGKTSVTERAIILNKIADR-MEANL 96
Cdd:cd07128 2 QSYVAGQWHAGT-GDGRTLHDAVTGEV---VARVSSEGLDFAAAVAYareKGGPALRALTFHERAAMLKALAKYlMERKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 97 ELLAVAETwdNGkAVRETMAADIPLAIDHFRYFAGAIRAQ--------EGSIGEL--DDNTVAYHFHEPL-GVVGQIIPW 165
Cdd:cd07128 78 DLYALSAA--TG-ATRRDSWIDIDGGIGTLFAYASLGRRElpnahflvEGDVEPLskDGTFVGQHILTPRrGVAVHINAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 166 NFPilmaVW----KLAPALAAGNCIVLKPAEQTPASIHVLLELIED--LLPAGVLNIVNGfgieAGAPLASHNNIRK-IA 238
Cdd:cd07128 155 NFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICG----SVGDLLDHLGEQDvVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 239 FTGETTTGRLIMQYAS--ENLIPVTLELGGKSPNIFFEDVASSKDAYYEKAQEGFTMFALNQGEVCTCPSRALVAKPIYD 316
Cdd:cd07128 227 FTGSAATAAKLRAHPNivARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 317 GFMSDGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADL-GGDLSGGYYVQPTVFEGKN 395
Cdd:cd07128 307 AVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVvGADAEKGAFFPPTLLLCDD 386
|
410 420 430
....*....|....*....|....*....|...
gi 2498343516 396 SMR---IFQEEIFGPVLSVTSFKDYDEAISIAN 425
Cdd:cd07128 387 PDAataVHDVEAFGPVATLMPYDSLAEAIELAA 419
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
62-471 |
1.09e-30 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 123.89 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 62 AVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAvrETMAADIPLAIDHFRYFAGAI---RAQEG 138
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG--WMFAENICGDQVQLRARAFVIysyRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 139 SIGEL--DDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIED--LLPAGVL 214
Cdd:cd07084 82 PGNHLgqGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 215 NIVNGFGiEAGAPLASHNNIRKIAFTGETTTGRLIMQYASEnlIPVTLELGGKSPNIFFEDVASSKDAYYEKAQEgFTMF 294
Cdd:cd07084 162 TLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQAVDYVAWQCVQD-MTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 295 AlnqGEVCTCPSRALV-AKPIYDGFMSDGIARVGKIIqgnplDTNTMMGAQASNDQLEKILSyidIGKQEGAKLLCGG-E 372
Cdd:cd07084 238 S---GQKCTAQSMLFVpENWSKTPLVEKLKALLARRK-----LEDLLLGPVQTFTTLAMIAH---MENLLGSVLLFSGkE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 373 RADLGGDLSGGYYVQPTVF----EGKNSMRIFQEEIFGPVLSVTSFKDYDEA-ISIANDTLYG-LGAGVWS-------RS 439
Cdd:cd07084 307 LKNHSIPSIYGACVASALFvpidEILKTYELVTEEIFGPFAIVVEYKKDQLAlVLELLERMHGsLTAAIYSndpiflqEL 386
|
410 420 430
....*....|....*....|....*....|....*.
gi 2498343516 440 GDTAYRAGRAIQAGR----VWTNTYHQYPAHAAFGG 471
Cdd:cd07084 387 IGNLWVAGRTYAILRgrtgVAPNQNHGGGPAADPRG 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
154-496 |
1.96e-30 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 123.68 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 154 EPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGVLNIVNGfGIEAGAPLASHnN 233
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEG-GPAVGEQLLQH-K 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 234 IRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNIfFEDVASSKDayyekaqegfTMFALNQ---GEVCTCPSRALV 310
Cdd:PLN02203 185 WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCI-VDSLSSSRD----------TKVAVNRivgGKWGSCAGQACI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 311 AKP---IYDGFMSDGIARVGKIIQ----GNPLDTNTMmgAQASNDQLEKILSYIDIGKQEGAKLLCGGErADlggdlSGG 383
Cdd:PLN02203 254 AIDyvlVEERFAPILIELLKSTIKkffgENPRESKSM--ARILNKKHFQRLSNLLKDPRVAASIVHGGS-ID-----EKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 384 YYVQPTVF-EGKNSMRIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWSRSGDTAYRAGRAIQAGRVWTN-TYH 461
Cdd:PLN02203 326 LFIEPTILlNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdAII 405
|
330 340 350
....*....|....*....|....*....|....*.
gi 2498343516 462 QYPAHA-AFGGYKQSGIGRENHKMMLDHYQQTKNLL 496
Cdd:PLN02203 406 QYACDSlPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
22-455 |
6.11e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 119.81 E-value: 6.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 22 NYIGGKYVApSSGEYFENITPVTGQvfcEVARGNAKDVDMAVAAGWkAFESWGKT----SVTERAIILNKIADRMEANLE 97
Cdd:PRK11903 7 NYVAGRWQA-GSGAGTPLFDPVTGE---ELVRVSATGLDLAAAFAF-AREQGGAAlralTYAQRAALLAAIVKVLQANRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 98 -LLAVAETwdNGKAVRETMAADIPLAIDHFRYFA------GAIRA-QEGSIGEL--DDNTVAYHFHEPL-GVVGQIIPWN 166
Cdd:PRK11903 82 aYYDIATA--NSGTTRNDSAVDIDGGIFTLGYYAklgaalGDARLlRDGEAVQLgkDPAFQGQHVLVPTrGVALFINAFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 167 FPIlMAVW-KLAPALAAGNCIVLKPAEQTPASIHVLLELIED--LLPAGVLNIVNGfgieAGAPLASH-NNIRKIAFTGE 242
Cdd:PRK11903 160 FPA-WGLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAagILPAGALSVVCG----SSAGLLDHlQPFDVVSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 243 TTTGRLIMQYAS--ENLIPVTLELGGKSPNIFFEDVASSKDAYYEKAQEGFTMFALNQGEVCTCPSRALVAKPIYDGFMS 320
Cdd:PRK11903 235 AETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 321 DGIARVGKIIQGNPLDTNTMMGAQASNDQLEKILSYIDIGKQEGAKLLCGGERADLGGDLSGGYYVQPTVF---EGKNSM 397
Cdd:PRK11903 315 ALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVDADPAVAACVGPTLLgasDPDAAT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2498343516 398 RIFQEEIFGPVLSVTSFKDYDEAISIANDTLYGLGAGVWsrSGDTAYRAGRAIQA----GRV 455
Cdd:PRK11903 395 AVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVY--SDDAAFLAAAALELadshGRV 454
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-450 |
1.33e-28 |
|
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: 118.03 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 59 VDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANL-ELLAVAEtwdngkavRET------MAADIPLAIDHFRYFAG 131
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGdELVARAH--------AETglpearLQGELGRTTGQLRLFAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 132 AIRAQEGSIGELDDNTVAYH---------FHEPLGVVGQIIPWNFPILMAVW--KLAPALAAGNCIVLKPAEQTPASIHV 200
Cdd:cd07129 73 LVREGSWLDARIDPADPDRQplprpdlrrMLVPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAHPAHPGTSEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 201 LLELIEDL-----LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENL--IPVTLELGGKSPNIFF 273
Cdd:cd07129 153 VARAIRAAlratgLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPepIPFYAELGSVNPVFIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 274 EDVASSKDAyyEKAQEGFTMFALNQGEVCTCPSRALV-AKPIYDGFmsdgIARVGKIIQGNPldTNTMM---GAQASNDQ 349
Cdd:cd07129 233 PGALAERGE--AIAQGFVGSLTLGAGQFCTNPGLVLVpAGPAGDAF----IAALAEALAAAP--AQTMLtpgIAEAYRQG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 350 LEKILSyidigkQEGAKLLCGGERADlggdlsGGYYVQPTVFE--GKNSMR--IFQEEIFGPVLSVTSFKDYDEAISIAN 425
Cdd:cd07129 305 VEALAA------APGVRVLAGGAAAE------GGNQAAPTLFKvdAAAFLAdpALQEEVFGPASLVVRYDDAAELLAVAE 372
|
410 420 430
....*....|....*....|....*....|....*.
gi 2498343516 426 dTLYG-LGAGVWSRSGDTA----------YRAGRAI 450
Cdd:cd07129 373 -ALEGqLTATIHGEEDDLAlarellpvleRKAGRLL 407
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
58-476 |
7.07e-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: 58.26 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 58 DVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMAADIPLAIDH-FRYFAGAIRAQ 136
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQAGGPHAQDRgLEAVAYAWREM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 137 ---------EGSIGELDDNTVAYHFH-EPLGV-----VGQIIPWN-FPILMAvwklapALAAGNCIVLKPAEQT--PASI 198
Cdd:cd07127 165 sripptaewEKPQGKHDPLAMEKTFTvVPRGValvigCSTFPTWNgYPGLFA------SLATGNPVIVKPHPAAilPLAI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 199 ------HVLLELIEDllPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTGETTTGRLIMQYASENLipVTLELGGKSpnif 272
Cdd:cd07127 239 tvqvarEVLAEAGFD--PNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVN---- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 273 fEDVASSKDAYYEKAQEGFTMFALNQGEVCTCPSRALVAKpiyDGFMSD-----------GIARVGKIIQGNPLDTNTMM 341
Cdd:cd07127 311 -TVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPR---DGIQTDdgrksfdevaaDLAAAIDGLLADPARAAALL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 342 GAQASNDQLEKILSyidiGKQEGAKLLCGGERADlgGDLSGGYYVQPTVFEGKNSMR-IFQEEIFGPVLSVTSFKDYDEA 420
Cdd:cd07127 387 GAIQSPDTLARIAE----ARQLGEVLLASEAVAH--PEFPDARVRTPLLLKLDASDEaAYAEERFGPIAFVVATDSTDHS 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2498343516 421 ISIANDT----------LYGLGAGVWSRSGDTAYRAGRAIQ---AGRVWTNTyhqypaHAAFGGYKQSG 476
Cdd:cd07127 461 IELARESvrehgamtvgVYSTDPEVVERVQEAALDAGVALSinlTGGVFVNQ------SAAFSDFHGTG 523
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
77-282 |
2.01e-06 |
|
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: 49.91 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 77 SVTERAIILNKIADRMEANLELLAVAETWDNGKAVRETMA---ADIPLAIDHFRYFAGAIRAQEGSIGE-----LDDNTV 148
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIAnwiAMMGCSESKLYKNIDTERGITASVGHiqdvlLPDNGE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 149 AYHFHEPLGVVGQIIPWNFPiLMAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAG----VLNIVNGFGIEA 224
Cdd:cd07077 94 TYVRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHgpkiLVLYVPHPSDEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2498343516 225 GAPLASHNNIRKIAFTGETTTGRLImqYASENLIPVtLELGGKSPNIFFEDVASSKDA 282
Cdd:cd07077 173 AEELLSHPKIDLIVATGGRDAVDAA--VKHSPHIPV-IGFGAGNSPVVVDETADEERA 227
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
59-459 |
1.16e-05 |
|
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: 47.65 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 59 VDMAVAAGWKAFESWGKTSVTERAIILNKIADRME-ANLEL--LAVAETwdnGKAVRETMAADiplaiDHF--RYFAGAI 133
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEdARIDLakLAVSET---GMGRVEDKVIK-----NHFaaEYIYNVY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 134 RAQEG-SIGELDDNTVAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAeqtPASIHVLLELIEDLLPAG 212
Cdd:cd07081 73 KDEKTcGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPH---PRAKKVTQRAATLLLQAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 213 VlnivngfgiEAGAPlasHNNIRKIAFTGETTTGRLiMQYASENLIPVT----------------LELGGKSPNIFFEDV 276
Cdd:cd07081 150 V---------AAGAP---ENLIGWIDNPSIELAQRL-MKFPGIGLLLATggpavvkaayssgkpaIGVGAGNTPVVIDET 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 277 ASSKDAyyekAQEGFTMFALNQGEVCTCPSRALVAKPIYDGFMSDGIARVGKIIQGNPLDT-------NTMMGAQASNDQ 349
Cdd:cd07081 217 ADIKRA----VQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQvqpvilkNGDVNRDIVGQD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 350 LEKILSYIDIGKQEGAKLLCgGERADLGgdlsggyyvqptvfegknSMRIFQEEIFGPVLSVTSFKDYDEAISIAnDTLY 429
Cdd:cd07081 293 AYKIAAAAGLKVPQETRILI-GEVTSLA------------------EHEPFAHEKLSPVLAMYRAANFADADAKA-LALK 352
|
410 420 430
....*....|....*....|....*....|....*...
gi 2498343516 430 GLG-----AGVWSRSG---DTAYRAGRAIQAGRVWTNT 459
Cdd:cd07081 353 LEGgcghtSAMYSDNIkaiENMNQFANAMKTSRFVKNG 390
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
25-210 |
8.28e-05 |
|
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: 45.28 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 25 GGKYVAPSSGEYFENITPV-----TGQVFCEVARGNAKDVDMAVAAGWKAFESWGKT----SVTERAIILNKIADRMEAN 95
Cdd:TIGR01092 245 GGTPVIIASGTAPKNITKVvegkkVGTLFHEDAHLWPTVEQTGERDMAVAARESSRMlqalSSEQRKEILHDIADALEDN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 96 LELLAVAETWD----NGKAVRETMAADIPLAIDHFRYFAGAIR---AQEGSIG------ELDDNTVAYHFHEPLGVVGQI 162
Cdd:TIGR01092 325 EDEILAENKKDvaaaQGAGYAASLVARLSMSPSKISSLAISLRqlaAMEDPIGrvlkrtRIADNLILEKTSVPIGVLLIV 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2498343516 163 IPWNFPILMAVWKLapALAAGNCIVLKPAEQTPASIHVLLELIEDLLP 210
Cdd:TIGR01092 405 FESRPDALVQIASL--AIRSGNGLLLKGGKEAARSNAILHKVITEAIP 450
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
60-213 |
2.41e-04 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 43.95 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 60 DMAVAAGWKAFESWGKTSvTERAIILNKIADRMEANLELLAVAETWDNGKA----VRETMAADIPLAIDHFRYFAGAIR- 134
Cdd:PLN02418 298 EMAVAARESSRKLQALSS-EERKKILLDVADALEANEELIKAENELDVAAAqeagYEKSLVSRLTLKPGKIASLAASIRq 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 135 --AQEGSIG------ELDDNTVAYHFHEPLGVvgqiipwnfpiLMAVWKLAP---------ALAAGNCIVLKPAEQTPAS 197
Cdd:PLN02418 377 laDMEDPIGrvlkrtEVADGLVLEKTSCPLGV-----------LLIIFESRPdalvqiaslAIRSGNGLLLKGGKEAARS 445
|
170
....*....|....*.
gi 2498343516 198 IHVLLELIEDLLPAGV 213
Cdd:PLN02418 446 NAILHKVITDAIPKTV 461
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
155-419 |
2.48e-04 |
|
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: 43.64 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 155 PLGVVGQIIPWNFPILMAVWKLAPALAAGNcivlKPAEQTPASIHVLLE-----LIEDLLPAGVLNIVNGFGIEAGApLA 229
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGN----KPLLKVDSKVSVVMEqflrlLHLCGMPATDVDLIHSDGPTMNK-IL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 230 SHNNIRKIAFTGETTTGRlimQYASENLIPVTLELGGKSPNIFFEDVASSKDAYYEKAQEGFTMfalnQGEVCTCPSRAL 309
Cdd:cd07126 217 LEANPRMTLFTGSSKVAE---RLALELHGKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYAC----SGQKCSAQSILF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 310 VAKPIYDGFMSDGIAR-----------VGKIIQgnpLDTNTMMgaqasnDQLEKILSYidigkqEGAKLLCGGERADlGG 378
Cdd:cd07126 290 AHENWVQAGILDKLKAlaeqrkledltIGPVLT---WTTERIL------DHVDKLLAI------PGAKVLFGGKPLT-NH 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2498343516 379 DLSGGY-YVQPT-VF------EGKNSMRIFQEEIFGPVLSVTSFKDYDE 419
Cdd:cd07126 354 SIPSIYgAYEPTaVFvpleeiAIEENFELVTTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
57-241 |
5.05e-04 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 42.61 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 57 KDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLAVaetwdngKAVRETMAADIPLAIDHFRYfagairAQ 136
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAE-------MAVEETGMGRVEDKIAKNHL------AA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 137 EGSIGELD--------DNTVAYHFHEPLGVVGQIIPWNFP--------ILMavwklapaLAAGNCIVLKPAeqtPASIHV 200
Cdd:cd07121 71 EKTPGTEDltttawsgDNGLTLVEYAPFGVIGAITPSTNPtetiinnsISM--------LAAGNAVVFNPH---PGAKKV 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2498343516 201 LLELIEDL--------LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTG 241
Cdd:cd07121 140 SAYAVELInkaiaeagGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG 188
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
57-241 |
9.60e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 41.81 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 57 KDVDMAVAAGWKAFESWGKTSVTERAIILNKIADRMEANLELLA---VAETwdnG------KAVRETMAADIPLAIDHFR 127
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAelaVEET---GmgrvedKIAKNVAAAEKTPGVEDLT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 128 yfagaIRAQEGsigelDDNTVAYHfHEPLGVVGQIIPWNFP--------ILMavwklapaLAAGNCIVLKPAeqtPASIH 199
Cdd:PRK15398 113 -----TEALTG-----DNGLTLIE-YAPFGVIGAVTPSTNPtetiinnaISM--------LAAGNSVVFSPH---PGAKK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2498343516 200 VLLELIEDL--------LPAGVLNIVNGFGIEAGAPLASHNNIRKIAFTG 241
Cdd:PRK15398 171 VSLRAIELLneaivaagGPENLVVTVAEPTIETAQRLMKHPGIALLVVTG 220
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
138-214 |
3.83e-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: 39.57 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2498343516 138 GSIGELDD----NTVAYHFHEPLGVVGQIIPWNFPILmAVWKLAPALAAGNCIVLKPAEQTPASIHVLLELIEDLLPAGV 213
Cdd:cd07080 91 GSPGILDEwvppGRGGYIRAQPRGLVVHIIAGNVPLL-PVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVDPNHP 169
|
.
gi 2498343516 214 L 214
Cdd:cd07080 170 L 170
|
|
| |
