|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
19-495 |
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: 958.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 19 YENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELL 98
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 99 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPA 178
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 179 LAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIP 258
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 259 VTLELGGKSPNIFFEDIMAQDDDYLDKALEGFAMFALNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTET 338
Cdd:cd07116 241 VTLELGGKSPNIFFADVMDADDAFFDKALEGFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 339 MIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVG--SGFYIEPTIFKGTNDMKIFQEEIFGPVLSVTTFKDFDEA 416
Cdd:cd07116 321 MIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGllGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFKDEEEA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118422 417 IKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLVSY 495
Cdd:cd07116 401 LEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY 479
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
19-495 |
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: 949.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 19 YENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELL 98
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 99 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPA 178
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 179 LAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIP 258
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 259 VTLELGGKSPNIFFEDIMAQDDDYLDKALEGFAMFALNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTET 338
Cdd:cd07559 241 VTLELGGKSPNIFFDDAMDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 339 MIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVG--SGFYIEPT-IFKGTNDMKIFQEEIFGPVLSVTTFKDFDE 415
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGldKGYFYEPTlIKGGNNDMRIFQEEIFGPVLAVITFKDEEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 416 AIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLVSY 495
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
18-495 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 657.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 18 QYENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLEL 97
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 98 LAVAETWDNGKPVRETLaADIPLAIDHFRYFAGCIRAQEGGISEID-EDTIAYHFHEPLGVVGQIIPWNFPILMATWKLA 176
Cdd:COG1012 85 LAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 177 PALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATEN 255
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 256 IIPVTLELGGKSPNIFFEDImaqDddyLDKALEG--FAMFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHP 333
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDA---D---LDAAVEAavRGAF-GNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 334 LDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTgGGERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKD 412
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLT-GGRRPDGEGGYFVEPTVLADvTPDMRIAREEIFGPVLSVIPFDD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 413 FDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYP-AHAAFGGYKKSGIGRENHKMMLEHYQQTKNL 491
Cdd:COG1012 396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
....
gi 491118422 492 LVSY 495
Cdd:COG1012 476 TIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
27-490 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 608.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 27 WVAPvKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDN 106
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 107 GKPVRETlAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIV 186
Cdd:pfam00171 80 GKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 187 LKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGG 265
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 266 KSPNIFFEDimaqDDdyLDKALEGFAMFA-LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQA 344
Cdd:pfam00171 239 KNPLIVLED----AD--LDAAVEAAVFGAfGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 345 SQEQQNKILGCIATGRAEGAQVLTGGGErhEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDT 423
Cdd:pfam00171 313 SKAQLERVLKYVEDAKEEGAKLLTGGEA--GLDNGYFVEPTVLANvTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491118422 424 IYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIY-PAHAAFGGYKKSGIGRENHKMMLEHYQQTKN 490
Cdd:pfam00171 391 EYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGdADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
19-494 |
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: 595.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 19 YENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELL 98
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 99 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPA 178
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 179 LAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIP 258
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 259 VTLELGGKSPNIFFedimaqDDDYLDKALEGFAMFAL-NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTE 337
Cdd:cd07117 241 ATLELGGKSANIIF------DDANWDKALEGAQLGILfNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 338 TMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVG--SGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFD 414
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldKGFFIEPTLIVNvTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 415 EAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLVS 494
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYID 474
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
22-489 |
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: 558.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQD-LLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATE-NII 257
Cdd:cd07091 167 AAGNTVVLKPAEQTPLSALYLAELIKEaGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 258 PVTLELGGKSPNIFFEDImaqddDyLDKALEgFAMFAL--NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:cd07091 247 KVTLELGGKSPNIVFDDA-----D-LDKAVE-WAAFGIffNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGgERHEvGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFD 414
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGG-ERHG-SKGYFIQPTVFTDvKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491118422 415 EAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
33-489 |
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: 550.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 33 GEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPV 110
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 111 RETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPA 190
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 191 EQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATE-NIIPVTLELGGKSP 268
Cdd:cd07112 161 EQSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 269 NIFFEDimAQDddyLDKALEGFAMFAL-NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQE 347
Cdd:cd07112 241 NIVFAD--APD---LDAAAEAAAAGIFwNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 348 QQNKILGCIATGRAEGAQVLTGGGERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYG 426
Cdd:cd07112 316 HFDKVLGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGvTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 427 LGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07112 396 LAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-493 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 537.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 61 ALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGG-I 139
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEvI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 140 SEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQD-LLPAGVLNVVNG 218
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEaGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 219 YGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDimaqDDdyLDKALEG--FAMFaLN 296
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDD----AD--LDAAVKGavFGAF-GN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 297 QGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTgGGERHEV 376
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLC-GGKRLEG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 377 GSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNC 455
Cdd:cd07078 314 GKGYFVPPTVLTDvDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 491118422 456 YHIYP-AHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07078 394 YSVGAePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
22-503 |
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: 537.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIP 258
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 259 VTLELGGKSPNIFFEDimAQDDDYLDKALegFAMFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTET 338
Cdd:cd07119 240 VALELGGKNPNIVFAD--ADFETAVDQAL--NGVF-FNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 339 MIGAQASQEQQNKILGCIATGRAEGAQVLTGGG--ERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDE 415
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKrpTGDELAKGYFVEPTIFDDvDRTMRIVQEEIFGPVLTVERFDTEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 416 AIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLVSY 495
Cdd:cd07119 395 AIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
....*...
gi 491118422 496 STKPAGFF 503
Cdd:cd07119 475 SPQPIGWF 482
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-493 |
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: 533.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAa 116
Cdd:cd07114 2 INPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 117 DIPLAIDHFRYFAGCIRAQEGGISEIDE-DTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPA 195
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 196 SILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFed 274
Cdd:cd07114 161 STLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVF-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 275 imaqDDDYLDKALEG--FAMFAlNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKI 352
Cdd:cd07114 239 ----DDADLDAAVNGvvAGIFA-AAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 353 LGCIATGRAEGAQVLTGGgERHEV---GSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLG 428
Cdd:cd07114 314 ERYVARAREEGARVLTGG-ERPSGadlGAGYFFEPTILADvTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491118422 429 AGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
38-493 |
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: 533.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 38 NISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAAD 117
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 118 IPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASI 197
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 198 LVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDIm 276
Cdd:cd07093 161 WLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 277 aqdddYLDKALEG--FAMFAlNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILG 354
Cdd:cd07093 240 -----DLDRAVDAavRSSFS-NNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 355 CIATGRAEGAQVLTGGG--ERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGV 431
Cdd:cd07093 314 YVELARAEGATILTGGGrpELPDLEGGYFVEPTVITGlDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491118422 432 WSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07093 394 WTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
22-489 |
1.88e-172 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 494.32 E-value: 1.88e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATE-NII 257
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 258 PVTLELGGKSPNIFFEDIMaqdddyLDKALEgFAMFAL--NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:cd07142 247 PVTLELGGKSPFIVCEDAD------VDKAVE-LAHFALffNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGErheVGS-GFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDF 413
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDR---IGSkGYYIQPTIFSDvKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491118422 414 DEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
22-494 |
6.27e-171 |
|
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: 490.71 E-value: 6.27e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA---KAQWNSSSPTTRSNILLKIADRLEQNLELL 98
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 99 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPA 178
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 179 LAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATE-NI 256
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsNL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 257 IPVTLELGGKSPNIFFEDImaqDddyLDKALEgFAMFAL--NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPL 334
Cdd:cd07141 250 KRVTLELGGKSPNIVFADA---D---LDYAVE-QAHEALffNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 335 DTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVgsGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDF 413
Cdd:cd07141 323 DPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDK--GYFIQPTVFSDvTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 414 DEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 491118422 494 S 494
Cdd:cd07141 481 K 481
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-494 |
9.78e-171 |
|
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: 489.26 E-value: 9.78e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 38 NISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAAD 117
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 118 IPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASI 197
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 198 LVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFedim 276
Cdd:cd07115 161 LRIAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVF---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 277 aqDDDYLDKALEG--FAMFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILG 354
Cdd:cd07115 237 --ADADLDAAVRAaaTGIF-YNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 355 CIATGRAEGAQVLTGGgeRHEVGSGFYIEPTIFKGT-NDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWS 433
Cdd:cd07115 314 YVDVGREEGARLLTGG--KRPGARGFFVEPTIFAAVpPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491118422 434 RSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLVS 494
Cdd:cd07115 392 RDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
22-489 |
1.07e-169 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 487.69 E-value: 1.07e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA-KAQWNSSSPTTRSNILLKIADRLEQNLELLAV 100
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 101 AETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALA 180
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 181 AGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPV 259
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 260 TLELGGKSPNIFFEDimaQDddyLDKALEGFA---MFalNQGEICTCPSRALVQESIADRFLEKAIERVK-RIKTGHPLD 335
Cdd:cd07144 251 TLECGGKSPALVFED---AD---LDQAVKWAAagiMY--NSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGG-GERHEVGSGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDF 413
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGeKAPEGLGKGYFIPPTIFTDVPqDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491118422 414 DEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-489 |
1.28e-165 |
|
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: 477.02 E-value: 1.28e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA-KAQWNSS-SPTTRSNILLKIADRLEQNLELLA 99
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATE-NII 257
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 258 PVTLELGGKSPNIFFedimaqDDDYLDKALE--GFAMFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:cd07143 250 KVTLELGGKSPNIVF------DDADLESAVVwtAYGIF-FNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTgGGERHEvGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFD 414
Cdd:cd07143 323 EDTFQGPQVSQIQYERIMSYIESGKAEGATVET-GGKRHG-NEGYFIEPTIFTDvTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491118422 415 EAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
38-493 |
3.20e-165 |
|
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: 475.26 E-value: 3.20e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 38 NISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVrETLAAD 117
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 118 IPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASI 197
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 198 LVLVELIQDL-LPAGVLNVVNGYGvEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDim 276
Cdd:cd07090 160 LLLAEILTEAgLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 277 aQDddyLDKALEGfAMFA--LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILG 354
Cdd:cd07090 237 -AD---LENAVNG-AMMAnfLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 355 CIATGRAEGAQVLTGGGERHE---VGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAG 430
Cdd:cd07090 312 YIESAKQEGAKVLCGGERVVPedgLENGFYVSPCVLTDcTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 431 VWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07090 392 VFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
19-493 |
3.82e-165 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 476.30 E-value: 3.82e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 19 YENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRL-EQNLEL 97
Cdd:PRK13252 7 QSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILrERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 98 lAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAP 177
Cdd:PRK13252 87 -AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 178 ALAAGNCIVLKPAEQTPASILVLVE-LIQDLLPAGVLNVVNGYGvEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENI 256
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEiYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 257 IPVTLELGGKSPNIFFedimaqDDDYLDKALEGfAMFA--LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPL 334
Cdd:PRK13252 245 KEVTMELGGKSPLIVF------DDADLDRAADI-AMLAnfYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 335 DTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHE--VGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFK 411
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggFANGAFVAPTVFTDcTDDMTIVREEIFGPVMSVLTFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 412 DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNL 491
Cdd:PRK13252 398 DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
..
gi 491118422 492 LV 493
Cdd:PRK13252 478 QV 479
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-492 |
9.42e-161 |
|
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: 463.75 E-value: 9.42e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETlAADI 118
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFAGCIRA----QEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTP 194
Cdd:cd07110 81 DDVAGCFEYYADLAEQldakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 195 ASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFE 273
Cdd:cd07110 161 LTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 274 DImaqddDyLDKALEgFAMFAL--NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNK 351
Cdd:cd07110 241 DA-----D-LEKAVE-WAMFGCfwNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 352 ILGCIATGRAEGAQVLTGGGERHEVGSGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAG 430
Cdd:cd07110 314 VLSFIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPtDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491118422 431 VWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLL 492
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
39-493 |
1.57e-160 |
|
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: 462.95 E-value: 1.57e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAADI 118
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFAGCIRAQEGGIS-EIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASI 197
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAgEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 198 LVLVELIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDIma 277
Cdd:cd07092 162 LLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 278 qDddyLDKALEGFAMFAL-NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCI 356
Cdd:cd07092 240 -D---LDAAVAGIATAGYyNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 357 AtGRAEGAQVLTGGGERHevGSGFYIEPTIFKGT-NDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRS 435
Cdd:cd07092 316 E-RAPAHARVLTGGRRAE--GPGYFYEPTVVAGVaQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 491118422 436 AHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
17-493 |
6.28e-159 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 459.76 E-value: 6.28e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 17 AQYENFIGGEWVApVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLE 96
Cdd:PRK13473 1 MQTKLLINGELVA-GEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 97 LLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGIS-EIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKL 175
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAgEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 176 APALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATEN 255
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 256 IIPVTLELGGKSPNIFFedimaqDDDYLDKALEGFAMFAL-NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPL 334
Cdd:PRK13473 240 VKRTHLELGGKAPVIVF------DDADLDAVVEGIRTFGYyNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 335 DTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEvGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDF 413
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPD-GKGYYYEPTLLAGaRQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 414 DEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMV 472
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
39-489 |
1.76e-157 |
|
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: 455.35 E-value: 1.76e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAaDI 118
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG-EV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFAGCIRAQEGgiseideDTIAYHF--------HEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPA 190
Cdd:cd07103 81 DYAASFLEWFAEEARRIYG-------RTIPSPApgkrilviKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 191 EQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPN 269
Cdd:cd07103 154 EETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 270 IFFEDImaqddDyLDKALEGfAMFA--LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQE 347
Cdd:cd07103 234 IVFDDA-----D-LDKAVDG-AIASkfRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 348 QQNKILGCIATGRAEGAQVLTGGgERHEVGsGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYG 426
Cdd:cd07103 307 AVEKVEALVEDAVAKGAKVLTGG-KRLGLG-GYFYEPTVLTDvTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYG 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 427 LGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETK 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
39-493 |
2.14e-157 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 455.26 E-value: 2.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAa 116
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 117 DIPLAIDHFRYFAGCIRAQEG-GISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPA 195
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGdSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 196 SILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFED 274
Cdd:cd07118 161 TTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 275 imAQDDDYLDKALegFAMFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILG 354
Cdd:cd07118 241 --ADLDAAADAVV--FGVY-FNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 355 CIATGRAEGAQVLTGGgERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWS 433
Cdd:cd07118 316 YVDAGRAEGATLLLGG-ERLASAAGLFYQPTIFTDvTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 434 RSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07118 395 KDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
39-493 |
6.01e-156 |
|
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: 451.30 E-value: 6.01e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKA-KAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETlAAD 117
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 118 IPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASI 197
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 198 LVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDim 276
Cdd:cd07109 161 LRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 277 aQDddyLDKALEGF--AMFAlNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDtETMIGAQASQEQQNKILG 354
Cdd:cd07109 239 -AD---LEAALPVVvnAIIQ-NAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 355 CIATGRAEGAQVLTGGG-ERHEVGSGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVW 432
Cdd:cd07109 313 FVARARARGARIVAGGRiAEGAPAGGYFVAPTLLDDVPpDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVW 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491118422 433 SRSAHTSYRAGRAIQAGRVWTNCYhiYPA---HAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07109 393 TRDGDRALRVARRLRAGQVFVNNY--GAGggiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
22-503 |
1.99e-155 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 451.88 E-value: 1.99e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA-----KAQWNSSSPTTRSNILLKIADRLEQNLE 96
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 97 LLAVAETWDNGKPVRETlAADIPLAIDHFRYFAGCIRA----QEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMAT 172
Cdd:PLN02467 91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEAldakQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 173 WKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQY 251
Cdd:PLN02467 170 WKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 252 ATENIIPVTLELGGKSPNIFFEDImaqddDyLDKALEgFAMFAL--NQGEICTCPSRALVQESIADRFLEKAIERVKRIK 329
Cdd:PLN02467 250 AAQMVKPVSLELGGKSPIIVFDDV-----D-LDKAVE-WAMFGCfwTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 330 TGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVT 408
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDvTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 409 TFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQT 488
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSV 482
|
490
....*....|....*
gi 491118422 489 KNLLVSYSTKPAGFF 503
Cdd:PLN02467 483 KQVTKYISDEPWGWY 497
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
39-493 |
8.76e-155 |
|
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: 448.73 E-value: 8.76e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAADI 118
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASIL 198
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 199 VLVELIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDimAQ 278
Cdd:cd07108 162 LLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD--AD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 279 DDDYLDKALEGfaMFALNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIAT 358
Cdd:cd07108 240 LDDAVDGAIAG--MRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 359 GRAE-GAQVLTGGGERHE--VGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSR 434
Cdd:cd07108 318 GLSTsGATVLRGGPLPGEgpLADGFFVQPTIFSGvDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 435 SAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRE-NHKMMLEHYQQTKNLLV 493
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREaSLEGMLEHFTQKKTVNI 457
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
21-489 |
7.39e-152 |
|
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: 441.56 E-value: 7.39e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 21 NFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAV 100
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 101 AETWDNGKPVRETLAADIPLAIDHFRYFAGCIRA-----QEGGiseideDTIAyhfHEPLGVVGQIIPWNFPILMATWKL 175
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDfefeeRRGN------SLVV---REPIGVCGLITPWNWPLNQIVLKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 176 APALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATE 254
Cdd:cd07138 152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 255 NIIPVTLELGGKSPNIFFEDimaQDddyLDKALEGFAMFA-LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHP 333
Cdd:cd07138 232 TVKRVALELGGKSANIILDD---AD---LEKAVPRGVAACfANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 334 LDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHE-VGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFK 411
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgLERGYFVKPTVFADvTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491118422 412 DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNcYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-493 |
4.91e-150 |
|
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: 437.01 E-value: 4.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIR---------AQEGGISEIdedtiayhFHEPLGVVGQIIPWNFPILM 170
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARdfpfeerrpGSGGGHVLV--------RREPVGVVAAIVPWNAPLFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 171 ATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLIM 249
Cdd:cd07139 154 AALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 250 QYATENIIPVTLELGGKSPNIFFedimaqDDDYLDKALEGFAM-FALNQGEICTCPSRALVQESIADRFLEKAIERVKRI 328
Cdd:cd07139 233 AVCGERLARVTLELGGKSAAIVL------DDADLDAAVPGLVPaSLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 329 KTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSV 407
Cdd:cd07139 307 KVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADvDNDMRIAQEEIFGPVLSV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 408 TTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPaHAAFGGYKKSGIGRENHKMMLEHYQQ 487
Cdd:cd07139 387 IPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDF-GAPFGGFKQSGIGREGGPEGLDAYLE 465
|
....*.
gi 491118422 488 TKNLLV 493
Cdd:cd07139 466 TKSIYL 471
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
20-494 |
5.20e-150 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 437.70 E-value: 5.20e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 20 ENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:TIGR02299 2 GHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAAdIPLAIDHFRYFAG-CIRAQEGGISEIDEdTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPA 178
Cdd:TIGR02299 82 VLECLDCGQPLRQTRQQ-VIRAAENFRFFADkCEEAMDGRTYPVDT-HLNYTVRVPVGPVGLITPWNAPFMLSTWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 179 LAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENII 257
Cdd:TIGR02299 160 LAFGNTVVLKPAEWSPLTAARLAEIAKEAgLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADTLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 258 PVTLELGGKSPNIFFedimaqDDDYLDKALEG--FAMFALNqGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:TIGR02299 240 RFSMELGGKSPVIVF------DDADLERALDAvvFMIFSFN-GERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGER-----HEVGSGFYIEPTIFKGT-NDMKIFQEEIFGPVLSVTT 409
Cdd:TIGR02299 313 PETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAptfrgEDLGRGNYVLPTVFTGAdNHMRIAQEEIFGPVLTVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 410 FKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:TIGR02299 393 FKDEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETK 472
|
....*
gi 491118422 490 NLLVS 494
Cdd:TIGR02299 473 NVALA 477
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
5-489 |
7.22e-150 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 439.24 E-value: 7.22e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 5 DPNQPGSKVQFKaqyENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSN 82
Cdd:PLN02466 47 EPITPPVQVSYT---QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 83 ILLKIADRLEQNLELLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQII 162
Cdd:PLN02466 124 ILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQII 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 163 PWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGS 241
Cdd:PLN02466 204 PWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 242 TQVGQLIMQYATE-NIIPVTLELGGKSPNIFFEDImaqdddYLDKALEgFAMFAL--NQGEICTCPSRALVQESIADRFL 318
Cdd:PLN02466 284 TDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDA------DVDKAVE-LAHFALffNQGQCCCAGSRTFVHERVYDEFV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 319 EKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGErheVGS-GFYIEPTIFKGTND-MKIF 396
Cdd:PLN02466 357 EKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDR---FGSkGYYIQPTVFSNVQDdMLIA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 397 QEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRE 476
Cdd:PLN02466 434 QDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGRE 513
|
490
....*....|...
gi 491118422 477 NHKMMLEHYQQTK 489
Cdd:PLN02466 514 KGIYSLNNYLQVK 526
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
22-485 |
6.27e-149 |
|
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: 434.52 E-value: 6.27e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVA 101
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 102 ETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEggiseidedtIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAA 181
Cdd:cd07111 105 ESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD----------TELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 182 GNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGvEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVT 260
Cdd:cd07111 175 GNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 261 LELGGKSPNIFFedimaqDDDYLDKALEGF--AMFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTET 338
Cdd:cd07111 254 LELGGKSPFIVF------DDADLDSAVEGIvdAIW-FNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 339 MIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEvgSGFYIEPTIFKGTNDM-KIFQEEIFGPVLSVTTFKDFDEAI 417
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPS--KGPFYPPTLFTNVPPAsRIAQEEIFGPVLVVLTFRTAKEAV 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491118422 418 KIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHY 485
Cdd:cd07111 405 ALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
38-489 |
1.18e-148 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 433.21 E-value: 1.18e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 38 NISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWN-SSSPTTRSNILLKIADRLEQNLELLA---VAETwdnGKPVRET 113
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRallVAEV---GAPVMTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 114 LAADIPLAIDHFRYFAGCIRA---QEGGISEIDEDTIAYHF--HEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLK 188
Cdd:cd07089 78 RAMQVDGPIGHLRYFADLADSfpwEFDLPVPALRGGPGRRVvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 189 PAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKS 267
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETdLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 268 PNIFFEDImaqddDYLDKALEGFAMFALNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQE 347
Cdd:cd07089 238 ANIVLDDA-----DLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 348 QQNKILGCIATGRAEGAQVLTGGGERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYG 426
Cdd:cd07089 313 QRDRVEGYIARGRDEGARLVTGGGRPAGLDKGFYVEPTLFADvDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 427 LGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07089 393 LSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
22-499 |
1.27e-145 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 426.93 E-value: 1.27e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQY-ATENII 257
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAaATSNLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 258 PVTLELGGKSPNIFFedimaqDDDYLDKALEgFAMFAL--NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:PLN02766 264 QVSLELGGKSPLLIF------DDADVDMAVD-LALLGIfyNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGG---GERhevgsGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFK 411
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGkpcGDK-----GYYIEPTIFTDvTEDMKIAQDEIFGPVMSLMKFK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 412 DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNL 491
Cdd:PLN02766 412 TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
....*...
gi 491118422 492 LVSYSTKP 499
Cdd:PLN02766 492 VTPLYNSP 499
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
63-493 |
2.78e-144 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 418.56 E-value: 2.78e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 63 DAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPvRETLAADIPLAIDHFRYFAGCIRAQEG-GISE 141
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGpELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 142 IDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQD-LLPAGVLNVVNGYG 220
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEaGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 221 VEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDimaqDDdyLDKALEG--FAMFaLNQG 298
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDED----AD--LDAAVEGavFGAF-FNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 299 EICTCPSRALVQESIADRFlekaIERVKRIKTGhpldtetmigaqasqeqqnkilgciatgraegaqvltgggerhevgs 378
Cdd:cd06534 233 QICTAASRLLVHESIYDEF----VEKLVTVLVD----------------------------------------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 379 gfyieptifkGTNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHI 458
Cdd:cd06534 262 ----------VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSI 331
|
410 420 430
....*....|....*....|....*....|....*.
gi 491118422 459 -YPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd06534 332 gVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
22-490 |
9.41e-143 |
|
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: 418.21 E-value: 9.41e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVA 101
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 102 ETWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQEGGI--SEIDEDTIaYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:cd07088 81 IVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIipSDRPNENI-FIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIP 258
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 259 VTLELGGKSPNIFFEDimaQDddyLDKALEG-FAMFALNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTE 337
Cdd:cd07088 239 VSLELGGKAPAIVMKD---AD---LDLAVKAiVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 338 TMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGeRHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEA 416
Cdd:cd07088 313 TDMGPLVNEAALDKVEEMVERAVEAGATLLTGGK-RPEGEKGYFYEPTVLTNvRQDMEIVQEEIFGPVLPVVKFSSLDEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491118422 417 IKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKN 490
Cdd:cd07088 392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKV 465
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
19-489 |
1.07e-142 |
|
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: 418.58 E-value: 1.07e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 19 YENFIGGEWVAPvkGEYFENISPVD-GKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLEL 97
Cdd:cd07097 1 YRNYIDGEWVAG--GDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 98 LAVAETWDNGKPVRETLAaDIPLAIDHFRYFAG-CIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLA 176
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGeALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 177 PALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATEN 255
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 256 IIPVTLELGGKSPNIFFEDimAQDDDYLDKALEGfAMFalNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDD--ADLDLAVECAVQG-AFF--STGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFD 414
Cdd:cd07097 313 EGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGvTNDMRIAREEIFGPVAAVIRVRDYD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 415 EAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCyhiyPA-----HAAFGGYKKSGIG-RENHKMMLEHYQQT 488
Cdd:cd07097 393 EALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNL----PTagvdyHVPFGGRKGSSYGpREQGEAALEFYTTI 468
|
.
gi 491118422 489 K 489
Cdd:cd07097 469 K 469
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
39-489 |
4.02e-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: 413.46 E-value: 4.02e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETlAADI 118
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFAGCIRAQEGgISEIDEDTIAYHfHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASIL 198
Cdd:cd07106 81 GGAVAWLRYTASLDLPDEV-IEDDDTRRVELR-RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 199 VLVELIQDLLPAGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDImaq 278
Cdd:cd07106 159 KLGELAQEVLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 279 DddyLDKALEGFAMFA-LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIA 357
Cdd:cd07106 235 D---IDAVAPKLFWGAfINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 358 TGRAEGAQVLTgGGERHEvGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSA 436
Cdd:cd07106 312 DAKAKGAKVLA-GGEPLD-GPGYFIPPTIVDDpPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491118422 437 HTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07106 390 ERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-495 |
8.30e-141 |
|
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: 412.92 E-value: 8.30e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAaDI 118
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFAGCIRAQEGgiSEIDEDTIAYHF--HEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPAS 196
Cdd:cd07107 81 MVAAALLDYFAGLVTELKG--ETIPVGGRNLHYtlREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 197 ILVLVELIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDIm 276
Cdd:cd07107 159 ALRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 277 aqDddyLDKALEGfAMFALN---QGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKIL 353
Cdd:cd07107 238 --D---PEAAADA-AVAGMNftwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 354 GCIATGRAEGAQVLTGGG--ERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAG 430
Cdd:cd07107 312 HYIDSAKREGARLVTGGGrpEGPALEGGFYVEPTVFADvTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491118422 431 VWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLVSY 495
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
21-496 |
8.84e-137 |
|
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: 403.65 E-value: 8.84e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 21 NFIGGEWVAPVKGEYFENISPVDGK-VFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGGI--SEIdEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAP 177
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETvpSEL-PNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 178 ALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENI 256
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 257 IPVTLELGGKSPNIffedIMaqDDDYLDKALEGFAMFAL-NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:cd07131 239 KRVALEMGGKNPII----VM--DDADLDLALEGALWSAFgTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGG--ERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKD 412
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGErlTGGGYEKGYFVEPTVFTDvTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 413 FDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHI-YPAHAAFGGYKKSGIG-RENHKMMLEHYQQTKN 490
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
....*.
gi 491118422 491 LLVSYS 496
Cdd:cd07131 473 VYVDYS 478
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
19-493 |
8.05e-133 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 393.32 E-value: 8.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 19 YENFIGGEWVApvKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA-KAQWNSSSPTTRSNILLKIADRLEQNLEL 97
Cdd:TIGR03216 1 IRNFINGAFVE--SGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAAlKGPWGKMTVAERADLLYAVADEIERRFDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 98 LAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEID----EDTIAYHFHEPLGVVGQIIPWNFPILMATW 173
Cdd:TIGR03216 79 FLAAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTECFEMAtpdgKGALNYAVRKPLGVVGVISPWNLPLLLMTW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 174 KLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVE-VGRPLATNPRIAKIAFTGSTQVGQLIMQY 251
Cdd:TIGR03216 159 KVGPALACGNTVVVKPSEETPGTATLLGEVMNAVgVPKGVYNVVHGFGPDsAGEFLTRHPGVDAITFTGETRTGSAIMKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 252 ATENIIPVTLELGGKSPNIFFEDImaqDddyLDKALEGFAMFA-LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKT 330
Cdd:TIGR03216 239 AADGVKPVSFELGGKNAAIVFADC---D---FDAAVAGILRSAfLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 331 GHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERH---EVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLS 406
Cdd:TIGR03216 313 GVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVPDfgdALAGGAWVQPTIWTGlPDSARVVTEEIFGPCCH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 407 VTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQ 486
Cdd:TIGR03216 393 IAPFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYT 472
|
....*..
gi 491118422 487 QTKNLLV 493
Cdd:TIGR03216 473 ELTNVCI 479
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-494 |
4.04e-124 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 371.54 E-value: 4.04e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATE-NII 257
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 258 PVTLELGGKSPNIFFEDimAQDddyLDKALEGFA--MFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:PRK09847 263 RVWLEAGGKSANIVFAD--CPD---LQQAASATAagIF-YNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVgsgfYIEPTIFKGT-NDMKIFQEEIFGPVLSVTTFKDFD 414
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAA----AIGPTIFVDVdPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 415 EAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLVS 494
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
14-474 |
6.51e-123 |
|
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: 369.24 E-value: 6.51e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 14 QFKAQYENFIGGEWVapVKGEYFENISPVD-GKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLE 92
Cdd:cd07124 28 ELGREYPLVIGGKEV--RTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 93 QNLELLAVAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMAT 172
Cdd:cd07124 106 RRRFELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 173 WKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQY 251
Cdd:cd07124 185 GMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 252 AT------ENIIPVTLELGGKSPNIFFEDImaqddDyLDKALEGFAMFALN-QGEICTCPSRALVQESIADRFLEKAIER 324
Cdd:cd07124 265 AAkvqpgqKWLKRVIAEMGGKNAIIVDEDA-----D-LDEAAEGIVRSAFGfQGQKCSACSRVIVHESVYDEFLERLVER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 325 VKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGaQVLTGGGERHEVGSGFYIEPTIFKGTN-DMKIFQEEIFGP 403
Cdd:cd07124 339 TKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGYFVQPTIFADVPpDHRLAQEEIFGP 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 404 VLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN--CYHIYPAHAAFGGYKKSGIG 474
Cdd:cd07124 418 VLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
36-476 |
2.05e-122 |
|
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: 365.88 E-value: 2.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 36 FENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETlA 115
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 116 ADIPLAIDHFRYFAGCIRAQEGGISEID-EDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTP 194
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPSDsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 195 ASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFE 273
Cdd:cd07150 160 VIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 274 DImaqDDDYLDKAlEGFAMFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKIL 353
Cdd:cd07150 240 DA---DLDYAVRA-AAFGAF-MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 354 GCIATGRAEGAQVLTGGGErhevgSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVW 432
Cdd:cd07150 315 RQVEDAVAKGAKLLTGGKY-----DGNFYQPTVLTDvTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 491118422 433 SRSAHTSYRAGRAIQAGRVWTNCYHIY-PAHAAFGGYKKSGIGRE 476
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGRE 434
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
39-489 |
2.58e-121 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 363.20 E-value: 2.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWnSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETlAA 116
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 117 DIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPas 196
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 197 iLVLVELIQDL-----LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIF 271
Cdd:cd07120 158 -QINAAIIRILaeipsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 272 FEDimAQDDDYLDKALEGFAMFAlnqGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNK 351
Cdd:cd07120 237 FDD--ADLDAALPKLERALTIFA---GQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 352 ILGCIATGRAEGAQV-LTGGGERHEVGSGFYIEPTIFK-GTNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGA 429
Cdd:cd07120 312 VDRMVERAIAAGAEVvLRGGPVTEGLAKGAFLRPTLLEvDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 430 GVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYK 451
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
18-493 |
1.88e-120 |
|
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: 361.63 E-value: 1.88e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 18 QYENFIGGEWVAPvKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLEL 97
Cdd:TIGR03374 1 QHKLLINGELVSG-EGEKQPVYNPATGEVILEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENAQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 98 LAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEG-GISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLA 176
Cdd:TIGR03374 80 FAELESRNCGKPLHSVFNDEIPAIVDVFRFFAGAARCLSGlAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 177 PALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENI 256
Cdd:TIGR03374 160 PALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGKTVGDPLTGHEKVRMVSLTGSIATGEHILSHTAPSI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 257 IPVTLELGGKSPNIFFedimaqDDDYLDKALEGFAMFAL-NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:TIGR03374 240 KRTHMELGGKAPVIVF------DDADIDAVVEGVRTFGFyNAGQDCTAACRIYAQRGIYDTLVEKLGAAVATLKSGAPDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEvGSGFYIEPTIFKGT-NDMKIFQEEIFGPVLSVTTFKDFD 414
Cdd:TIGR03374 314 ESTELGPLSSLAHLERVMKAVEEAKALGHIKVITGGEKRK-GNGYYFAPTLLAGAkQDDAIVQKEVFGPVVSITSFDDEE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118422 415 EAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:TIGR03374 393 QVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHIMV 471
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
16-495 |
1.23e-119 |
|
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: 359.89 E-value: 1.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 16 KAQYENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA--KAQWNSSSPTTRSNILLKIADRLEQ 93
Cdd:cd07140 3 KMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 94 NLELLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDE----DTIAYHFHEPLGVVGQIIPWNFPIL 169
Cdd:cd07140 83 HQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQarpnRNLTLTKREPIGVCGIVIPWNYPLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 170 MATWKLAPALAAGNCIVLKPAEQTPASILVLVEL-IQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLI 248
Cdd:cd07140 163 MLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 249 MQY-ATENIIPVTLELGGKSPNIFFEDImaqdddYLDKALE-GFAMFALNQGEICTCPSRALVQESIADRFLEKAIERVK 326
Cdd:cd07140 243 MKScAVSNLKKVSLELGGKSPLIIFADC------DMDKAVRmGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 327 RIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGgeRHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVL 405
Cdd:cd07140 317 KMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGG--KQVDRPGFFFEPTVFTDvEDHMFIAKEESFGPIM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 406 SVTTFK--DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLE 483
Cdd:cd07140 395 IISKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALN 474
|
490
....*....|..
gi 491118422 484 HYQQTKNLLVSY 495
Cdd:cd07140 475 EYLKTKTVTIEY 486
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
57-489 |
2.23e-119 |
|
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: 357.23 E-value: 2.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 57 DIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAEtwdngkpVRET------LAADIPLAIDHFRYFAG 130
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWL-------IRESgstrpkAAFEVGAAIAILREAAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 131 CIRAQEGGISEID-EDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASI-LVLVELIQDL- 207
Cdd:cd07104 74 LPRRPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 208 LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDimaQDddyLDKAL 287
Cdd:cd07104 154 LPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDD---AD---LDLAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 288 EGFAMFA-LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQV 366
Cdd:cd07104 228 SAAAFGAfLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 367 LTGGgeRHEvgsGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRA 445
Cdd:cd07104 308 LTGG--TYE---GLFYQPTVLSDvTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAER 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 491118422 446 IQAGRVWTNCYHIY-PAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07104 383 LETGMVHINDQTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
36-483 |
8.06e-118 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 354.35 E-value: 8.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 36 FENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETlA 115
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 116 ADIPLAIDHFRYFAGCIRAQEGGISEID-----EDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPA 190
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVDayeynERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 191 EQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPN 269
Cdd:cd07145 160 SNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 270 IFFEDimaQDddyLDKALEGfAMFA--LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQE 347
Cdd:cd07145 240 IVLKD---AD---LERAVSI-AVRGrfENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 348 QQNKILGCIATGRAEGAQVLTGGgerhEVGSGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYG 426
Cdd:cd07145 313 AVERMENLVNDAVEKGGKILYGG----KRDEGSFFPPTVLENDTpDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 491118422 427 LGAGVWSRSAHTSYRAGRAIQAGRVWTN-CYHIYPAHAAFGGYKKSGIGRENHK-MMLE 483
Cdd:cd07145 389 LQASVFTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRyTMLE 447
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-495 |
8.30e-117 |
|
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: 352.51 E-value: 8.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPvKGEYFENI-SPVDGKVFTKVPRSSAEDIELALDAAHKA-KAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:cd07113 3 FIDGRPVAG-QSEKRLDItNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGGI------SEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATW 173
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsipSMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 174 KLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGvEVGRPLATNPRIAKIAFTGSTQVGQLIMQYA 252
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 253 TENIIPVTLELGGKSPNIFFEDimAQDDDYLDKALE-GFamfaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTG 331
Cdd:cd07113 241 ASDLTRVTLELGGKNAAAFLKD--ADIDWVVEGLLTaGF----LHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 332 HPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHevGSGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTF 410
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA--GEGYFVQPTLVLARSaDSRLMREETFGPVVSFVPY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 411 KDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKN 490
Cdd:cd07113 393 EDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKS 472
|
....*
gi 491118422 491 LLVSY 495
Cdd:cd07113 473 VMIRY 477
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
20-489 |
1.42e-116 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 352.46 E-value: 1.42e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 20 ENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLA 99
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 VAETWDNGKPVRETLAaDIPLAIDHFRYFAG-CIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPA 178
Cdd:PLN02278 106 QLMTLEQGKPLKEAIG-EVAYGASFLEYFAEeAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 179 LAAGNCIVLKPAEQTPASILVLVEL-IQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENII 257
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELaLQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 258 PVTLELGGKSPNIFFedimaqDDDYLDKALEGfAMFA--LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLD 335
Cdd:PLN02278 265 RVSLELGGNAPFIVF------DDADLDVAVKG-ALASkfRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 336 TETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGgERHEVGSGFYiEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFD 414
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGG-KRHSLGGTFY-EPTVLGDvTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491118422 415 EAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
21-496 |
1.68e-114 |
|
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: 346.47 E-value: 1.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 21 NFIGGEWVAPvKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAV 100
Cdd:cd07086 1 GVIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 101 AETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGGI--SEIdEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPA 178
Cdd:cd07086 80 LVSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTipSER-PGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 179 LAAGNCIVLKPAEQTPASILVLVELIQDLL-----PAGVLNVVNGYGvEVGRPLATNPRIAKIAFTGSTQVGQLIMQYAT 253
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVLeknglPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 254 ENIIPVTLELGGKSPNIFFEDimAQdddyLDKALEG--FAMFAlNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTG 331
Cdd:cd07086 237 RRFGRVLLELGGNNAIIVMDD--AD----LDLAVRAvlFAAVG-TAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 332 HPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTF 410
Cdd:cd07086 310 DPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGvTDDARIVQEETFAPILYVIKF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 411 KDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRA--IQAGRVWTNcyhIYP----AHAAFGGYKKSGIGRENHKMMLEH 484
Cdd:cd07086 390 DSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVN---IPTsgaeIGGAFGGEKETGGGRESGSDAWKQ 466
|
490
....*....|..
gi 491118422 485 YQQTKNLLVSYS 496
Cdd:cd07086 467 YMRRSTCTINYS 478
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
36-489 |
2.13e-113 |
|
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: 342.65 E-value: 2.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 36 FENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLA 115
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 116 aDIPLAIDHFRYFAGCIR----------AQEGGiseidEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCI 185
Cdd:cd07149 81 -EVDRAIETLRLSAEEAKrlagetipfdASPGG-----EGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 186 VLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYAteNIIPVTLELG 264
Cdd:cd07149 155 VLKPASQTPLSALKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKA--GLKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 265 GKSPNIffedIMAQDDdyLDKALEGFAMFAL-NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQ 343
Cdd:cd07149 233 SNAAVI----VDADAD--LEKAVERCVSGAFaNAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 344 ASQEQQNKILGCIATGRAEGAQVLTgGGERHevgsGFYIEPTIFKGT-NDMKIFQEEIFGPVLSVTTFKDFDEAIKIAND 422
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEGGARLLT-GGKRD----GAILEPTVLTDVpPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAND 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491118422 423 TIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPA-HAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGREGPRYAIEEMTEIK 449
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-489 |
2.80e-112 |
|
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: 340.44 E-value: 2.80e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 25 GEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLK----IADRLEQNLELLaV 100
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKaaqiLEERRDEIVEWL-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 101 AETwdngKPVRETLAADIPLAIDHFRYFAGCIRAQEGGISEID-EDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:cd07151 80 RES----GSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDvPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASI-LVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENII 257
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAgLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 258 PVTLELGGKSPNIFFEDimAQDDDYLDKALegFAMFaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTE 337
Cdd:cd07151 236 KVALELGGNNPFVVLED--ADIDAAVNAAV--FGKF-LHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 338 TMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGErhevgSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEA 416
Cdd:cd07151 311 TVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEA-----EGNVLEPTVLSDvTNDMEIAREEIFGPVAPIIKADDEEEA 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491118422 417 IKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIY-PAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07151 386 LELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDK 459
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
39-475 |
2.29e-105 |
|
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: 322.25 E-value: 2.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPvRETLAADI 118
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFAG----CIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTP 194
Cdd:cd07099 80 LLALEAIDWAARnaprVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 195 ASILVLVELIQDL-LPAGVLNVVNGYGvEVGRPLATNpRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFE 273
Cdd:cd07099 160 LVGELLAEAWAAAgPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 274 DimAQDDDYLDKALEGfAMFalNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKIL 353
Cdd:cd07099 238 D--ADLERAAAAAVWG-AMV--NAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 354 GCIATGRAEGAQVLTGGgeRHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVW 432
Cdd:cd07099 313 RHVDDAVAKGAKALTGG--ARSNGGGPFYEPTVLTDvPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 491118422 433 SRSAHTSYRAGRAIQAGRVWTNCyHIYPA---HAAFGGYKKSGIGR 475
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSIND-VLLTAgipALPFGGVKDSGGGR 435
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
39-491 |
1.09e-101 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 312.71 E-value: 1.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVR----ETL 114
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRhafeEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 115 aaDIPLAIDHFRYFAGCI---RAQEGGISEIDEDTIAYHfhePLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAE 191
Cdd:cd07101 81 --DVAIVARYYARRAERLlkpRRRRGAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 192 QTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIakIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNI 270
Cdd:cd07101 156 QTALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 271 FFEDImaqddDyLDKALEG--FAMFAlNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQ 348
Cdd:cd07101 234 VLEDA-----D-LDKAAAGavRACFS-NAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 349 QNKILGCIATGRAEGAQVLTGGGERHEVGSGFYiEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGL 427
Cdd:cd07101 307 LDRVTAHVDDAVAKGATVLAGGRARPDLGPYFY-EPTVLTGvTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118422 428 GAGVWSRSAHTSYRAGRAIQAGRVwtNCYHIYPA-----HAAFGGYKKSGIGRENHKMMLEHYQQTKNL 491
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTV--NVNEGYAAawasiDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
18-476 |
8.19e-100 |
|
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: 308.35 E-value: 8.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 18 QYENFIGGEWVAPvKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKA-KAQWNSSSPTTRSNILLKIADRLEQNLE 96
Cdd:cd07082 1 QFKYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 97 LLAVAETWDNGKPVRETL-----AAD-IPLAIDHFRYFAGciRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILM 170
Cdd:cd07082 80 EVANLLMWEIGKTLKDALkevdrTIDyIRDTIEELKRLDG--DSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 171 ATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIM 249
Cdd:cd07082 158 TVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 250 QYATenIIPVTLELGGKSPNIFFEDimAQDDDYLDKALEGfaMFALNqGEICTCPSRALVQESIADRFLEKAIERVKRIK 329
Cdd:cd07082 238 KQHP--MKRLVLELGGKDPAIVLPD--ADLELAAKEIVKG--ALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 330 TGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVgsgfYIEPT-IFKGTNDMKIFQEEIFGPVLSVT 408
Cdd:cd07082 311 VGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGN----LIYPTlLDPVTPDMRLAWEEPFGPVLPII 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 409 TFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCY-----HIYPahaaFGGYKKSGIGRE 476
Cdd:cd07082 387 RVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqrgpDHFP----FLGRKDSGIGTQ 455
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
23-472 |
1.79e-99 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 308.79 E-value: 1.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 23 IGGEWVApvKGEYFENISPVD-GKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRL-EQNLELLAV 100
Cdd:PRK03137 41 IGGERIT--TEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIrRRKHEFSAW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 101 aETWDNGKPVRETlAADIPLAIDHFRYFA-GCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:PRK03137 119 -LVKEAGKPWAEA-DADTAEAIDFLEYYArQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATEnIIP 258
Cdd:PRK03137 197 VAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK-VQP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 259 -------VTLELGGKSPNIFFEDImaqddDyLDKALEGFAMFALN-QGEICTCPSRALVQESIADRFLEKAIERVKRIKT 330
Cdd:PRK03137 276 gqiwlkrVIAEMGGKDAIVVDEDA-----D-LDLAAESIVASAFGfSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 331 GHPLDTETMiGAQASQEQQNKILGCIATGRAEGaQVLTGGGerHEVGSGFYIEPTIFKGTNDM-KIFQEEIFGPVLSVTT 409
Cdd:PRK03137 350 GNPEDNAYM-GPVINQASFDKIMSYIEIGKEEG-RLVLGGE--GDDSKGYFIQPTIFADVDPKaRIMQEEIFGPVVAFIK 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491118422 410 FKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN--C------YHiypahaAFGGYKKSG 472
Cdd:PRK03137 426 AKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCtgaivgYH------PFGGFNMSG 490
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
28-491 |
7.45e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 307.58 E-value: 7.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 28 VAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNG 107
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 108 KPVR----ETLaaDIPLAIDHFRYFAGCIRAQE---GGISEIdedTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALA 180
Cdd:PRK09407 106 KARRhafeEVL--DVALTARYYARRAPKLLAPRrraGALPVL---TKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 181 AGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNprIAKIAFTGSTQVGQLIMQYATENIIPV 259
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 260 TLELGGKSPNIFFEDimaQDddyLDKALEG--FAMFAlNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTE 337
Cdd:PRK09407 259 SLELGGKNPMIVLDD---AD---LDKAAAGavRACFS-NAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 338 TMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVGSGFYiEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEA 416
Cdd:PRK09407 332 ADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPLFY-EPTVLTGvTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 417 IKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVwtNCYHIY-PAHAAF----GGYKKSGIGRENHKMMLEHYQQTKNL 491
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARGRAIAARIRAGTV--NVNEGYaAAWGSVdapmGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
39-489 |
2.81e-98 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 303.97 E-value: 2.81e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAaDI 118
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-EV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFAGCIRAQEG-----GISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQT 193
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGeeiplDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 194 PASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYAteNIIPVTLELGGKSPNIFF 272
Cdd:cd07094 163 PLSALELAKILVEAgVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA--GGKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 273 EDImaqDddyLDKALEGFAMFALNQ-GEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNK 351
Cdd:cd07094 241 RDA---D---LDAAIEALAKGGFYHaGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 352 ILGCIATGRAEGAQVLTgGGERhevgSGFYIEPTIFKGT-NDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAG 430
Cdd:cd07094 315 VERWVEEAVEAGARLLC-GGER----DGALFKPTVLEDVpRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 431 VWSRSAHTSYRAGRAIQAGRVWTNCYHIYPA-HAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEK 449
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
22-494 |
1.16e-97 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 303.37 E-value: 1.16e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVA 101
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 102 ETWDNGKPVRETlAADIPLAIDHFRYFAgciraQEGgiSEIDEDTIAYH--------FHEPLGVVGQIIPWNFPILMATW 173
Cdd:PRK11241 94 MTLEQGKPLAEA-KGEISYAASFIEWFA-----EEG--KRIYGDTIPGHqadkrlivIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 174 KLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYA 252
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 253 TENIIPVTLELGGKSPNIFFedimaqDDDYLDKALEG-FAMFALNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTG 331
Cdd:PRK11241 246 AKDIKKVSLELGGNAPFIVF------DDADLDKAVEGaLASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 332 HPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGgERHEVGSGFYiEPTIFKGT-NDMKIFQEEIFGPVLSVTTF 410
Cdd:PRK11241 320 DGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGG-KAHELGGNFF-QPTILVDVpANAKVAKEETFGPLAPLFRF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 411 KDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKN 490
Cdd:PRK11241 398 KDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKY 477
|
....
gi 491118422 491 LLVS 494
Cdd:PRK11241 478 MCIG 481
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
58-476 |
1.48e-97 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 301.30 E-value: 1.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 58 IELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAaDIPLAIDHFRYFAgciraqEG 137
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYA------EN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 138 GIS-----EIDEDTI-AYHFHEPLGVVGQIIPWNFPIlmatWK----LAPALAAGNCIVLKPAEQTPASILVLVELIQDL 207
Cdd:cd07100 74 AEAfladePIETDAGkAYVRYEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 208 -LPAGVLNVVNGYGVEVGRPLAtNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDimaqdDDyLDKA 286
Cdd:cd07100 150 gFPEGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDD-----AD-LDKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 287 LEGfAMFA--LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGA 364
Cdd:cd07100 223 VKT-AVKGrlQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 365 QVLTGGgERHEvGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAG 443
Cdd:cd07100 302 TLLLGG-KRPD-GPGAFYPPTVLTDvTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVA 379
|
410 420 430
....*....|....*....|....*....|...
gi 491118422 444 RAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGRE 476
Cdd:cd07100 380 RRLEAGMVFINGMVKSDPRLPFGGVKRSGYGRE 412
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-489 |
1.61e-96 |
|
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: 298.72 E-value: 1.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 57 DIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGkPVRETLAADIPLAIDHFRYFAG-CIRAQ 135
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-ATAAWAGFNVDLAAGMLREAASlITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 136 EGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLN 214
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 215 VVNGY---GVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDimAQdddyLDKALEGFA 291
Cdd:cd07105 160 VVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLED--AD----LDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 292 MFA-LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHpldteTMIGAQASQEQQNKILGCIATGRAEGAQVLTGG 370
Cdd:cd07105 234 FGAfLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 371 GERHEvGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAG 449
Cdd:cd07105 309 LADES-PSGTSMPPTILDNvTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 491118422 450 RVWTNCYHIY-PAHAAFGGYKKSGIGRENHKMMLEHYQQTK 489
Cdd:cd07105 388 AVHINGMTVHdEPTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-474 |
5.71e-96 |
|
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: 298.66 E-value: 5.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 21 NFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAV 100
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 101 AETWDNGKpvreTLA---ADIPLAIDHFRYFAGCIRAQEGGISE-IDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLA 176
Cdd:cd07085 83 LITLEHGK----TLAdarGDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 177 PALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATEN 255
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 256 IIPVTLELGGKSPNIffedIMAQDDdyLDKALEGFAMFAL-NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPL 334
Cdd:cd07085 238 GKRVQALGGAKNHAV----VMPDAD--LEQTANALVGAAFgAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 335 DTETMIGAQASQEQQNKILGCIATGRAEGAQ-VLTGGGERHEVGS-GFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFK 411
Cdd:cd07085 312 DPGADMGPVISPAAKERIEGLIESGVEEGAKlVLDGRGVKVPGYEnGNFVGPTILDNvTPDMKIYKEEIFGPVLSIVRVD 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491118422 412 DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCyhiyP-----AHAAFGGYKKSGIG 474
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV----PipvplAFFSFGGWKGSFFG 455
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
84-489 |
4.76e-94 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 291.64 E-value: 4.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 84 LLKIADRLEQNLELLAVAETWDNGKpVRETLAADIPLAIDHFRYFAGCIRAQEGGISEIDE--DTIaYHFHEPLGVVGQI 161
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK-IQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRpgENI-LLFKRALGVTTGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 162 IPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTG 240
Cdd:PRK10090 79 LPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 241 STQVGQLIMQYATENIIPVTLELGGKSPNIffedIMaqDDDYLDKALEGF-AMFALNQGEICTCPSRALVQESIADRFLE 319
Cdd:PRK10090 159 SVSAGEKIMAAAAKNITKVCLELGGKAPAI----VM--DDADLDLAVKAIvDSRVINSGQVCNCAERVYVQKGIYDQFVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 320 KAIERVKRIKTGHPLDTETM-IGAQASQEQQNKILGCIATGRAEGAQVLTGGgeRHEVGSGFYIEPTIFKGT-NDMKIFQ 397
Cdd:PRK10090 233 RLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGG--KAVEGKGYYYPPTLLLDVrQEMSIMH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 398 EEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGREN 477
Cdd:PRK10090 311 EETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGAD 390
|
410
....*....|..
gi 491118422 478 HKMMLEHYQQTK 489
Cdd:PRK10090 391 GKHGLHEYLQTQ 402
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
36-493 |
9.27e-94 |
|
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: 292.23 E-value: 9.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 36 FENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETlA 115
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 116 ADIPLAIDHFRYFAGCIRAQEG-----GISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPA 190
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGevlplDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 191 EQTPASILVLVE-LIQDLLPAGVLNVV---NgygvEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENiiPVTLELGGK 266
Cdd:cd07147 160 SRTPLSALILGEvLAETGLPKGAFSVLpcsR----DDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 267 SPNIFFEDimaQDddyLDKALEGFAMFALNQ-GEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQAS 345
Cdd:cd07147 234 AAVIVDSD---AD---LDFAAQRIIFGAFYQaGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 346 QEQQNKILGCIATGRAEGAQVLTGGgERHevgsGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTI 424
Cdd:cd07147 308 ESEAERVEGWVNEAVDAGAKLLTGG-KRD----GALLEPTILEDVPpDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSK 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 425 YGLGAGVWSRSAHTSYRAGRAIQAGRVWTNcyHIyPA----HAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07147 383 FGLQAGVFTRDLEKALRAWDELEVGGVVIN--DV-PTfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
44-474 |
8.84e-91 |
|
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: 284.19 E-value: 8.84e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 44 GKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAvaeTWDngkpVRETLAA------D 117
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIA---DWI----VRESGSIrpkagfE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 118 IPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASI 197
Cdd:cd07152 74 VGAAIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 198 LVLVELIQDL--LPAGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFedi 275
Cdd:cd07152 154 GVVIARLFEEagLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVL--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 276 maqDDDYLDKALEGFAMFA-LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILG 354
Cdd:cd07152 230 ---DDADLDLAASNGAWGAfLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 355 CIATGRAEGAQVLTGGgeRHEvgsGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWS 433
Cdd:cd07152 307 IVDDSVAAGARLEAGG--TYD---GLFYRPTVLSGvKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIIS 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 491118422 434 RSahtsyrAGRAIQAG-RVWTNCYHI------YPAHAAFGGYKKSGIG 474
Cdd:cd07152 382 RD------VGRAMALAdRLRTGMLHIndqtvnDEPHNPFGGMGASGNG 423
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
39-474 |
6.25e-89 |
|
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: 279.52 E-value: 6.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETlAADI 118
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRYFagcIRAQEGGISEIDEDTIA----YHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTP 194
Cdd:cd07102 80 RGMLERARYM---ISIAEEALADIRVPEKDgferYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 195 ASILVLVELIQD-LLPAGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFE 273
Cdd:cd07102 157 LCGERFAAAFAEaGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 274 DimAQDDDYLDKALEGfAMFalNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKIL 353
Cdd:cd07102 236 D--ADLDAAAESLVDG-AFF--NSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 354 GCIATGRAEGAQVLTGGGE-RHEVGSGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGV 431
Cdd:cd07102 311 AQIADAIAKGARALIDGALfPEDKAGGAYLAPTVLTNVDhSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 491118422 432 WSRSAHTSYRAGRAIQAGRVWTN-CYHIYPAhAAFGGYKKSGIG 474
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNrCDYLDPA-LAWTGVKDSGRG 433
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
41-475 |
2.58e-86 |
|
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: 273.41 E-value: 2.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 41 PVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAADIPL 120
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 121 AIDHFRYFagcIRAQEGGISEIDEDTIAYHFH-------EPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQT 193
Cdd:cd07098 83 TCEKIRWT---LKHGEKALRPESRPGGLLMFYkrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 194 PASILVLVELIQDLL-----PAGVLNVVNGYGvEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSP 268
Cdd:cd07098 160 AWSSGFFLSIIRECLaacghDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 269 NIFFEDimaqdddyldKALEGFAMFAL-----NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQ 343
Cdd:cd07098 239 AIVLDD----------ADLDQIASIIMrgtfqSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 344 ASQEQQNKILGCIATGRAEGAQVLTGG--GERHEVGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIA 420
Cdd:cd07098 309 ISPARFDRLEELVADAVEKGARLLAGGkrYPHPEYPQGHYFPPTLLVDvTPDMKIAQEEVFGPVMVVMKASDDEEAVEIA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 491118422 421 NDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHI--YPAHAAFGGYKKSGIGR 475
Cdd:cd07098 389 NSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVnyYVQQLPFGGVKGSGFGR 445
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
41-491 |
6.39e-85 |
|
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: 269.23 E-value: 6.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 41 PVDGKVFTKVPRSSAEDIELALDAAHkakaqwNSSSPTT---RSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAaD 117
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAA------SYRSTLTryqRSAILNKAAALLEARREEFARLITLESGLCLKDTRY-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 118 IPLAIDHFRYFAGCIRAQEGGISEIDEDT-----IAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQ 192
Cdd:cd07146 79 VGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 193 TPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMqyATENIIPVTLELGGKSPNIf 271
Cdd:cd07146 159 TPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIA--ATAGYKRQLLELGGNDPLI- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 272 fedIMaqDDDYLDKA--LEGFAMFAlNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQ 349
Cdd:cd07146 236 ---VM--DDADLERAatLAVAGSYA-NSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 350 NKILGCIATGRAEGAQVLTGGGERhevgsGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLG 428
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQRQ-----GALYAPTVLDHVPpDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491118422 429 AGVWSRSAHTSYRAGRAIQAGRVWTN-CYHIYPAHAAFGGYKKSGIG-RENHKMMLEHYQQTKNL 491
Cdd:cd07146 385 SGVCTNDLDTIKRLVERLDVGTVNVNeVPGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
12-474 |
1.33e-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: 259.80 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 12 KVQFKAQYENFIGGEWVApvKGEYFENISPVD-GKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADR 90
Cdd:TIGR01237 26 KEQLGKTYPLVINGERVE--TENKIVSINPCDkSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 91 LEQNLELLAVAETWDNGKPVRETlAADIPLAIDHFRYFA-GCIRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPIL 169
Cdd:TIGR01237 104 VRRRRHEFSALLVKEVGKPWNEA-DAEVAEAIDFMEYYArQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 170 MATWKLAPALAAGNCIVLKPAEQTPASILVLVE-LIQDLLPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLI 248
Cdd:TIGR01237 183 IMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEiLEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 249 ------MQYATENIIPVTLELGGKspniffEDIMAQDDDYLDKALEG--FAMFALNqGEICTCPSRALVQESIADRFLEK 320
Cdd:TIGR01237 263 feraakVQPGQKHLKRVIAEMGGK------DTVIVDEDADIELAAQSafTSAFGFA-GQKCSAGSRAVVHEKVYDEVVER 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 321 AIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEvgsGFYIEPTIFKGTN-DMKIFQEE 399
Cdd:TIGR01237 336 FVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSK---GYFIGPTIFADVDrKARLAQEE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491118422 400 IFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN--CYHIYPAHAAFGGYKKSGIG 474
Cdd:TIGR01237 413 IFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTD 489
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
24-476 |
3.99e-72 |
|
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: 236.72 E-value: 3.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 24 GGEWVAPvkGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAET 103
Cdd:cd07130 4 DGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 104 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGGI--SEIdedtiAYHF----HEPLGVVGQIIPWNFPILMATWKLAP 177
Cdd:cd07130 82 LEMGKILPEGLG-EVQEMIDICDFAVGLSRQLYGLTipSER-----PGHRmmeqWNPLGVVGVITAFNFPVAVWGWNAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 178 ALAAGNCIVLKPAEQTPASILVLVELIQDLL-----PAGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYA 252
Cdd:cd07130 156 ALVCGNVVVWKPSPTTPLTAIAVTKIVARVLeknglPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 253 TENIIPVTLELGGKSPNIFFEDimaQDddyLDKALEGfAMFAL--NQGEICTCPSRALVQESIADRFLEKAIERVKRIKT 330
Cdd:cd07130 235 AARFGRSLLELGGNNAIIVMED---AD---LDLAVRA-VLFAAvgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 331 GHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGgeRHEVGSGFYIEPTIFKGTNDMKIFQEEIFGPVLSVTTF 410
Cdd:cd07130 308 GDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGG--KVIDGPGNYVEPTIVEGLSDAPIVKEETFAPILYVLKF 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491118422 411 KDFDEAIKIANDTIYGLGAGVWSRSAHtsyRAGRAIQA-----GRVWTNcyhIYPAHA----AFGGYKKSGIGRE 476
Cdd:cd07130 386 DTLEEAIAWNNEVPQGLSSSIFTTDLR---NAFRWLGPkgsdcGIVNVN---IGTSGAeiggAFGGEKETGGGRE 454
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
39-476 |
3.59e-70 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 231.17 E-value: 3.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAADI 118
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAiDHFRYFAgciRAQEGGISEIDED------TIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQ 192
Cdd:PRK09406 86 KCA-KGFRYYA---EHAEALLADEPADaaavgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 193 TPASILVLVELIQDL-LPAGVLN--VVNGYGVEVgrpLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPN 269
Cdd:PRK09406 162 VPQTALYLADLFRRAgFPDGCFQtlLVGSGAVEA---ILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 270 IffedIMAQDDdyLDKALEgFAMFA--LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQE 347
Cdd:PRK09406 239 I----VMPSAD--LDRAAE-TAVTArvQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 348 QQNKILGCIATGRAEGAQVLTGGgERHEvGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYG 426
Cdd:PRK09406 312 GRDEVEKQVDDAVAAGATILCGG-KRPD-GPGWFYPPTVITDiTPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 491118422 427 LGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHI-YPAhAAFGGYKKSGIGRE 476
Cdd:PRK09406 390 LGSNAWTRDEAEQERFIDDLEAGQVFINGMTVsYPE-LPFGGVKRSGYGRE 439
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
12-474 |
3.69e-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: 232.08 E-value: 3.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 12 KVQFKAQYENFIGGEWVApvKGEYFENISPVD-GKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADR 90
Cdd:cd07083 12 KEEFGRAYPLVIGGEWVD--TKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 91 LEQNLELLAVAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYH--FHEPLGVVGQIIPWNFPI 168
Cdd:cd07083 90 LRRRRRELIATLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNesFYVGLGAGVVISPWNFPV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 169 LMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQL 247
Cdd:cd07083 169 AIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 248 IMQYATEN------IIPVTLELGGKspNIFFEDIMAQdddyLDKALEGFAMFALN-QGEICTCPSRALVQESIADRFLEK 320
Cdd:cd07083 249 IYEAAARLapgqtwFKRLYVETGGK--NAIIVDETAD----FELVVEGVVVSAFGfQGQKCSAASRLILTQGAYEPVLER 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 321 AIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLtgGGERHEvGSGFYIEPTIFKGTN-DMKIFQEE 399
Cdd:cd07083 323 LLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVL--GGKRLE-GEGYFVAPTVVEEVPpKARIAQEE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118422 400 IFGPVLSVTTFK--DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHI--YPAHAAFGGYKKSGIG 474
Cdd:cd07083 400 IFGPVLSVIRYKddDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGTN 478
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
14-474 |
9.82e-70 |
|
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: 231.70 E-value: 9.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 14 QFKAQYENFIGGEWVA-P-VKGEYFEN------ISPVDGKVFT-KVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNIL 84
Cdd:cd07125 18 ALADALKAFDEKEWEAiPiINGEETETgegapvIDPADHERTIgEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 85 LKIADRLEQNL-EL--LAVAETwdnGKPVRETLAaDIPLAIDHFRYFAGciRAQE--------GGISEIDEdtiaYHFHe 153
Cdd:cd07125 98 EKAADLLEANRgELiaLAAAEA---GKTLADADA-EVREAIDFCRYYAA--QARElfsdpelpGPTGELNG----LELH- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 154 PLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPR 232
Cdd:cd07125 167 GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAgVPRDVLQLVPGDGEEIGEALVAHPR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 233 IAKIAFTGSTQVGQLIMQ---YATENIIPVTLELGGKspNIFFEDIMAQDDDYLDKALE-GFamfaLNQGEICTCPSRAL 308
Cdd:cd07125 247 IDGVIFTGSTETAKLINRalaERDGPILPLIAETGGK--NAMIVDSTALPEQAVKDVVQsAF----GSAGQRCSALRLLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 309 VQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEG-----AQVltgggerhEVGSGFYIE 383
Cdd:cd07125 321 LQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAwliapAPL--------DDGNGYFVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 384 PTIFKGTNDmKIFQEEIFGPVLSVTTFK--DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGrvwtNCY----- 456
Cdd:cd07125 393 PGIIEIVGI-FDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYinrni 467
|
490 500
....*....|....*....|...
gi 491118422 457 -----HIYPahaaFGGYKKSGIG 474
Cdd:cd07125 468 tgaivGRQP----FGGWGLSGTG 486
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-479 |
6.76e-68 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 225.99 E-value: 6.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPvKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVA 101
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 102 ETWDNGKPVRET------LAADIPLAIDHFRyfagcirAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKL 175
Cdd:PRK09457 83 IARETGKPLWEAatevtaMINKIAISIQAYH-------ERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 176 APALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLI-MQYAT 253
Cdd:PRK09457 156 VPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQFAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 254 ENIIPVTLELGGKSPNIF--FEDIMAQDDDYLDKALegfamfaLNQGEICTCPSRALVQESI-ADRFLEKAIERVKRIKT 330
Cdd:PRK09457 235 QPEKILALEMGGNNPLVIdeVADIDAAVHLIIQSAF-------ISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 331 GHPL-DTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEvGSGFyIEPTIFKGTNDMKIFQEEIFGPVLSVTT 409
Cdd:PRK09457 308 GRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQA-GTGL-LTPGIIDVTGVAELPDEEYFGPLLQVVR 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491118422 410 FKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRV-WTNCYHIYPAHAAFGGYKKSGigreNHK 479
Cdd:PRK09457 386 YDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG----NHR 452
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
57-475 |
1.21e-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: 223.69 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 57 DIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETL------AADIPLAIDHFRYFAG 130
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQtevaamAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 131 cIRAQEGGiseideDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LP 209
Cdd:cd07095 81 -ERATPMA------QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 210 AGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLI-MQYATENIIPVTLELGGKSPniffedIMAQDDDYLDKALE 288
Cdd:cd07095 154 PGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPGKILALEMGGNNP------LVVWDVADIDAAAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 289 GFAMFA-LNQGEICTCPSRALV-QESIADRFLEKAIERVKRIKTGHPLDTET-MIGAQASQEQQNKILGCiATGRAEGAQ 365
Cdd:cd07095 227 LIVQSAfLTAGQRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAARYLLAQ-QDLLALGGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 366 VLtGGGERHEVGSGFyIEPTIFKGTNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRA 445
Cdd:cd07095 306 PL-LAMERLVAGTAF-LSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLAR 383
|
410 420 430
....*....|....*....|....*....|.
gi 491118422 446 IQAGRV-WTNCYHIYPAHAAFGGYKKSGIGR 475
Cdd:cd07095 384 IRAGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-485 |
5.91e-67 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 222.81 E-value: 5.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 38 NISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLA-- 115
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAev 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 116 ADIPLAIDHFRYFAGCIRAQEGGISEIDEDTIAYhfhEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPA 195
Cdd:PRK13968 91 AKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 196 SILVLVELIQDL-LPAGVLNVVNGYGVEVGRpLATNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFED 274
Cdd:PRK13968 168 CAQLIAQVFKDAgIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 275 imAQDDDYLDKALEGFAMfalNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILG 354
Cdd:PRK13968 247 --ADLELAVKAAVAGRYQ---NTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 355 CIATGRAEGAQVLTGGgERHEvGSGFYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWS 433
Cdd:PRK13968 322 QVEATLAEGARLLLGG-EKIA-GAGNYYAPTVLANvTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 491118422 434 RSAHTSYRAGRAIQAGRVWTNCYHIYPAHAAFGGYKKSGIGREnhkmmLEHY 485
Cdd:PRK13968 400 TDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE-----LSHF 446
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
148-475 |
4.90e-65 |
|
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: 216.62 E-value: 4.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 148 AYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGyGVEVGRPL 227
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVEG-GVEVATAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 228 ATNPrIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDImaqdddYLDKALE--GFAMFaLNQGEICTCPS 305
Cdd:cd07087 173 LAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDA------NLEVAARriAWGKF-LNAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 306 RALVQESIADRFLEKAIERVKRiktghpldtetMIGAQASQ-EQQNKILGCIATGR----AEGAQVLTGGG----ERhev 376
Cdd:cd07087 245 YVLVHESIKDELIEELKKAIKE-----------FYGEDPKEsPDYGRIINERHFDRlaslLDDGKVVIGGQvdkeER--- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 377 gsgfYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN- 454
Cdd:cd07087 311 ----YIAPTILDDvSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNd 386
|
330 340
....*....|....*....|..
gi 491118422 455 -CYHIYPAHAAFGGYKKSGIGR 475
Cdd:cd07087 387 vLLHAAIPNLPFGGVGNSGMGA 408
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
76-475 |
2.94e-62 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 209.65 E-value: 2.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 76 SPTTRSNILLKIADRLEQNLELLAVAETWD-NGKPVRETLAADIPLAIDHFRY----FAGCIRAQEGGISEIDEDTIAYH 150
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADfGHRSRHETLLAEILPSIAGIKHarkhLKKWMKPSRRHVGLLFLPAKAEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 151 FHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGyGVEVGRPLATN 230
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVTG-GADVAAAFSSL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 231 PrIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDIMaqdddyLDKALEGFAMF-ALNQGEICTCPSRALV 309
Cdd:cd07133 177 P-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDAD------LAKAAERIAFGkLLNAGQTCVAPDYVLV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 310 QESIADRFLEKAIERVKRI-KTGHPLDTETMIgaqASQEQQNKILGCIATGRAEGAQVLTGGGERHEVGSGFYIEPT-IF 387
Cdd:cd07133 250 PEDKLEEFVAAAKAAVAKMyPTLADNPDYTSI---INERHYARLQGLLEDARAKGARVIELNPAGEDFAATRKLPPTlVL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 388 KGTNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN--CYHIYPAHAAF 465
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtLLHVAQDDLPF 406
|
410
....*....|
gi 491118422 466 GGYKKSGIGR 475
Cdd:cd07133 407 GGVGASGMGA 416
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-489 |
1.36e-61 |
|
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: 208.97 E-value: 1.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVA 101
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 102 ETWDNGKpVRETLAADIPLAIDHFRYFAGCIRAQEGGISE-IDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALA 180
Cdd:TIGR01722 84 ITAEHGK-THSDALGDVARGLEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 181 AGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRpLATNPRIAKIAFTGSTQVGQLIMQYATENIIPV 259
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVLNVVHGDKEAVDR-LLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 260 TLELGGKSPNIFFEDimAQDDDYLDkALEGFAMFAlnQGEICTCPSRA-LVQEsiADRFLEKAIERVKRIKTGHPLDTET 338
Cdd:TIGR01722 242 QALGGAKNHMVVMPD--ADKDAAAD-ALVGAAYGA--AGQRCMAISAAvLVGA--ADEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 339 MIGAQASQEQQNKILGCIATGRAEGAQVLTGGG----ERHEvgSGFYIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDF 413
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRgykvDGYE--EGNWVGPTLLERVPpTMKAYQEEIFGPVLCVLEADTL 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118422 414 DEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYP-AHAAFGGYKKSGIGRENH--KMMLEHYQQTK 489
Cdd:TIGR01722 393 EEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPlPYFSFTGWKDSFFGDHHIygKQGTHFYTRGK 471
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
64-475 |
3.51e-59 |
|
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: 201.30 E-value: 3.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 64 AAHKA-KAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPVRETLAADI-PL------AIDHFRYFAgciRAQ 135
Cdd:cd07134 5 AAQQAhALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEIlPVlseinhAIKHLKKWM---KPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 136 EGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNV 215
Cdd:cd07134 82 RVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 216 VNGyGVEVGRPLATNPrIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFfedimaqDDDY-LDKALEGFAM-- 292
Cdd:cd07134 162 FEG-DAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIV-------DETAdLKKAAKKIAWgk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 293 FaLNQGEICTCPSRALVQESIADRFLE---KAIERV--KRIKTGHPLDTETMIGAQASqeqqNKILGCIATGRAEGAQVL 367
Cdd:cd07134 233 F-LNAGQTCIAPDYVFVHESVKDAFVEhlkAEIEKFygKDAARKASPDLARIVNDRHF----DRLKGLLDDAVAKGAKVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 368 TGG----GERhevgsgfYIEPTIFKG-TNDMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRA 442
Cdd:cd07134 308 FGGqfdaAQR-------YIAPTVLTNvTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKV 380
|
410 420 430
....*....|....*....|....*....|....*
gi 491118422 443 GRAIQAGRVWTN--CYHIYPAHAAFGGYKKSGIGR 475
Cdd:cd07134 381 LARTSSGGVVVNdvVLHFLNPNLPFGGVNNSGIGS 415
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
53-456 |
1.62e-58 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 209.41 E-value: 1.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 53 SSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNL-EL--LAVAE---TWDNG-KPVREtlaadiplAIDHF 125
Cdd:COG4230 590 ATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRaELmaLLVREagkTLPDAiAEVRE--------AVDFC 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 126 RYFAGCIRAQEGgiseidedtiAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPasiLV---LVE 202
Cdd:COG4230 662 RYYAAQARRLFA----------APTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTP---LIaarAVR 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 203 LIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLI-MQYATENIIPVTL--ELGGKspNiffedimaq 278
Cdd:COG4230 729 LLHEAgVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQ--N--------- 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 279 dddyldkalegfAMF----AL--------------NQGEICTcpsrAL----VQESIADRFLEKAIERVKRIKTGHPLDT 336
Cdd:COG4230 798 ------------AMIvdssALpeqvvddvlasafdSAGQRCS----ALrvlcVQEDIADRVLEMLKGAMAELRVGDPADL 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 337 ETMIGAQASQEQQNKILGCIATGRAEGaQVLTGGGERHEVGSGFYIEPTIFKgTNDMKIFQEEIFGPVLSVTTFK--DFD 414
Cdd:COG4230 862 STDVGPVIDAEARANLEAHIERMRAEG-RLVHQLPLPEECANGTFVAPTLIE-IDSISDLEREVFGPVLHVVRYKadELD 939
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 491118422 415 EAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGrvwtNCY 456
Cdd:COG4230 940 KVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVY 977
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
22-476 |
4.86e-58 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 200.45 E-value: 4.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 22 FIGGEWVApvKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVA 101
Cdd:PLN02315 24 YVGGEWRA--NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 102 ETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGGI--SEiDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPAL 179
Cdd:PLN02315 102 VSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIipSE-RPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 180 AAGNCIVLKPAEQTPASILVLVELIQDLL-----PAGVLNVVNGyGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATE 254
Cdd:PLN02315 180 VCGNCVVWKGAPTTPLITIAMTKLVAEVLeknnlPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 255 NIIPVTLELGGKSPniffedIMAQDDDYLDKALEGfAMFAL--NQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGH 332
Cdd:PLN02315 259 RFGKCLLELSGNNA------IIVMDDADIQLAVRS-VLFAAvgTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 333 PLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHevGSGFYIEPTIFKGTNDMKIFQEEIFGPVLSVTTFKD 412
Cdd:PLN02315 332 PLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE--SEGNFVQPTIVEISPDADVVKEELFGPVLYVMKFKT 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 413 FDEAIKIANDTIYGLGAGVWSRSAHTSYR------AGRAIQAGRVWTNCYHIypaHAAFGGYKKSGIGRE 476
Cdd:PLN02315 410 LEEAIEINNSVPQGLSSSIFTRNPETIFKwigplgSDCGIVNVNIPTNGAEI---GGAFGGEKATGGGRE 476
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
105-475 |
3.79e-57 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 196.57 E-value: 3.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 105 DNGKPVRETLA-------ADIPLAIDHFRYFAGCIRAQeggiseidedTIAYHFH-------EPLGVVGQIIPWNFPILM 170
Cdd:cd07136 47 DLGKSEFEAYMteigfvlSEINYAIKHLKKWMKPKRVK----------TPLLNFPsksyiyyEPYGVVLIIAPWNYPFQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 171 AtwkLAP---ALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGyGVEVGRPLaTNPRIAKIAFTGSTQVGQL 247
Cdd:cd07136 117 A---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVEG-GVEENQEL-LDQKFDYIFFTGSVRVGKI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 248 IMQYATENIIPVTLELGGKSPNIFFEDimAQdddyLDKALE--GFAMFaLNQGEICTCPSRALVQESIADRFLEKAIERV 325
Cdd:cd07136 192 VMEAAAKHLTPVTLELGGKSPCIVDED--AN----LKLAAKriVWGKF-LNAGQTCVAPDYVLVHESVKEKFIKELKEEI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 326 KRIKTGHPLDTETMiGAQASQEQQNKILGCIatgraEGAQVLTGGGERHEvgsGFYIEPTIFKG-TNDMKIFQEEIFGPV 404
Cdd:cd07136 265 KKFYGEDPLESPDY-GRIINEKHFDRLAGLL-----DNGKIVFGGNTDRE---TLYIEPTILDNvTWDDPVMQEEIFGPI 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 405 LSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN--CYHIYPAHAAFGGYKKSGIGR 475
Cdd:cd07136 336 LPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtIMHLANPYLPFGGVGNSGMGS 408
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
54-474 |
5.92e-57 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 204.71 E-value: 5.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 54 SAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNL-ELLAVA-----ETWDNG-KPVREtlaadiplAIDHFR 126
Cdd:PRK11905 588 SAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMpELFALAvreagKTLANAiAEVRE--------AVDFLR 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 127 YFAGCIRAQEGGISeidedtiayhfHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQD 206
Cdd:PRK11905 660 YYAAQARRLLNGPG-----------HKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHE 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 207 L-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLI---MQYATENIIPVTLELGGkspniffEDIMAQD--- 279
Cdd:PRK11905 729 AgVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIqrtLAKRSGPPVPLIAETGG-------QNAMIVDssa 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 280 ------DDYL----DKAlegfamfalnqGEICTcpsrAL----VQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQAS 345
Cdd:PRK11905 802 lpeqvvADVIasafDSA-----------GQRCS----ALrvlcLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVID 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 346 QEQQNKILGCIATGRAEGAQVltgggERHEVGS----GFYIEPTIF--KGTNDMKifqEEIFGPVLSVTTFK--DFDEAI 417
Cdd:PRK11905 867 AEAQANIEAHIEAMRAAGRLV-----HQLPLPAetekGTFVAPTLIeiDSISDLE---REVFGPVLHVVRFKadELDRVI 938
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 418 KIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHI------YPahaaFGGYKKSGIG 474
Cdd:PRK11905 939 DDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIgavvgvQP----FGGEGLSGTG 997
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
153-474 |
1.03e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 196.40 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 153 EPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGyGVEVGRPLATNPr 232
Cdd:PTZ00381 108 EPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEG-GVEVTTELLKEP- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 233 IAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFfedimaqdDDYLDKALEGFAMF---ALNQGEICTCPSRALV 309
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIV--------DKSCNLKVAARRIAwgkFLNAGQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 310 QESIADRFLEKAIERVKRiktghpldtetMIGA-QASQEQQNKILGCIATGRAE------GAQVLTGGgerhEVG-SGFY 381
Cdd:PTZ00381 258 HRSIKDKFIEALKEAIKE-----------FFGEdPKKSEDYSRIVNEFHTKRLAelikdhGGKVVYGG----EVDiENKY 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 382 IEPTIFkgTN---DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN--CY 456
Cdd:PTZ00381 323 VAPTII--VNpdlDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVF 400
|
330
....*....|....*...
gi 491118422 457 HIYPAHAAFGGYKKSGIG 474
Cdd:PTZ00381 401 HLLNPNLPFGGVGNSGMG 418
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-499 |
1.50e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 198.43 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 6 PNQpGSKVQFKAQYENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILL 85
Cdd:PLN02419 102 PEQ-STQPQMPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVML 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 86 KIADRLEQNLELLAVAETWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQEGG-ISEIDEDTIAYHFHEPLGVVGQIIPW 164
Cdd:PLN02419 181 KFQELIRKNMDKLAMNITTEQGKTLKDS-HGDIFRGLEVVEHACGMATLQMGEyLPNVSNGVDTYSIREPLGVCAGICPF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 165 NFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGrPLATNPRIAKIAFTGSTQ 243
Cdd:PLN02419 260 NFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAgLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNT 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 244 VGQLIMQYATENIIPVTLELGGKSPNIFFEDimAQDDDYLDKAL-EGFAMfalnQGEICTCPSrALVQESIADRFLEKAI 322
Cdd:PLN02419 339 AGMHIYARAAAKGKRIQSNMGAKNHGLVLPD--ANIDATLNALLaAGFGA----AGQRCMALS-TVVFVGDAKSWEDKLV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 323 ERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEVG--SGFYIEPTIFKG-TNDMKIFQEE 399
Cdd:PLN02419 412 ERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGyeKGNFIGPTILSGvTPDMECYKEE 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 400 IFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIYP-AHAAFGGYKKSGIGRENH 478
Cdd:PLN02419 492 IFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPlPFFSFTGNKASFAGDLNF 571
|
490 500
....*....|....*....|...
gi 491118422 479 --KMMLEHYQQTKNLLVSYSTKP 499
Cdd:PLN02419 572 ygKAGVDFFTQIKLVTQKQKDIH 594
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
39-474 |
3.29e-55 |
|
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: 191.48 E-value: 3.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 39 ISPVDGKVFTKVPRSSAEDIELALDAA---HKAKAQWnsSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKP-----V 110
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAhalFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPlvdakV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 111 RETLAAD-IPLAIDHFRYFAGciRAQEGGISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKP 189
Cdd:cd07148 82 EVTRAIDgVELAADELGQLGG--REIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 190 AEQTPASILVLVELIQDL-LPAGVLNVVnGYGVEVGRPLATNPRIAKIAFTGSTQVGqlimQYATENIIPVT---LELGG 265
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAgLPEGWCQAV-PCENAVAEKLVTDPRVAFFSFIGSARVG----WMLRSKLAPGTrcaLEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 266 KSPNIffedimAQDDDYLDKALE-----GFamfaLNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMI 340
Cdd:cd07148 235 AAPVI------VDRSADLDAMIPplvkgGF----YHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 341 GAQASQEQQNKILGCIATGRAEGAQVLTGGgerHEVGSGFYiEPT-IFKGTNDMKIFQEEIFGPVLSVTTFKDFDEAIKI 419
Cdd:cd07148 305 GPLIRPREVDRVEEWVNEAVAAGARLLCGG---KRLSDTTY-APTvLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQ 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491118422 420 ANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNcyhiypAHAA-------FGGYKKSGIG 474
Cdd:cd07148 381 ANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVN------DHTAfrvdwmpFAGRRQSGYG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
4-456 |
7.99e-54 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 195.42 E-value: 7.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 4 VDPNQPGSKVQFKAQYENFIGGEWVAP----VKGEYFENISPVDG-KVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPT 78
Cdd:PRK11904 528 LNLNDRSELEPLAAAIAAFLEKQWQAGpiinGEGEARPVVSPADRrRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 79 TRSNILLKIADRLEQNL-ELLA--VAE---TWDNG-KPVREtlaadiplAIDHFRYFAGCIRAQEGGISEI----DEDTI 147
Cdd:PRK11904 608 ERAAILERAADLLEANRaELIAlcVREagkTLQDAiAEVRE--------AVDFCRYYAAQARRLFGAPEKLpgptGESNE 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 148 AyhFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPasiLVLVELIQDL----LPAGVLNVVNGYGVEV 223
Cdd:PRK11904 680 L--RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTP---LIAAEAVKLLheagIPKDVLQLLPGDGATV 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 224 GRPLATNPRIAKIAFTGSTQVGQLIMQ-YATEN--IIPVTLELGGKspNIFFEDIMAQD----DDYLDKAlegFAmfalN 296
Cdd:PRK11904 755 GAALTADPRIAGVAFTGSTETARIINRtLAARDgpIVPLIAETGGQ--NAMIVDSTALPeqvvDDVVTSA---FR----S 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 297 QGEICTcpsrAL----VQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEG---AQVLTG 369
Cdd:PRK11904 826 AGQRCS----ALrvlfVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLP 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 370 GGERHevgsGFYIEPTIFKgTNDMKIFQEEIFGPVLSVTTFK--DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQ 447
Cdd:PRK11904 902 AGTEN----GHFVAPTAFE-IDSISQLEREVFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVR 976
|
....*....
gi 491118422 448 AGrvwtNCY 456
Cdd:PRK11904 977 VG----NVY 981
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
53-475 |
1.39e-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: 183.96 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 53 SSAEDIELALDAAHKakaqwnssspTTRSNILLKIADRLEQ----------NLELLAVAETWDNGKPVRETLAADIPLAI 122
Cdd:cd07135 2 TPLDEIDSIHSRLRA----------TFRSGKTKDLEYRLWQlkqlywavkdNEEAIVEALKKDLGRPPFETLLTEVSGVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 123 DHFRYFagciraqeggISEIDE--------DTIAYHF-------HEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVL 187
Cdd:cd07135 72 NDILHM----------LKNLKKwakdekvkDGPLAFMfgkprirKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 188 KPAEQTPASILVLVELIQDLLPAGVLNVVNGyGV-EVGRPLatNPRIAKIAFTGSTQVGQLIMQYATENIIPVTLELGGK 266
Cdd:cd07135 142 KPSELTPHTAALLAELVPKYLDPDAFQVVQG-GVpETTALL--EQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 267 SPNIFFEDImaqDDDYLDKALegfaMFA--LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMiGAQA 344
Cdd:cd07135 219 SPVIVTKNA---DLELAAKRI----LWGkfGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDY-TRIV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 345 SQEQQNKILGCIATgraEGAQVLTGGgeRHEVGSGFyIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDT 423
Cdd:cd07135 291 NPRHFNRLKSLLDT---TKGKVVIGG--EMDEATRF-IPPTIVSDVSwDDSLMSEELFGPVLPIIKVDDLDEAIKVINSR 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 491118422 424 IYGLGAGVWSRSAH------TSYRAGraiqaGRVWTNCY-HIYPAHAAFGGYKKSGIGR 475
Cdd:cd07135 365 DTPLALYIFTDDKSeidhilTRTRSG-----GVVINDTLiHVGVDNAPFGGVGDSGYGA 418
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
14-474 |
3.26e-52 |
|
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: 184.34 E-value: 3.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 14 QFKAQYENFIGGEW-VAPVKGEYFEN-------ISPVDGK-VFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNIL 84
Cdd:TIGR01238 23 PLEAQIHAWADKTWqAAPIIGHSYKAdgeaqpvTNPADRRdIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 85 LKIADRLEQNLELLAVAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRaqeggiSEIDEDTiayhfHEPLGVVGQIIPW 164
Cdd:TIGR01238 103 DRLADLLELHMPELMALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVR------DVLGEFS-----VESRGVFVCISPW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 165 NFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQ 243
Cdd:TIGR01238 171 NFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 244 VGQLIMQYATE---NIIPVTLELGGKSPNIFFEDIMAQD--DDYLDKALEgfamfalNQGEICTCPSRALVQESIADRFL 318
Cdd:TIGR01238 251 VAQLINQTLAQredAPVPLIAETGGQNAMIVDSTALPEQvvRDVLRSAFD-------SAGQRCSALRVLCVQEDVADRVL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 319 EKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEG---AQVLTGGGERHEVGSgfYIEPTIFKgTNDMKI 395
Cdd:TIGR01238 324 TMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGT--FVAPTLFE-LDDIAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 396 FQEEIFGPVLSVTTFK--DFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN------CYHIYPahaaFGG 467
Cdd:TIGR01238 401 LSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrnqvgaVVGVQP----FGG 476
|
....*..
gi 491118422 468 YKKSGIG 474
Cdd:TIGR01238 477 QGLSGTG 483
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
19-474 |
3.57e-49 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 176.10 E-value: 3.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 19 YENFIGGEWVAPVKGEYFENISPVDGKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELL 98
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 99 AVAETWDNGKPVRETLAaDIPLAIDHFRYFA--GCIRAQEGGISEID------EDTIAYHFHEPLGVVGQIIPWNFPILM 170
Cdd:PLN00412 96 AECLVKEIAKPAKDAVT-EVVRSGDLISYTAeeGVRILGEGKFLVSDsfpgneRNKYCLTSKIPLGVVLAIPPFNYPVNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 171 ATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGStQVGQLIM 249
Cdd:PLN00412 175 AVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 250 QYAteNIIPVTLELGGKSPNIFFEDimaQDDDYLDKAL--EGFAMfalnQGEICTCPSRALVQESIADRFLEKAIERVKR 327
Cdd:PLN00412 254 KKA--GMVPLQMELGGKDACIVLED---ADLDLAAANIikGGFSY----SGQRCTAVKVVLVMESVADALVEKVNAKVAK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 328 IKTGHPLDtETMIGAQASQEQQNKILGCIATGRAEGAQVLTggGERHEvgsGFYIEPTIFKG-TNDMKIFQEEIFGPVLS 406
Cdd:PLN00412 325 LTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQ--EWKRE---GNLIWPLLLDNvRPDMRIAWEEPFGPVLP 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118422 407 VTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHIY-PAHAAFGGYKKSGIG 474
Cdd:PLN00412 399 VIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARgPDHFPFQGLKDSGIG 467
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
50-454 |
1.18e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 174.78 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 50 VPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAvaetwdnGKPVRE---TLA---ADIPLAID 123
Cdd:PRK11809 676 VREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLM-------GLLVREagkTFSnaiAEVREAVD 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 124 HFRYFAGCIRAqeggisEIDEDTiayhfHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPasiLVLVEL 203
Cdd:PRK11809 749 FLRYYAGQVRD------DFDNDT-----HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTP---LIAAQA 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 204 IQDLL----PAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQyateNI----------IPVTLELGGKSPN 269
Cdd:PRK11809 815 VRILLeagvPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQR----NLagrldpqgrpIPLIAETGGQNAM 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 270 I-----FFEDIMAqddDYLDKALEgfamfalNQGEICTcpsrAL----VQESIADRFLEKAIERVKRIKTGHPLDTETMI 340
Cdd:PRK11809 891 IvdssaLTEQVVA---DVLASAFD-------SAGQRCS----ALrvlcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDI 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 341 GAQASQEQQNKILGCIATGRAEGAQVL-TGGGERHEVGSGFYIEPTIFKgTNDMKIFQEEIFGPVLSVTTFK--DFDEAI 417
Cdd:PRK11809 957 GPVIDAEAKANIERHIQAMRAKGRPVFqAARENSEDWQSGTFVPPTLIE-LDSFDELKREVFGPVLHVVRYNrnQLDELI 1035
|
410 420 430
....*....|....*....|....*....|....*..
gi 491118422 418 KIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN 454
Cdd:PRK11809 1036 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1072
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
105-422 |
1.45e-45 |
|
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: 165.09 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 105 DNGKPVRETLAA-------DIPLAIDHFRYFAGCIRAQEGGISEIDEdtiAYHFHEPLGVVGQIIPWNFPILMATWKLAP 177
Cdd:cd07132 47 DLRKPKFEAVLSeillvknEIKYAISNLPEWMKPEPVKKNLATLLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 178 ALAAGNCIVLKPAEQTPASILVLVELI-----QDLLPagvlnVVNGyGVEVGRPLaTNPRIAKIAFTGSTQVGQLIMQYA 252
Cdd:cd07132 124 AIAAGNCVVIKPSEVSPATAKLLAELIpkyldKECYP-----VVLG-GVEETTEL-LKQRFDYIFYTGSTSVGKIVMQAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 253 TENIIPVTLELGGKSPNiffedimaqdddYLDKALE--------GFAMFaLNQGEICTCPSRALVQESIADRFLEKAIER 324
Cdd:cd07132 197 AKHLTPVTLELGGKSPC------------YVDKSCDidvaarriAWGKF-INAGQTCIAPDYVLCTPEVQEKFVEALKKT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 325 VKRIKTGHPLDTETMiGAQASQEQQNKILGCIatgraEGAQVLTGG----GERhevgsgfYIEPTIFKGTNDM-KIFQEE 399
Cdd:cd07132 264 LKEFYGEDPKESPDY-GRIINDRHFQRLKKLL-----SGGKVAIGGqtdeKER-------YIAPTVLTDVKPSdPVMQEE 330
|
330 340
....*....|....*....|...
gi 491118422 400 IFGPVLSVTTFKDFDEAIKIAND 422
Cdd:cd07132 331 IFGPILPIVTVNNLDEAIEFINS 353
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
23-434 |
5.40e-45 |
|
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: 165.45 E-value: 5.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 23 IGGEWVAPvkGEYFENISPVD-GKVFTKVPRSSAEDIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNL--ELLA 99
Cdd:cd07123 37 IGGKEVRT--GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYryELNA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 100 vAETWDNGKPVREtlaADIPLA---IDHFR---YFAGCIRAQEggisEIDEDTIAYHF--HEPL-GVVGQIIPWNFPILM 170
Cdd:cd07123 115 -ATMLGQGKNVWQ---AEIDAAcelIDFLRfnvKYAEELYAQQ----PLSSPAGVWNRleYRPLeGFVYAVSPFNFTAIG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 171 ATWKLAPALAaGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIM 249
Cdd:cd07123 187 GNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAgLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLW 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 250 QYATENI-----IP-VTLELGGKspNIFFEDIMAQDDDYLDKALEGFAMFalnQGEICTCPSRALVQESIADRFLEKAIE 323
Cdd:cd07123 266 KQIGENLdryrtYPrIVGETGGK--NFHLVHPSADVDSLVTATVRGAFEY---QGQKCSAASRAYVPESLWPEVKERLLE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 324 RVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAE-GAQVLTGGGERHEVGsgFYIEPTIFKGTN-DMKIFQEEIF 401
Cdd:cd07123 341 ELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVG--YFVEPTVIETTDpKHKLMTEEIF 418
|
410 420 430
....*....|....*....|....*....|....*.
gi 491118422 402 GPVLSVTTFKD--FDEAIKIANDT-IYGLGAGVWSR 434
Cdd:cd07123 419 GPVLTVYVYPDsdFEETLELVDTTsPYALTGAIFAQ 454
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
153-493 |
7.54e-43 |
|
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: 157.57 E-value: 7.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 153 EPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGyGVEVGRPLATNpR 232
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEG-GVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 233 IAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFfedimaqdDDYLDK--ALEGFAM--FALNQGEICTCPSRAL 308
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIV--------DSTVDLkvAVRRIAGgkWGCNNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 309 VQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQ--------NKILGCIATgraegaqvltgGGERHEvgSGF 380
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQrlsrllddPSVADKIVH-----------GGERDE--KNL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 381 YIEPTIFKGTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN--CYH 457
Cdd:cd07137 317 YIEPTILLDPPlDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtVVQ 396
|
330 340 350
....*....|....*....|....*....|....*.
gi 491118422 458 IYPAHAAFGGYKKSGIGRENHKMMLEHYQQTKNLLV 493
Cdd:cd07137 397 YAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
153-492 |
1.17e-37 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 144.10 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 153 EPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGyGVEVGRPLATNpR 232
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEG-GPAVGEQLLQH-K 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 233 IAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPNIFFEDIMAQDDDYLDKALEGfAMFALNQGEICTCPSRALVQES 312
Cdd:PLN02203 185 WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTKVAVNRIVG-GKWGSCAGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 313 IADRFLEKAIERVKRIKTGHPLDTETMigAQASQEQQNKILGCIATGRAEGAQVLTGGGERHEvgsGFYIEPTIFKGTN- 391
Cdd:PLN02203 264 FAPILIELLKSTIKKFFGENPRESKSM--ARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEK---KLFIEPTILLNPPl 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 392 DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTNCYHI-YPAHA-AFGGYK 469
Cdd:PLN02203 339 DSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIqYACDSlPFGGVG 418
|
330 340
....*....|....*....|...
gi 491118422 470 KSGIGRENHKMMLEHYQQTKNLL 492
Cdd:PLN02203 419 ESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
59-476 |
1.02e-34 |
|
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: 135.44 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 59 ELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAETWDNGKPvrETLAADIPLAIDHFRYFAGCIRAqeGG 138
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG--WMFAENICGDQVQLRARAFVIYS--YR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 139 ISEIDEDTI-------AYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQD--LLP 209
Cdd:cd07084 78 IPHEPGNHLgqglkqqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 210 AGVLNVVNGYGvEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATEniIPVTLELGGKSPNIFFEDimAQDDDYLDKALEg 289
Cdd:cd07084 158 PEDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPD--AQAVDYVAWQCV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 290 FAMFaLNQGEICTCPSRALVQESIADR-FLEKAIERVKRIKtghplDTETMIGAqasqEQQNKILGCIATGRAEGAQVLT 368
Cdd:cd07084 232 QDMT-ACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRK-----LEDLLLGP----VQTFTTLAMIAHMENLLGSVLL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 369 -GGGERHEVGSGFYI---EPTIFKGTND-----MKIFQEEIFGPVLSVTTFKDFDEAIKIA---------NDTIYGLGAG 430
Cdd:cd07084 302 fSGKELKNHSIPSIYgacVASALFVPIDeilktYELVTEEIFGPFAIVVEYKKDQLALVLEllermhgslTAAIYSNDPI 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 491118422 431 VWSRSAHTSYRAGRAIQAGRVWTNcyhIYPAHAAFGGYKKSGIGRE 476
Cdd:cd07084 382 FLQELIGNLWVAGRTYAILRGRTG---VAPNQNHGGGPAADPRGAG 424
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
58-421 |
6.69e-32 |
|
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: 127.27 E-value: 6.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 58 IELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELL---AVAETwdnGKPVREtLAADIPLAIDHFRYFAGCIRA 134
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELvarAHAET---GLPEAR-LQGELGRTTGQLRLFADLVRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 135 QEGGISEIDE-----------DTIAYHFhePLGVVGQIIPWNFPILMATW--KLAPALAAGNCIVLKPAEQTPA-SILVl 200
Cdd:cd07129 77 GSWLDARIDPadpdrqplprpDLRRMLV--PLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAHPAHPGtSELV- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 201 VELIQDL-----LPAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQ--YATENIIPVTLELGGKSPNIFFE 273
Cdd:cd07129 154 ARAIRAAlratgLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDaaAARPEPIPFYAELGSVNPVFILP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 274 DIMAQDDDYLDKALegFAMFALNQGEICTCPSRALVQESIA-DRFLEKAIERVKRIKtGHPLDTETMigAQASQEQQNKI 352
Cdd:cd07129 234 GALAERGEAIAQGF--VGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAP-AQTMLTPGI--AEAYRQGVEAL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 353 LGciatgrAEGAQVLTGGGERhevGSGFYIEPTIFK--GTNDMK--IFQEEIFGPVLSVTTFKDFDEAIKIAN 421
Cdd:cd07129 309 AA------APGVRVLAGGAAA---EGGNQAAPTLFKvdAAAFLAdpALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
153-492 |
3.80e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 125.93 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 153 EPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVLNVVNGYGVEVGRPLATnpR 232
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALLEQ--K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 233 IAKIAFTGSTQVGQLIMQYATENIIPVTLELGGKSPniffedIMAQDDDYLDKALEGF--AMFALNQGEICTCPSRALVQ 310
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSP------VVVDSDTDLKVTVRRIiaGKWGCNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 311 ESIADRFLEKAIERVKRIKTGHPLDTETM--IGAQASQEQQNKILgciatGRAEGAQVLTGGGERHEvgSGFYIEPTIFK 388
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPMESKDMsrIVNSTHFDRLSKLL-----DEKEVSDKIVYGGEKDR--ENLKIAPTILL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 389 GTN-DMKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWSRSAHTSYRAGRAIQAGRVWTN--CYHIYPAHAAF 465
Cdd:PLN02174 336 DVPlDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiAVHLALHTLPF 415
|
330 340
....*....|....*....|....*..
gi 491118422 466 GGYKKSGIGRENHKMMLEHYQQTKNLL 492
Cdd:PLN02174 416 GGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
20-421 |
4.21e-26 |
|
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: 111.21 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 20 ENFIGGEWVAPvKGEYFENISPVDGKVftkVPRSSAEDIELALDAAH-KAKAQWNSSSPT--TRSNILLKIADRL-EQNL 95
Cdd:cd07128 2 QSYVAGQWHAG-TGDGRTLHDAVTGEV---VARVSSEGLDFAAAVAYaREKGGPALRALTfhERAAMLKALAKYLmERKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 96 ELLAVAETwdNGKPVRETlAADIPLAIDHFRYFAGCIRAQ--------EGGISEIDEDT--IAYHFHEPL-GVVGQIIPW 164
Cdd:cd07128 78 DLYALSAA--TGATRRDS-WIDIDGGIGTLFAYASLGRRElpnahflvEGDVEPLSKDGtfVGQHILTPRrGVAVHINAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 165 NFPIlmatW----KLAPALAAGNCIVLKPAEQTPASILVLVELIQD--LLPAGVLNVVNGygvEVGRPLAT-NPRIAkIA 237
Cdd:cd07128 155 NFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICG---SVGDLLDHlGEQDV-VA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 238 FTGSTQVGQLIMQYA--TENIIPVTLELGGKSPNIFFEDimAQDDDyldkalEGFAMFA--------LNQGEICTCPSRA 307
Cdd:cd07128 227 FTGSAATAAKLRAHPniVARSIRFNAEADSLNAAILGPD--ATPGT------PEFDLFVkevaremtVKAGQKCTAIRRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 308 LVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEgAQVLTGGGERHEV-----GSGFYI 382
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGPDRFEVvgadaEKGAFF 377
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 491118422 383 EPTIFKGTNDMK---IFQEEIFGPVLSVTTFKDFDEAIKIAN 421
Cdd:cd07128 378 PPTLLLCDDPDAataVHDVEAFGPVATLMPYDSLAEAIELAA 419
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
20-433 |
1.05e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 88.99 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 20 ENFIGGEWVAPvKGEYFENISPVDGKVFTKVprsSAEDIELALDAAHkAKAQWNSS----SPTTRSNILLKIADRLEQNL 95
Cdd:PRK11903 6 ANYVAGRWQAG-SGAGTPLFDPVTGEELVRV---SATGLDLAAAFAF-AREQGGAAlralTYAQRAALLAAIVKVLQANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 96 E-LLAVAETwdNGKPVRETLAADIPLAIDHFRYFA------GCIRA-QEGGISEIDEDTI--AYHFHEPL-GVVGQIIPW 164
Cdd:PRK11903 81 DaYYDIATA--NSGTTRNDSAVDIDGGIFTLGYYAklgaalGDARLlRDGEAVQLGKDPAfqGQHVLVPTrGVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 165 NFPilmaTW----KLAPALAAGNCIVLKPAEQTPASILVLVELIQD--LLPAGVLNVVNGYGVEVgrpLATNPRIAKIAF 238
Cdd:PRK11903 159 NFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAagILPAGALSVVCGSSAGL---LDHLQPFDVVSF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 239 TGSTQVGQLIMQYAteNIIPVTLELggkspNIffedimaqDDDYLDKAL---------EGFAMFA--------LNQGEIC 301
Cdd:PRK11903 232 TGSAETAAVLRSHP--AVVQRSVRV-----NV--------EADSLNSALlgpdaapgsEAFDLFVkevvremtVKSGQKC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 302 TCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIGAQASQEQQNKILGCIATGRAEgAQVLTGGGERHEVGS--- 378
Cdd:PRK11903 297 TAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGFALVDAdpa 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 379 -GFYIEPTIFkGTND----MKIFQEEIFGPVLSVTTFKDFDEAIKIANDTIYGLGAGVWS 433
Cdd:PRK11903 376 vAACVGPTLL-GASDpdaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
57-472 |
2.02e-12 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 69.43 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 57 DIELALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQNLELLAVAetwdngkpVRETLAADIPLAidhfrYFAGCIRAQE 136
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHA--------VMHTTGQAFMMA-----FQAGGPHAQD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 137 GGIS-------EIDEDTIAYHFHEPLGVVGQ--------IIPWNFPILMA-----TWKLAPA----LAAGNCIVLKPAeq 192
Cdd:cd07127 152 RGLEavayawrEMSRIPPTAEWEKPQGKHDPlamektftVVPRGVALVIGcstfpTWNGYPGlfasLATGNPVIVKPH-- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 193 tPASILVL---VELIQDLL------PAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYATENIipVTLEL 263
Cdd:cd07127 230 -PAAILPLaitVQVAREVLaeagfdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--VYTEK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 264 GGKSPNIffedIMAQDDdyLDKALEGFAM-FALNQGEICTCPSRALV-QESIADR-----FLEKAIERVKRIK--TGHPL 334
Cdd:cd07127 307 AGVNTVV----VDSTDD--LKAMLRNLAFsLSLYSGQMCTTPQNIYVpRDGIQTDdgrksFDEVAADLAAAIDglLADPA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 335 DTETMIGAQASQEqqnkILGCIATGRAEGAQVLTGGGERHEVGSGFYIE-PTIFKGT-NDMKIFQEEIFGPVLSVTTFKD 412
Cdd:cd07127 381 RAAALLGAIQSPD----TLARIAEARQLGEVLLASEAVAHPEFPDARVRtPLLLKLDaSDEAAYAEERFGPIAFVVATDS 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118422 413 FDEAIKIANDTIYGLGAGVWS----------RSAHTSYRAGRAIQ---AGRVWTNcyhiypAHAAFGGYKKSG 472
Cdd:cd07127 457 TDHSIELARESVREHGAMTVGvystdpevveRVQEAALDAGVALSinlTGGVFVN------QSAAFSDFHGTG 523
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
154-415 |
1.68e-08 |
|
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: 56.74 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 154 PLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-LPAGVLNVVNGYGVEVGRPL-ATNP 231
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCgMPATDVDLIHSDGPTMNKILlEANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 232 RIakIAFTGSTQVGQlimQYATENIIPVTLELGGKSPNIFFEDImaQDDDYLDKALEGFAMFAlnQGEICTCPS-----R 306
Cdd:cd07126 222 RM--TLFTGSSKVAE---RLALELHGKVKLEDAGFDWKILGPDV--SDVDYVAWQCDQDAYAC--SGQKCSAQSilfahE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 307 ALVQESIADRFLEKAIERVKRIKTGHPLDTETmigAQASQEQQNKILGCiatgraEGAQVLTGGGE--RHEVGSGF-YIE 383
Cdd:cd07126 293 NWVQAGILDKLKALAEQRKLEDLTIGPVLTWT---TERILDHVDKLLAI------PGAKVLFGGKPltNHSIPSIYgAYE 363
|
250 260 270
....*....|....*....|....*....|....*....
gi 491118422 384 PT-IF------KGTNDMKIFQEEIFGPVLSVTTFKDFDE 415
Cdd:cd07126 364 PTaVFvpleeiAIEENFELVTTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
63-341 |
1.46e-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: 50.30 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 63 DAAHKAKAQWNSSSPTTRSNILLKIADRLE---QNLELLAVAETWDNGKPVRETLAADIPLAIDHFRYfagcIRAQEGGI 139
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYdtrQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYK----NIDTERGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 140 SEIDEDTI---------AYHFHEPLGVVGQIIPWNFPILMATwKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPA 210
Cdd:cd07077 77 TASVGHIQdvllpdngeTYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 211 G----VLNVVNGYGVEVGRPLATNPRIAKIAFTGSTQVGQLIMQYAteNIIPVTLELGGKSPNIFFEdimaqdDDYLDKA 286
Cdd:cd07077 156 HgpkiLVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDE------TADEERA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 491118422 287 LEGFAMFALNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLDTETMIG 341
Cdd:cd07077 228 SGSVHDSKFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSK 282
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
138-467 |
2.79e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 46.33 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 138 GISEIDEDT----IAyhfhEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDL-----L 208
Cdd:cd07122 79 GVIEEDEEKgiveIA----EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaagA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 209 PAGVLNVVNGYGVEVGRPLATNPRIAKIAFTGSTqvGQLIMQYATENiiPVtleLG---GKSPnIFFE---DI-MAQDDD 281
Cdd:cd07122 155 PEGLIQWIEEPSIELTQELMKHPDVDLILATGGP--GMVKAAYSSGK--PA---IGvgpGNVP-AYIDetaDIkRAVKDI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 282 YLDKALEgfamfalnQGEICTCPSRALVQESIADRFL------------EKAIERVKRI--KTGHPLDTETMigAQASQE 347
Cdd:cd07122 227 ILSKTFD--------NGTICASEQSVIVDDEIYDEVRaelkrrgayflnEEEKEKLEKAlfDDGGTLNPDIV--GKSAQK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 348 qqnkilgcIAT----GRAEGAQVLtgGGERHEVGSGfyiEPtifkgtndmkiFQEEIFGPVLSVTTFKDFDEAIKIAND- 422
Cdd:cd07122 297 --------IAElagiEVPEDTKVL--VAEETGVGPE---EP-----------LSREKLSPVLAFYRAEDFEEALEKAREl 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 491118422 423 -TIYGLG--AGVWSRSAHTSYRAGRAIQAGRVWTNCyhiyPahAAFGG 467
Cdd:cd07122 353 lEYGGAGhtAVIHSNDEEVIEEFALRMPVSRILVNT----P--SSLGG 394
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
61-420 |
4.84e-04 |
|
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: 42.64 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 61 ALDAAHKAKAQWNSSSPTTRSNILLKIADRLEQ---NLELLAVAETwdnGKPVRETlaadiPLAIDHF--RYFAGCIRAQ 135
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDariDLAKLAVSET---GMGRVED-----KVIKNHFaaEYIYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 136 EG-GISEIDEDTIAYHFHEPLGVVGQIIPWNFPILMATWKLAPALAAGNCIVLKPAEQTP-ASILVLVELIQDLLPAG-- 211
Cdd:cd07081 76 KTcGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKkVTQRAATLLLQAAVAAGap 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 212 --VLNVVNGYGVEVGRPLATNPRIAKIAFTGstqvGQLIMQYATENIIPVTLELGGKSPniffedIMAQDDDYLDKALEG 289
Cdd:cd07081 156 enLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTP------VVIDETADIKRAVQS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 290 FAMFA-LNQGEICTCPSRALVQESIADRFLEKAIERVKRIKTGHPLdtetmigaqasQEQQNKILGCIA-----TGRAEG 363
Cdd:cd07081 226 IVKSKtFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEEL-----------QQVQPVILKNGDvnrdiVGQDAY 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 491118422 364 AQVLTGGGERHEVGSGFYIEPTIFkgtNDMKIFQEEIFGPVLSVTTFKDFDEAIKIA 420
Cdd:cd07081 295 KIAAAAGLKVPQETRILIGEVTSL---AEHEPFAHEKLSPVLAMYRAANFADADAKA 348
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
154-348 |
6.47e-04 |
|
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: 42.26 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 154 PLGVVGQIIPWNFPILmATWKLAPALAAGNCIVLKPAEQTPASILVLVELIQDLLPAGVL----NVVN--GYGVEVGRPL 227
Cdd:cd07080 112 PRGLVVHIIAGNVPLL-PVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVDPNHPLtdsiSVVYwpGGDAELEERI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 228 aTNPRIAKIAFTGSTQVgQLIMQYAteniiPVTLELGGKSPNIFFE--DIMAQDDDYLDKALEGFAM--FALNQgEICTC 303
Cdd:cd07080 191 -LASADAVVAWGGEEAV-KAIRSLL-----PPGCRLIDFGPKYSFAviDREALESEKLAEVADALAEdiCRYDQ-QACSS 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491118422 304 PSRALVQESIA---DRF---LEKAIERVKRIKTGHPLDTETMIG-AQASQEQ 348
Cdd:cd07080 263 PQVVFVEKDDDeelREFaeaLAAALERLPRRYPALSLSAAESAKiARARLEA 314
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
119-252 |
3.24e-03 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 39.73 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118422 119 PLAIDHFRY-FAGCIRAQeggiseidedtiayhfhePLGVVGQIIPWNFPiLMATWKLAPALAAGNCIVLKPAEQTP-AS 196
Cdd:pfam05893 70 PFILDEWLPtKPSYEKAF------------------PPGLVFHVLSGNVP-LLPVMSILMGLLVKNVNLLKVSSSDPfTA 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491118422 197 ILVLVELIqdllpagvlnvvngyGVEVGRPLAtnPRIAKIAF-TGSTQVGQLIMQYA 252
Cdd:pfam05893 131 AALLASFA---------------DLDPTHPLA--DSLSVVYWdGGSTQLEDLIVANA 170
|
|
| |
