|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
9-483 |
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: 806.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 9 YGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHL 88
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIP 248
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 249 ATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSL 328
Cdd:cd07117 241 ATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 329 IYEAQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQA 408
Cdd:cd07117 321 VNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 409 NDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNL 483
Cdd:cd07117 401 NDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
9-483 |
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: 801.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 9 YGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHL 88
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIP 248
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 249 ATLELGGKSANIFFDDA-----NWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDEST 323
Cdd:cd07559 241 VTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 324 QLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDE 403
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 404 VIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNL 483
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-483 |
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: 641.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 6 KERYGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHK 85
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 86 EHLAQVETYDNGKPIRETLnVDIPLGADHFRYFAGVLRAEEGSAQVFD-ENTLSLIIREPIGVVGQVVPWNFPFLMAAWK 164
Cdd:COG1012 83 EELAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 165 LAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAAS 243
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 244 ERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDEST 323
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 324 QLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDE 403
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 404 VIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIP-AGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVN 482
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 740282804 483 L 483
Cdd:COG1012 479 L 479
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
9-479 |
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: 596.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 9 YGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKT--WKTVSQVDRADYLLKIADAIDAHKE 86
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 87 HLAQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLA 166
Cdd:cd07091 84 ELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 167 PALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASER 245
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 246 -LIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQ 324
Cdd:cd07091 244 nLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 325 LGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEV 404
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGS----KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 405 IEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
17-479 |
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: 590.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 17 WVPaSDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDN 96
Cdd:pfam00171 1 WVD-SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 97 GKPIRETLnVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVV 176
Cdd:pfam00171 80 GKPLAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 177 IKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGG 255
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 256 KSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVK 335
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 336 KVLSYVELAKEEGARVVAGGERitdgELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGL 415
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 416 GGGVFTQNLNRAIRVARAIETGRMWVNTYNSI-PAGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGdADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-491 |
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: 573.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 13 INNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAF--KTWKTVSQVDRADYLLKIADAIDAHKEHLAQ 90
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 91 VETYDNGKPIRETlNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALA 170
Cdd:cd07119 82 LETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 171 AGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPA 249
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 250 TLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLI 329
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 330 YEAQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAN 409
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 410 DSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNLSDKPSG 489
Cdd:cd07119 401 DTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSPQPIG 480
|
..
gi 740282804 490 FY 491
Cdd:cd07119 481 WF 482
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
28-481 |
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: 557.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKT--WKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLN 105
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 106 vDIPLGADHFRYFAGVLRAEEGSAQVFDE-NTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTS 184
Cdd:cd07114 81 -QVRYLAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 185 LSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFD 263
Cdd:cd07114 160 ASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 264 DANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVEL 343
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 344 AKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQN 423
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 740282804 424 LNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
9-481 |
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: 544.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 9 YGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHL 88
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIP 248
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 249 ATLELGGKSANIFF------DDANWKQALDGAMLgILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDES 322
Cdd:cd07116 241 VTLELGGKSPNIFFadvmdaDDAFFDKALEGFVM-FALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 323 TQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVdATNDMRVAREEIFGPVAVVIKFHSED 402
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFK-GGNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 403 EVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
57-481 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 543.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLnVDIPLGADHFRYFAGVLRAEEG-SAQVFDEN 135
Cdd:cd07078 9 AAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLHGeVIPSPDPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 136 TLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSG 214
Cdd:cd07078 88 ELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVVTGDGDEVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 215 QYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFV 294
Cdd:cd07078 168 AALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 295 QDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERItdgELGKGCFVRPTLI 374
Cdd:cd07078 248 HESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL---EGGKGYFVPPTVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 375 VDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNS-IPAGAPF 453
Cdd:cd07078 325 TDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPF 404
|
410 420
....*....|....*....|....*...
gi 740282804 454 GGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07078 405 GGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
28-481 |
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: 541.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNVD 107
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSL 187
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 188 LELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDAN 266
Cdd:cd07093 161 WLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 267 WKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKE 346
Cdd:cd07093 241 LDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 347 EGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNR 426
Cdd:cd07093 321 EGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 427 AIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07093 401 AHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
10-483 |
0e+00 |
|
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: 519.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 10 GLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKT-VSQVDRADYLLKIADAIDAHKEHL 88
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSkVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:cd07144 89 AAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLI 247
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 248 PATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKV-KVGLPWDESTQLG 326
Cdd:cd07144 249 AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 327 SLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGeLGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIE 406
Cdd:cd07144 329 PQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEG-LGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740282804 407 QANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNL 483
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
7-490 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 516.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 7 ERYGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKE 86
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 87 HLAQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLA 166
Cdd:PRK13252 85 ELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 167 PALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGsKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASER 245
Cdd:PRK13252 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 246 LIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQL 325
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 326 GSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVI 405
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 406 EQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNLSD 485
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
....*
gi 740282804 486 KPSGF 490
Cdd:PRK13252 484 FQSPF 488
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
30-483 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 515.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 30 NPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNVDIP 109
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 110 LGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLE 189
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 190 LGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWK 268
Cdd:cd07115 163 IAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 269 QALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEG 348
Cdd:cd07115 243 AAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 349 ARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAI 428
Cdd:cd07115 323 ARLLTGGKRPGA----RGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 429 RVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNL 483
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
11-481 |
5.10e-179 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 510.74 E-value: 5.10e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFK---TWKTVSQVDRADYLLKIADAIDAHKEH 87
Cdd:cd07141 9 IFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 88 LAQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAP 167
Cdd:cd07141 89 LASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 168 ALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASE-R 245
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 246 LIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQL 325
Cdd:cd07141 249 LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 326 GSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVI 405
Cdd:cd07141 329 GPQIDEEQFKKILELIESGKKEGAKLECGGKRHGD----KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740282804 406 EQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-484 |
6.58e-178 |
|
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: 507.23 E-value: 6.58e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIrETLNVD 107
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSL 187
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 188 LELGSILQDI-LPPGVVNIVTGKGSkSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDAN 266
Cdd:cd07090 160 LLLAEILTEAgLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 267 WKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKE 346
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 347 EGARVVAGGERIT-DGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLN 425
Cdd:cd07090 319 EGAKVLCGGERVVpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 426 RAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNLS 484
Cdd:cd07090 399 RAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
11-484 |
9.46e-175 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 499.82 E-value: 9.46e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVpASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQ 90
Cdd:PRK13473 5 LLINGELV-AGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 91 VETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQV-FDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPAL 169
Cdd:PRK13473 84 LESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGeYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 170 AAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPA 249
Cdd:PRK13473 164 AAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 250 TLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLI 329
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 330 YEAQVKKVLSYVELAKEEG-ARVVAGGERITdgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQA 408
Cdd:PRK13473 324 SAAHRDRVAGFVERAKALGhIRVVTGGEAPD----GKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740282804 409 NDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNLS 484
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
10-483 |
1.69e-174 |
|
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: 499.36 E-value: 1.69e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 10 GLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKT-W-KTVSQVDRADYLLKIADAIDAHKEH 87
Cdd:cd07143 8 GLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 88 LAQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAP 167
Cdd:cd07143 88 LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 168 ALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASE-R 245
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 246 LIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQL 325
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 326 GSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVI 405
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGGKRHGN----EGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740282804 406 EQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNL 483
Cdd:cd07143 404 KRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
23-479 |
7.10e-174 |
|
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: 497.12 E-value: 7.10e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 23 GAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFK--TWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPI 100
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 101 RETLNVDIPLGADHFRYFAgvlraeEGSAQVFDE------NTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCT 174
Cdd:cd07112 81 SDALAVDVPSAANTFRWYA------EAIDKVYGEvaptgpDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 175 VVIKPSSHTSLSLLELGSI-LQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVG--LDVYKAASErLIPATL 251
Cdd:cd07112 155 VVLKPAEQSPLTALRLAELaLEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGrrFLEYSGQSN-LKRVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 252 ELGGKSANIFFDDA-NWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIY 330
Cdd:cd07112 234 ECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 331 EAQVKKVLSYVELAKEEGARVVAGGERitDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAND 410
Cdd:cd07112 314 EAHFDKVLGYIESGKAEGARLVAGGKR--VLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 411 SLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:cd07112 392 SVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
13-477 |
2.40e-173 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 495.87 E-value: 2.40e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 13 INNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVE 92
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 93 TYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAG 172
Cdd:TIGR01804 82 TLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 173 CTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATL 251
Cdd:TIGR01804 162 NAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 252 ELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYE 331
Cdd:TIGR01804 242 ELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLISA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 332 AQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDS 411
Cdd:TIGR01804 322 AHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDT 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740282804 412 LYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMK 477
Cdd:TIGR01804 402 EYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
28-481 |
1.51e-170 |
|
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: 488.41 E-value: 1.51e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNVD 107
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSL 187
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 188 LELGSILQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANW 267
Cdd:cd07108 161 LLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 268 KQALDGAMLGILFN-QGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKE 346
Cdd:cd07108 241 DDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 347 E-GARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLN 425
Cdd:cd07108 321 TsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 740282804 426 RAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRE-THKVILEHYTQMKNIIV 481
Cdd:cd07108 401 RALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREaSLEGMLEHFTQKKTVNI 457
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-479 |
6.62e-168 |
|
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: 481.55 E-value: 6.62e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLnVD 107
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAG--------VLRAEEGSAQVFdentlslIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKP 179
Cdd:cd07103 80 VDYAASFLEWFAEearriygrTIPSPAPGKRIL-------VIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 180 SSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSA 258
Cdd:cd07103 153 AEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 259 NIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVL 338
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 339 SYVELAKEEGARVVAGGERITDGelgkGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGG 418
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLGLG----GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740282804 419 VFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:cd07103 389 VFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
11-480 |
1.93e-167 |
|
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: 481.22 E-value: 1.93e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFK--TWKTVSQVDRADYLLKIADAIDAHKEHL 88
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:cd07142 86 AALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASE-RL 246
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 247 IPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLG 326
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 327 SLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIE 406
Cdd:cd07142 326 PQVDKEQFEKILSYIEHGKEEGATLITGGDRIGS----KGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740282804 407 QANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNII 480
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-481 |
5.89e-165 |
|
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: 473.74 E-value: 5.89e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNVD 107
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGVLRAEEGSAQV-FDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLS 186
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGeYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 187 LLELGSILQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDAN 266
Cdd:cd07092 161 TLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 267 WKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKe 346
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 347 EGARVVAGGERITdgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNR 426
Cdd:cd07092 320 AHARVLTGGRRAE----GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 427 AIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07092 396 AMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-481 |
4.48e-163 |
|
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: 469.42 E-value: 4.48e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKT--WKTvSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLN 105
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTgdWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 106 VDIPLGADHFRYFAGVLRAEEGS-----AQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPS 180
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEfdlpvPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 181 SHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSAN 259
Cdd:cd07089 160 PDTPLSALLLGEIIAETdLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 260 IFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLS 339
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 340 YVELAKEEGARVVAGGERiTDGeLGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGV 419
Cdd:cd07089 320 YIARGRDEGARLVTGGGR-PAG-LDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740282804 420 FTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
28-480 |
1.65e-162 |
|
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: 467.98 E-value: 1.65e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLnVD 107
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA-WD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGV---LRAEEGSAQVFDENTLSLIIR-EPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHT 183
Cdd:cd07110 80 VDDVAGCFEYYADLaeqLDAKAERAVPLPSEDFKARVRrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 184 SLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFF 262
Cdd:cd07110 160 SLTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 263 DDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVE 342
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 343 LAKEEGARVVAGGERitDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQ 422
Cdd:cd07110 320 RGKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 740282804 423 NLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNII 480
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
11-480 |
1.24e-161 |
|
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: 465.82 E-value: 1.24e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQ 90
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 91 VETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEgsaqvFDE---NtlSLIIREPIGVVGQVVPWNFPFLMAAWKLAP 167
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDFE-----FEErrgN--SLVVREPIGVCGLITPWNWPLNQIVLKVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 168 ALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERL 246
Cdd:cd07138 154 ALAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 247 IPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLG 326
Cdd:cd07138 234 KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 327 SLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGeLGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIE 406
Cdd:cd07138 314 PLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEG-LERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740282804 407 QANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNtYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNII 480
Cdd:cd07138 393 IANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
11-481 |
1.30e-161 |
|
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: 466.28 E-value: 1.30e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAF--KTWKTVSQVDRADYLLKIADAIDAHKEHL 88
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRA---EEGSAQVFDENTLslIIREPIGVVGQVVPWNFPFLMAAWKL 165
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGHVL--VRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 166 APALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGkGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASE 244
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 245 RLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQ 324
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 325 LGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgeLGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEV 404
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAG--LDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740282804 405 IEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYnSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
31-479 |
1.34e-158 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 457.95 E-value: 1.34e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 31 PANGEQLAVCAEATQADVDKAVAAATEAFKT--WKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNvDI 108
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 109 PLGADHFRYFAGVLRAEEG-SAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSL 187
Cdd:cd07118 83 EGAADLWRYAASLARTLHGdSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 188 LELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDAN 266
Cdd:cd07118 163 LMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 267 WKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKE 346
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 347 EGARVVAGGERItdgELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNR 426
Cdd:cd07118 323 EGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 740282804 427 AIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-473 |
1.09e-152 |
|
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: 443.76 E-value: 1.09e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 5 IKERYGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAH 84
Cdd:cd07111 18 HDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 85 KEHLAQVETYDNGKPIRETLNVDIPLGADHFRYFAgvlraeeGSAQVFDEntlSLIIREPIGVVGQVVPWNFPFLMAAWK 164
Cdd:cd07111 98 QRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHA-------GWAQLLDT---ELAGWKPVGVVGQIVPWNFPLLMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 165 LAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSkSGQYILDHPGFSKLAFTGSTEVGLDVYKAAS 243
Cdd:cd07111 168 ICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 244 ERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDEST 323
Cdd:cd07111 247 GTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 324 QLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDE 403
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPS----KGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 404 VIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHY 473
Cdd:cd07111 403 AVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
1-491 |
7.52e-152 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 442.63 E-value: 7.52e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 1 MSLHIKERyGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAF-----KTWKTVSQVDRADYLL 75
Cdd:PLN02467 1 MAIPVPRR-QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 76 KIADAIDAHKEHLAQVETYDNGKPIRETLnVDIPLGADHFRYFAGvlRAEEGSAQ------VFDENTLSLIIREPIGVVG 149
Cdd:PLN02467 80 AIAAKITERKSELAKLETLDCGKPLDEAA-WDMDDVAGCFEYYAD--LAEALDAKqkapvsLPMETFKGYVLKEPLGVVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 150 QVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAF 228
Cdd:PLN02467 157 LITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAPLASHPGVDKIAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 229 TGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSK 308
Cdd:PLN02467 237 TGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 309 LFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERitDGELGKGCFVRPTLIVDATNDMRVAREEI 388
Cdd:PLN02467 317 WAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 389 FGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKV 468
Cdd:PLN02467 395 FGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEW 474
|
490 500
....*....|....*....|...
gi 740282804 469 ILEHYTQMKNIIVNLSDKPSGFY 491
Cdd:PLN02467 475 GLENYLSVKQVTKYISDEPWGWY 497
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-479 |
1.38e-151 |
|
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: 439.66 E-value: 1.38e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETlNVD 107
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGVLRAEEgsAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSL 187
Cdd:cd07106 80 VGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 188 LELGSILQDILPPGVVNIVTGkGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANW 267
Cdd:cd07106 158 LKLGELAQEVLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 268 KQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEE 347
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 348 GARVVAGGERitdgELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRA 427
Cdd:cd07106 317 GAKVLAGGEP----LDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 740282804 428 IRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
28-481 |
2.91e-150 |
|
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: 436.67 E-value: 2.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKT-WKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNv 106
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 107 DIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLS 186
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 187 LLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDA 265
Cdd:cd07109 160 ALRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 266 NWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGlPWDESTQLGSLIYEAQVKKVLSYVELAK 345
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 346 EEGARVVAGGeRITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLN 425
Cdd:cd07109 319 ARGARIVAGG-RIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 426 RAIRVARAIETGRMWVNTYNsiPAGA---PFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYG--AGGGielPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
57-481 |
4.66e-149 |
|
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: 430.11 E-value: 4.66e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLnVDIPLGADHFRYFAGVLRAEEGSAQVF-DEN 135
Cdd:cd06534 5 AAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPSpDPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 136 TLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSG 214
Cdd:cd06534 84 GEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGGDEVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 215 QYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFV 294
Cdd:cd06534 164 AALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 295 QDTIYDKFVAELSklfdkvkvglpwdestqlgsliyeaqvkkvlsyvelakeegarvvaggeritdgelgkgcfvrpTLI 374
Cdd:cd06534 244 HESIYDEFVEKLV----------------------------------------------------------------TVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 375 VDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNS-IPAGAPF 453
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPF 339
|
410 420
....*....|....*....|....*...
gi 740282804 454 GGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd06534 340 GGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
11-485 |
1.22e-146 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 430.38 E-value: 1.22e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKT--WKTVSQVDRADYLLKIADAIDAHKEHL 88
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYK-AASERL 246
Cdd:PLN02466 220 LACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLElAAKSNL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 247 IPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLG 326
Cdd:PLN02466 300 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 327 SLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIE 406
Cdd:PLN02466 380 PQIDSEQFEKILRYIKSGVESGATLECGGDRFGS----KGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 407 QANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNLSD 485
Cdd:PLN02466 456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPLKN 534
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-481 |
6.58e-146 |
|
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: 425.91 E-value: 6.58e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 13 INNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVE 92
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 93 TYDNGKPIRETlNVDIPLGADHFRYFAGVLRAEEGSAQVFD-ENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAA 171
Cdd:cd07088 82 VEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 172 GCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPAT 250
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 251 LELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIY 330
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 331 EAQVKKVLSYVELAKEEGARVVAGGERItdgELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAND 410
Cdd:cd07088 321 EAALDKVEEMVERAVEAGATLLTGGKRP---EGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740282804 411 SLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
11-487 |
2.62e-145 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 425.77 E-value: 2.62e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFK--TWKTVSQVDRADYLLKIADAIDAHKEHL 88
Cdd:PLN02766 23 LFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:PLN02766 103 AALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASE-RL 246
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 247 IPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLG 326
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 327 SLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIE 406
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGGKPCGD----KGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 407 QANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNLSDK 486
Cdd:PLN02766 419 KANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPLYNS 498
|
.
gi 740282804 487 P 487
Cdd:PLN02766 499 P 499
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-477 |
2.38e-143 |
|
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: 419.73 E-value: 2.38e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 12 LINNEWVPASDGAEfnVYNPAN-GEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQ 90
Cdd:cd07097 4 YIDGEWVAGGDGEE--NRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 91 VETYDNGKPIRETLNvDIPLGADHFRYFAG-VLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPAL 169
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGeALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 170 AAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIP 248
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 249 ATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSL 328
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 329 IYEAQVKKVLSYVELAKEEGARVVAGGERITDGElgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQA 408
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYGGERLKRPD--EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 409 NDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNtynsIP-AG----APFGGYKQSGIG-RETHKVILEHYTQMK 477
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN----LPtAGvdyhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
28-483 |
2.82e-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: 413.69 E-value: 2.82e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNvD 107
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSL 187
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 188 LELGSILQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANW 267
Cdd:cd07107 160 LRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 268 KQALDGAMLGILFN-QGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKE 346
Cdd:cd07107 240 EAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 347 EGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNR 426
Cdd:cd07107 320 EGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQ 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 740282804 427 AIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVNL 483
Cdd:cd07107 400 AHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-484 |
4.97e-139 |
|
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: 409.04 E-value: 4.97e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 12 LINNEWVPASDGAEFNVYNPANGEQL-AVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQ 90
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 91 VETYDNGKPIRETLNvDIPLGADHFRYFAGVLRAEEGSAqVFDE--NTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:cd07131 82 LVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGET-VPSElpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLI 247
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 248 PATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGS 327
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 328 LIYEAQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQ 407
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 408 ANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTyNSIPAGA--PFGGYKQSGIG-RETHKVILEHYTQMKNIIVNLS 484
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNA-PTIGAEVhlPFGGVKKSGNGhREAGTTALDAFTEWKAVYVDYS 478
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
12-482 |
7.11e-137 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 404.07 E-value: 7.11e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 12 LINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQV 91
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 92 ETYDNGKPIRETLNvDIPLGADHFRYFAgvlraEEGSaQVFDE-------NTLSLIIREPIGVVGQVVPWNFPFLMAAWK 164
Cdd:PLN02278 108 MTLEQGKPLKEAIG-EVAYGASFLEYFA-----EEAK-RVYGDiipspfpDRRLLVLKQPVGVVGAITPWNFPLAMITRK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 165 LAPALAAGCTVVIKPSSHTSLSLLELGSI-LQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAAS 243
Cdd:PLN02278 181 VGPALAAGCTVVVKPSELTPLTALAAAELaLQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 244 ERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDEST 323
Cdd:PLN02278 261 ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 324 QLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGelgkGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDE 403
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLG----GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 404 VIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVN 482
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLG 495
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
29-479 |
3.99e-135 |
|
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: 398.26 E-value: 3.99e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 29 YNPANGEQLAVCAEATQADVDKAVAAATEAFK--TWKTVSQVdRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETlNV 106
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEA-RF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 107 DIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLS 186
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 187 LLELGSILQDI--LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDD 264
Cdd:cd07120 160 NAAIIRILAEIpsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 265 ANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELA 344
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 345 KEEGARVVAGGERITDGeLGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNL 424
Cdd:cd07120 320 IAAGAEVVLRGGPVTEG-LAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 740282804 425 NRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGReTHKV-ILEHYTQMKNI 479
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGR-LHGVaALEDFIEYKHI 453
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
10-481 |
7.04e-134 |
|
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: 395.66 E-value: 7.04e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 10 GLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKT-WKTVSQVDRADYLLKIADAIDAHKEHL 88
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 89 AQVETYDNGKPIRETLNVDIPLGADHFRYFAGVlrAEEGSAQVFD--------ENTLSLIIREPIGVVGQVVPWNFPFLM 160
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGW--ATKINGETLApsipsmqgERYTAFTRREPVGVVAGIVPWNFSVMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 161 AAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSkSGQYILDHPGFSKLAFTGSTEVGLDVY 239
Cdd:cd07113 159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 240 KAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPW 319
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 320 DESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITdgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFH 399
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA----GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 400 SEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
..
gi 740282804 480 IV 481
Cdd:cd07113 474 MI 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-481 |
7.59e-133 |
|
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: 392.48 E-value: 7.59e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 26 FNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETlN 105
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 106 VDIPLGADHFRYFAGVLRAEEGS-----AQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPS 180
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGEtipvdAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 181 SHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSAN 259
Cdd:cd07145 160 SNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 260 IFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLS 339
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 340 YVELAKEEGARVVAGGERItdgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGV 419
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRD------EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740282804 420 FTQNLNRAIRVARAIETGRMWVNTYNSIPAGA-PFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
2-483 |
5.55e-132 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 391.57 E-value: 5.55e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 2 SLHIKERygLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKT--WKTVSQVDRADYLLKIAD 79
Cdd:PRK09847 15 SLAIENR--LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 80 AIDAHKEHLAQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFL 159
Cdd:PRK09847 93 LMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 160 MAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDV 238
Cdd:PRK09847 173 LTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 239 YKAASERLIPAT-LELGGKSANIFFDDA-NWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVG 316
Cdd:PRK09847 253 LKDAGDSNMKRVwLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 317 LPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERitdgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVI 396
Cdd:PRK09847 333 HPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA------GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 397 KFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQM 476
Cdd:PRK09847 407 RFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTEL 486
|
....*..
gi 740282804 477 KNIIVNL 483
Cdd:PRK09847 487 KTIWISL 493
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
5-481 |
1.51e-131 |
|
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: 389.93 E-value: 1.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 5 IKERYGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKT--WKTVSQVDRADYLLKIADAID 82
Cdd:cd07140 2 LKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 83 AHKEHLAQVETYDNGKPIRETLNVDIPLGADHFRYFAGVLRAEEGSA----QVFDENTLSLIIREPIGVVGQVVPWNFPF 158
Cdd:cd07140 82 EHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTipinQARPNRNLTLTKREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 159 LMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSI-LQDILPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLD 237
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 238 VYK-AASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVG 316
Cdd:cd07140 242 IMKsCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 317 LPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVI 396
Cdd:cd07140 322 DPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR----PGFFFEPTVFTDVEDHMFIAKEESFGPIMIIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 397 KFHSED--EVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYT 474
Cdd:cd07140 398 KFDDGDvdGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYL 477
|
....*..
gi 740282804 475 QMKNIIV 481
Cdd:cd07140 478 KTKTVTI 484
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
28-477 |
7.86e-125 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 371.38 E-value: 7.86e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNvD 107
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKG-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAgvlraEEGSaQVFDENTLS-------LIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPS 180
Cdd:TIGR01780 80 ILYAASFLEWFA-----EEAK-RVYGDTIPSpqsdkrlIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 181 SHTSLSLLELGSILQDI-LPPGVVNIVTG-KGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSA 258
Cdd:TIGR01780 154 EQTPLSALALARLAEQAgIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 259 NIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVL 338
Cdd:TIGR01780 234 FIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 339 SYVELAKEEGARVVAGGERitdGELGkGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGG 418
Cdd:TIGR01780 314 KHIADAVEKGAKVVTGGKR---HELG-GNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAY 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 419 VFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMK 477
Cdd:TIGR01780 390 FFSRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
57-481 |
9.36e-124 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 368.01 E-value: 9.36e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVEtydngkpIRET------LNVDIPLGADHFRYFAGVLRAEEG--- 127
Cdd:cd07104 11 AAQKAWAATPPQERAAILRKAAEILEERRDEIADWL-------IRESgstrpkAAFEVGAAIAILREAAGLPRRPEGeil 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 128 -SAQvfdENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSL-LELGSILQDI-LPPGVVN 204
Cdd:cd07104 84 pSDV---PGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAgLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 205 IVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQ 284
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 285 VCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERitdgelg 364
Cdd:cd07104 241 ICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 365 KGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN-- 442
Cdd:cd07104 314 EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdq 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 740282804 443 TYNSIPAgAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07104 394 TVNDEPH-VPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-484 |
1.32e-123 |
|
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: 369.59 E-value: 1.32e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 12 LINNEWVpASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQV 91
Cdd:cd07086 2 VIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 92 ETYDNGKPIRETLN-----VDIplgADhfrYFAGVLRAEEGsaQVFDE---NTLSLIIREPIGVVGQVVPWNFPFLMAAW 163
Cdd:cd07086 81 VSLEMGKILPEGLGevqemIDI---CD---YAVGLSRMLYG--LTIPSerpGHRLMEQWNPLGVVGVITAFNFPVAVPGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 164 KLAPALAAGCTVVIKPSSHTSLSLLELGSILQDIL-----PPGVVNIVTGkGSKSGQYILDHPGFSKLAFTGSTEVGLDV 238
Cdd:cd07086 153 NAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLeknglPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 239 YKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLP 318
Cdd:cd07086 232 GETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 319 WDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGElgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKF 398
Cdd:cd07086 312 LDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGE--PGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 399 HSEDEVIEQANDSLYGLGGGVFTQNLNRAIRV--ARAIETGRMWVNtynsIP-----AGAPFGGYKQSGIGRETHKVILE 471
Cdd:cd07086 390 DSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVN----IPtsgaeIGGAFGGEKETGGGRESGSDAWK 465
|
490
....*....|...
gi 740282804 472 HYTQMKNIIVNLS 484
Cdd:cd07086 466 QYMRRSTCTINYS 478
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
28-481 |
8.50e-122 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 363.84 E-value: 8.50e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLN-V 106
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKeV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 107 D-----IPLGADHFRYFAGV---LRAEEGSaqvfdENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIK 178
Cdd:cd07149 83 DraietLRLSAEEAKRLAGEtipFDASPGG-----EGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 179 PSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERliPATLELGGKS 257
Cdd:cd07149 158 PASQTPLSALKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 258 ANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKV 337
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 338 LSYVELAKEEGARVVAGGERItdgelgkGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGG 417
Cdd:cd07149 316 EEWVEEAVEGGARLLTGGKRD-------GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 418 GVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGA-PFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07149 389 GVFTNDLQKALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
29-463 |
8.97e-120 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 358.84 E-value: 8.97e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 29 YNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLnVDI 108
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 109 PLGADHFRYFAG----VLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTS 184
Cdd:cd07099 80 LLALEAIDWAARnaprVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 185 LSLLELGSILQDILPP-GVVNIVTGKGSkSGQYILDHpGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFD 263
Cdd:cd07099 160 LVGELLAEAWAAAGPPqGVLQVVTGDGA-TGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 264 DANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVEL 343
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 344 AKEEGARVVAGGERITdgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQN 423
Cdd:cd07099 318 AVAKGAKALTGGARSN----GGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 740282804 424 LNRAIRVARAIETGRMWVN--TYNSIPAGAPFGGYKQSGIGR 463
Cdd:cd07099 394 LARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGR 435
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-481 |
1.20e-117 |
|
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: 353.17 E-value: 1.20e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 26 FNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLn 105
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 106 VDIPLGADHFRYFAGVLRAEEGSAQVFD-ENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTS 184
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPSDsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 185 LSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFD 263
Cdd:cd07150 160 VIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 264 DANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVEL 343
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 344 AKEEGARVVAGGERitdgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQN 423
Cdd:cd07150 320 AVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 424 LNRAIRVARAIETGRMWVN--TYNSiPAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07150 393 LQRAFKLAERLESGMVHINdpTILD-EAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
57-464 |
2.37e-116 |
|
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: 349.07 E-value: 2.37e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNvDIPLGADHFRYFAgvlraEEGSAQVFDE-- 134
Cdd:cd07100 10 AAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYA-----ENAEAFLADEpi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 135 ---NTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKG 210
Cdd:cd07100 84 etdAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPEGVFQNLLIDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 211 SKSGQyILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGS 290
Cdd:cd07100 164 DQVEA-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 291 RIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITdgelGKGCFVR 370
Cdd:cd07100 243 RFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD----GPGAFYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 371 PTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAG 450
Cdd:cd07100 319 PTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPR 398
|
410
....*....|....
gi 740282804 451 APFGGYKQSGIGRE 464
Cdd:cd07100 399 LPFGGVKRSGYGRE 412
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
9-482 |
4.11e-116 |
|
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: 351.52 E-value: 4.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 9 YGLLINNEWVPASDgaEFNVYNPAN-GEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEH 87
Cdd:cd07124 33 YPLVIGGKEVRTEE--KIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 88 LAQVETYDNGKPIRETLnVDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAP 167
Cdd:cd07124 111 LAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 168 ALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASER- 245
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 246 -----LIPATLELGGKSANIFFDDANwkqaLDGAMLGIL---FN-QGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVG 316
Cdd:cd07124 270 pgqkwLKRVIAEMGGKNAIIVDEDAD----LDEAAEGIVrsaFGfQGQKCSACSRVIVHESVYDEFLERLVERTKALKVG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 317 LPWDESTQLGSLIYEAQVKKVLSYVELAKEEGaRVVAGGERitDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVI 396
Cdd:cd07124 346 DPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEV--LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 397 KFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN--TYNSIPAGAPFGGYKQSGIGRETHKV-ILEHY 473
Cdd:cd07124 423 KAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTGSKAGGPdYLLQF 502
|
....*....
gi 740282804 474 TQMKNIIVN 482
Cdd:cd07124 503 MQPKTVTEN 511
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
15-481 |
2.48e-114 |
|
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: 345.06 E-value: 2.48e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 15 NEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLaqVETY 94
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEI--VEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 95 dngkpIRET----LNVDIPLGADH--FRYFAGVLRAEEGSAQVFD-ENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAP 167
Cdd:cd07151 79 -----IRESgstrIKANIEWGAAMaiTREAATFPLRMEGRILPSDvPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 168 ALAAGCTVVIKPSSHTSLS--LLeLGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASE 244
Cdd:cd07151 154 ALALGNAVVLKPASDTPITggLL-LAKIFEEAgLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 245 RLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQ 324
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 325 LGSLIYEAQVKKVLSYVELAKEEGARVVAGGERitdgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEV 404
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEA 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 405 IEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN--TYNSIPaGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07151 386 LELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDEP-HVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-482 |
8.26e-114 |
|
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: 344.17 E-value: 8.26e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 12 LINNEWVpASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFK-TWKTVSQVDRADYLLKIADAIDAHKEHLAQ 90
Cdd:cd07082 5 LINGEWK-ESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRgWWPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 91 VETYDNGKPIRETL-NVDipLGADHFRYFAGVLRAEEGSAQVFDE-----NTLSLIIREPIGVVGQVVPWNFPFLMAAWK 164
Cdd:cd07082 84 LLMWEIGKTLKDALkEVD--RTIDYIRDTIEELKRLDGDSLPGDWfpgtkGKIAQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 165 LAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAAS 243
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 244 erLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDEST 323
Cdd:cd07082 242 --MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 324 QLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITdgelgkGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDE 403
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG------GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 404 VIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSI-PAGAPFGGYKQSGIGRETHKVILEHYTQMKNIIVN 482
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRgPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-481 |
1.76e-107 |
|
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: 326.46 E-value: 1.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPiRETLNVDIPLGADHFRYFAGVL-RAEEGSAQVFDEN 135
Cdd:cd07105 11 AAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLItQIIGGSIPSDKPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 136 TLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSG 214
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLNVVTHSPEDAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 215 QYI---LDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSR 291
Cdd:cd07105 170 EVVealIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 292 IFVQDTIYDKFVAELSKLFDKVKVGlpwdeSTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGeriTDGELGKGCFVRP 371
Cdd:cd07105 250 IIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGG---LADESPSGTSMPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 372 TLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNT---YNSip 448
Cdd:cd07105 322 TILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGmtvHDE-- 399
|
410 420 430
....*....|....*....|....*....|...
gi 740282804 449 AGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07105 400 PTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-481 |
1.76e-104 |
|
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: 319.38 E-value: 1.76e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLnVD 107
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-VE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGVLRAEEG-----SAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSH 182
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGeeiplDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 183 TSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIpaTLELGGKSANIF 261
Cdd:cd07094 162 TPLSALELAKILVEAgVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRI--ALELGGNAPVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 262 FDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYV 341
Cdd:cd07094 240 DRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 342 ELAKEEGARVVAGGERitdgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFT 421
Cdd:cd07094 320 EEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740282804 422 QNLNRAIRVARAIETGRMWVNTYNSIPAGA-PFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
8-483 |
5.01e-104 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 319.54 E-value: 5.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 8 RYGLLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEH 87
Cdd:PRK11241 10 RQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 88 LAQVETYDNGKPIRETLNvDIPLGADHFRYFAgvlraEEGSAQVFD------ENTLSLIIREPIGVVGQVVPWNFPFLMA 161
Cdd:PRK11241 90 LARLMTLEQGKPLAEAKG-EISYAASFIEWFA-----EEGKRIYGDtipghqADKRLIVIKQPIGVTAAITPWNFPAAMI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 162 AWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYK 240
Cdd:PRK11241 164 TRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLME 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 241 AASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWD 320
Cdd:PRK11241 244 QCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 321 ESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGelgkGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHS 400
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG----GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 401 EDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNII 480
Cdd:PRK11241 400 EADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMC 479
|
...
gi 740282804 481 VNL 483
Cdd:PRK11241 480 IGL 482
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
18-479 |
3.05e-102 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 316.05 E-value: 3.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 18 VPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLA---QVETy 94
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLdlvQLET- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 95 dnGKPIR----ETLnvDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALA 170
Cdd:PRK09407 105 --GKARRhafeEVL--DVALTARYYARRAPKLLAPRRRAGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 171 AGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFskLAFTGSTEVGLDVYKAASERLIPA 249
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 250 TLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLI 329
Cdd:PRK09407 259 SLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 330 YEAQVKKVLSYVELAKEEGARVVAGGERITDgeLGKgCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAN 409
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVLAGGKARPD--LGP-LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 410 DSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN-----TYNSIpaGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:PRK09407 416 DTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSV--DAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
28-481 |
4.36e-99 |
|
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: 305.71 E-value: 4.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 28 VYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETlNVD 107
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 108 IPLGADHFRYFAGVLRAEEGSAQVFD-----ENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSH 182
Cdd:cd07147 82 VARAIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 183 TSLSLLELGSIL-QDILPPGVVNIVTGKgSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERliPATLELGGKSANIF 261
Cdd:cd07147 162 TPLSALILGEVLaETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 262 FDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYV 341
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 342 ELAKEEGARVVAGGERitdgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFT 421
Cdd:cd07147 319 NEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740282804 422 QNLNRAIRVARAIETGRMWVntyNSIPA----GAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07147 392 RDLEKALRAWDELEVGGVVI---NDVPTfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
31-481 |
1.83e-98 |
|
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: 304.23 E-value: 1.83e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 31 PANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIR----ETLnv 106
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRhafeEVL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 107 DIPLGADHFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLS 186
Cdd:cd07101 81 DVAIVARYYARRAERLLKPRRRRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 187 LLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFskLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDA 265
Cdd:cd07101 161 ALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 266 NWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAK 345
Cdd:cd07101 239 DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 346 EEGARVVAGGERITDgeLGKgCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLN 425
Cdd:cd07101 319 AKGATVLAGGRARPD--LGP-YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740282804 426 RAIRVARAIETGRMWVN-----TYNSIpaGAPFGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07101 396 RGRRIAARLRAGTVNVNegyaaAWASI--DAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
74-477 |
1.93e-98 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 302.43 E-value: 1.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 74 LLKIADAIDAHKEHLAQVETYDNGKpIRETLNVDIPLGADHFRYFAGVLRAEEGS-AQVFDENTLSLIIREPIGVVGQVV 152
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK-IQQLAEVEVAFTADYIDYMAEWARRYEGEiIQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 153 PWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGS 231
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 232 TEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFD 311
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 312 KVKVGLPWDEST-QLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITdgelGKGCFVRPTLIVDATNDMRVAREEIFG 390
Cdd:PRK10090 240 AVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 391 PVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVIL 470
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGL 395
|
....*..
gi 740282804 471 EHYTQMK 477
Cdd:PRK10090 396 HEYLQTQ 402
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
29-463 |
1.81e-97 |
|
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: 301.91 E-value: 1.81e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 29 YNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPiretlNVDI 108
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKT-----MVDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 109 PLG-----ADHFRYFAG----VLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKP 179
Cdd:cd07098 76 SLGeilvtCEKIRWTLKhgekALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 180 SSHTSLSLLELGSILQDIL-----PPGVVNIVTGKGsKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELG 254
Cdd:cd07098 156 SEQVAWSSGFFLSIIRECLaacghDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 255 GKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQV 334
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 335 KKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYG 414
Cdd:cd07098 315 DRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 740282804 415 LGGGVFTQNLNRAIRVARAIETGRMWVNTY--NSIPAGAPFGGYKQSGIGR 463
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGR 445
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
9-460 |
6.34e-97 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 301.85 E-value: 6.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 9 YGLLINNEWVPASDgaEFNVYNPAN-GEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEH 87
Cdd:PRK03137 37 YPLIIGGERITTED--KIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 88 LAQVETYDNGKPIRETlNVDIPLGADHFRYFA-GVLRAEEGSAQVF---DENTLSLIirePIGVVGQVVPWNFPFLMAAW 163
Cdd:PRK03137 115 FSAWLVKEAGKPWAEA-DADTAEAIDFLEYYArQMLKLADGKPVESrpgEHNRYFYI---PLGVGVVISPWNFPFAIMAG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 164 KLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAA 242
Cdd:PRK03137 191 MTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 243 S---------ERLIpatLELGGKSANIFFDDANwkqaLDGAMLGILFN----QGQVCCAGSRIFVQDTIYDKFVAELSKL 309
Cdd:PRK03137 271 AkvqpgqiwlKRVI---AEMGGKDAIVVDEDAD----LDLAAESIVASafgfSGQKCSACSRAIVHEDVYDEVLEKVVEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 310 FDKVKVGLPwDESTQLGSLIYEAQVKKVLSYVELAKEEGaRVVAGGEritdGELGKGCFVRPTLIVDATNDMRVAREEIF 389
Cdd:PRK03137 344 TKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGE----GDDSKGYFIQPTIFADVDPKARIMQEEIF 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740282804 390 GPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN---TynsipaGA-----PFGGYKQSG 460
Cdd:PRK03137 418 GPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcT------GAivgyhPFGGFNMSG 490
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
29-479 |
1.42e-96 |
|
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: 299.16 E-value: 1.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 29 YNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNvDI 108
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 109 PLGADHFRYFAGVlrAEEGSAQVFDENTLSL---IIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSL 185
Cdd:cd07102 80 RGMLERARYMISI--AEEALADIRVPEKDGFeryIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 186 SLLELGSILQDI-LPPGVVNIVTGKGSKSGQyILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDD 264
Cdd:cd07102 158 CGERFAAAFAEAgLPEGVFQVLHLSHETSAA-LIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 265 ANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELA 344
Cdd:cd07102 237 ADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 345 KEEGARVVAGGERITDGELGkGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNL 424
Cdd:cd07102 317 IAKGARALIDGALFPEDKAG-GAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 425 NRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGRETHKVILEHYTQMKNI 479
Cdd:cd07102 396 ARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
11-481 |
6.76e-93 |
|
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: 290.57 E-value: 6.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQ 90
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 91 VETYDNGKPIRETL--------NVDIPLGADHfryfagVLRAE--EGSAQVFDENTlsliIREPIGVVGQVVPWNFPFLM 160
Cdd:cd07085 83 LITLEHGKTLADARgdvlrgleVVEFACSIPH------LLKGEylENVARGIDTYS----YRQPLGVVAGITPFNFPAMI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 161 AAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGkGSKSGQYILDHPGFSKLAFTGSTEVGLDVY 239
Cdd:cd07085 153 PLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 240 KAASERLIPATLELGGKSANIFFDDANWKQALD---GAMLGilfNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVG 316
Cdd:cd07085 232 ERAAANGKRVQALGGAKNHAVVMPDADLEQTANalvGAAFG---AAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 317 LPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVI 396
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 397 KFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNtynsIPAGAP-----FGGYKQSGIGrETH---KV 468
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLHfygKD 463
|
490
....*....|...
gi 740282804 469 ILEHYTQMKNIIV 481
Cdd:cd07085 464 GVRFYTQTKTVTS 476
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
34-462 |
1.37e-86 |
|
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: 273.02 E-value: 1.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 34 GEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKpIRETLNVDIPLGAD 113
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 114 HFRYFAGVLRAEEGSAQVFDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSL-LELGS 192
Cdd:cd07152 80 ELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 193 ILQDI-LPPGVVNIVTGkGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQAL 271
Cdd:cd07152 160 LFEEAgLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 272 DGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARV 351
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 352 VAGGERitdgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVA 431
Cdd:cd07152 319 EAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430
....*....|....*....|....*....|...
gi 740282804 432 RAIETGRMWVN--TYNSIPAgAPFGGYKQSGIG 462
Cdd:cd07152 392 DRLRTGMLHINdqTVNDEPH-NPFGGMGASGNG 423
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
63-481 |
6.46e-86 |
|
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: 271.54 E-value: 6.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 63 KTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLnVDIPLGADHFRYFAGVLRAEEGSAQVFDENT-----L 137
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVGRAADVLRFAAAEALRDDGESFSCDLTAngkarK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 138 SLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQY 216
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 217 ILDHPGFSKLAFTGSTEVGLDVykAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQD 296
Cdd:cd07146 194 LITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 297 TIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERitdgelgKGCFVRPTLIVD 376
Cdd:cd07146 272 SVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDH 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 377 ATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVntyNSIPA----GAP 452
Cdd:cd07146 345 VPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNV---NEVPGfrseLSP 421
|
410 420 430
....*....|....*....|....*....|
gi 740282804 453 FGGYKQSGIG-RETHKVILEHYTQMKNIIV 481
Cdd:cd07146 422 FGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
9-462 |
3.51e-82 |
|
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: 263.65 E-value: 3.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 9 YGLLINNEWVPASdgAEFNVYNPANGEQ-LAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEH 87
Cdd:TIGR01237 33 YPLVINGERVETE--NKIVSINPCDKSEvVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 88 LAQVETYDNGKPIRETlNVDIPLGADHFRYFAGVLRAEEGSAQVFD-ENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLA 166
Cdd:TIGR01237 111 FSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGKPVNSrEGETNQYVYTPTGVTVVISPWNFPFAIMVGMTV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 167 PALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAAS-- 243
Cdd:TIGR01237 190 APIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkv 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 244 -------ERLIpatLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVG 316
Cdd:TIGR01237 270 qpgqkhlKRVI---AEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 317 LPWDESTQLGSLIYEAQVKKVLSYVELAKEEGaRVVAGGEritdGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVI 396
Cdd:TIGR01237 347 PPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGC----GDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFI 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740282804 397 KFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN--TYNSIPAGAPFGGYKQSGIG 462
Cdd:TIGR01237 422 RASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTD 489
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
14-464 |
2.16e-81 |
|
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: 260.60 E-value: 2.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 14 NNEWVPAsdGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVET 93
Cdd:cd07130 4 DGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 94 YDNGKPIRETLN-----VDIplgADHF----RYFAGVLRAEEGSAQVFDENTlsliirEPIGVVGQVVPWNFPFLMAAWK 164
Cdd:cd07130 82 LEMGKILPEGLGevqemIDI---CDFAvglsRQLYGLTIPSERPGHRMMEQW------NPLGVVGVITAFNFPVAVWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 165 LAPALAAGCTVVIKPSSHTSLSLLELGSILQDIL-----PPGVVNIVTGkGSKSGQYILDHPGFSKLAFTGSTEVGLDVY 239
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLeknglPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 240 KAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPW 319
Cdd:cd07130 232 QAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 320 DESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITdgelGKGCFVRPTlIVDATNDMRVAREEIFGPVAVVIKFH 399
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVID----GPGNYVEPT-IVEGLSDAPIVKEETFAPILYVLKFD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 400 SEDEVIEQANDSLYGLGGGVFTQNLNRAIRV--ARAIETGRMWVNTYNS---IpaGAPFGGYKQSGIGRE 464
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIGTSgaeI--GGAFGGEKETGGGRE 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
7-465 |
7.21e-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: 231.31 E-value: 7.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 7 ERYGLLINNEWVPASDgAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKE 86
Cdd:cd07083 17 RAYPLVIGGEWVDTKE-RMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 87 HLAQVETYDNGKPIRETLNvDIPLGADHFRYFAGVLRAEEGSAQVFDENTLSL--IIREPIGVVGQVVPWNFPFLMAAWK 164
Cdd:cd07083 96 ELIATLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDneSFYVGLGAGVVISPWNFPVAIFTGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 165 LAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAAS 243
Cdd:cd07083 175 IVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 244 ERL------IPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGL 317
Cdd:cd07083 255 RLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 318 PWDESTQLGSLIYEAQVKKVLSYVELAKEEGaRVVAGGERITdgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIK 397
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE----GEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740282804 398 FHSED--EVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN--TYNSIPAGAPFGGYKQSGIGRET 465
Cdd:cd07083 410 YKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNAKT 481
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
9-488 |
2.26e-69 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 229.64 E-value: 2.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 9 YGLLINNEWVPASDGAEFNVYNPANGE-QLAVCAeATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEH 87
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKtQYKVQA-CTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 88 LAQVETYDNGKPIRETLnVDIPLGADHFRYFA--GVLRAEEGSAQVFD------ENTLSLIIREPIGVVGQVVPWNFPFL 159
Cdd:PLN00412 95 IAECLVKEIAKPAKDAV-TEVVRSGDLISYTAeeGVRILGEGKFLVSDsfpgneRNKYCLTSKIPLGVVLAIPPFNYPVN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 160 MAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGStEVGLDV 238
Cdd:PLN00412 174 LAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 239 YKAAseRLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLP 318
Cdd:PLN00412 253 SKKA--GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 319 WDEStQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERitdgelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKF 398
Cdd:PLN00412 331 EDDC-DITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 399 HSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVntyNSIPAGA----PFGGYKQSGIGRETHKVILEHYT 474
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQI---NSAPARGpdhfPFQGLKDSGIGSQGITNSINMMT 479
|
490
....*....|....
gi 740282804 475 QMKNIIVNLSdKPS 488
Cdd:PLN00412 480 KVKSTVINLP-KPS 492
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
30-464 |
1.37e-68 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 226.54 E-value: 1.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 30 NPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIR----ETLN 105
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLAsakaEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 106 VdiplgADHFRYFAG---VLRAEEgSAQVFDENTLSLIIR-EPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSS 181
Cdd:PRK09406 87 C-----AKGFRYYAEhaeALLADE-PADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 182 HTSLSLLELGSILQDI-LPPGVVNIVTgKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANI 260
Cdd:PRK09406 161 NVPQTALYLADLFRRAgFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 261 FFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSY 340
Cdd:PRK09406 240 VMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 341 VELAKEEGARVVAGGERITdgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVF 420
Cdd:PRK09406 320 VDDAVAAGATILCGGKRPD----GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 740282804 421 TQNLNRAIRVARAIETGRMWVNTYN-SIPAgAPFGGYKQSGIGRE 464
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMTvSYPE-LPFGGVKRSGYGRE 439
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
30-473 |
6.13e-68 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 225.13 E-value: 6.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 30 NPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETlNVDIP 109
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-RAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 110 LGADHFRYFAgvlraEEGSAQVFDENTL-----SLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTS 184
Cdd:PRK13968 92 KSANLCDWYA-----EHGPAMLKAEPTLvenqqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 185 LSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDhPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFD 263
Cdd:PRK13968 167 GCAQLIAQVFKDAgIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 264 DANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYD----KFVAELSKLfdkvKVGLPWDESTQLGSLI-------YEA 332
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASafteRFVAAAAAL----KMGDPRDEENALGPMArfdlrdeLHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 333 QVKKVLSyvelakeEGARVVAGGERITdgelGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSL 412
Cdd:PRK13968 322 QVEATLA-------EGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740282804 413 YGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAGAPFGGYKQSGIGREthkviLEHY 473
Cdd:PRK13968 391 FGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE-----LSHF 446
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
57-463 |
4.48e-64 |
|
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: 213.93 E-value: 4.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNVDIPLGADHFRYF-------------AGVLR 123
Cdd:cd07087 9 ETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHAlkhlkkwmkprrvSVPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 124 AEEGSAQvfdentlslIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSS---HTSlSLLElgSILQDILPP 200
Cdd:cd07087 89 LQPAKAY---------VIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSElapATS-ALLA--KLIPKYFDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 201 GVVNIVTGKGSKSgQYILDHPgFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILF 280
Cdd:cd07087 157 EAVAVVEGGVEVA-TALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 281 NQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVkVGLPWDESTQLGSLIYEAQVKKVLSYVelakeEGARVVAGGERITd 360
Cdd:cd07087 235 NAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQVDK- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 361 gelgKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAND-----SLYglgggVFTQNLNRAIRVARAIE 435
Cdd:cd07087 308 ----EERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSrpkplALY-----LFSEDKAVQERVLAETS 378
|
410 420 430
....*....|....*....|....*....|
gi 740282804 436 TGRMWVN--TYNSIPAGAPFGGYKQSGIGR 463
Cdd:cd07087 379 SGGVCVNdvLLHAAIPNLPFGGVGNSGMGA 408
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
140-463 |
2.98e-63 |
|
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: 211.96 E-value: 2.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 140 IIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPS---SHTSLSLLELgsiLQDILPPGVVNIVTGkGSKSGQY 216
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSeftPRTSALLAEL---LAEYFDEDEVAVVTG-GADVAAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 217 ildhpgFSKLAF-----TGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSR 291
Cdd:cd07133 173 ------FSSLPFdhllfTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 292 IFVQDTIYDKFVAELSKLFDKVKVGLPwdESTQLGSLIYEAQVKKVLSYVELAKEEGARVVaggERITDGELGKGCfvR- 370
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKMYPTLA--DNPDYTSIINERHYARLQGLLEDARAKGARVI---ELNPAGEDFAAT--Rk 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 371 --PTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAND-----SLYglgggVFTQNLNRAIRVARAIETGRMWVN- 442
Cdd:cd07133 320 lpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINArprplALY-----YFGEDKAEQDRVLRRTHSGGVTINd 394
|
330 340
....*....|....*....|..
gi 740282804 443 -TYNSIPAGAPFGGYKQSGIGR 463
Cdd:cd07133 395 tLLHVAQDDLPFGGVGASGMGA 416
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
57-463 |
2.71e-62 |
|
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: 209.38 E-value: 2.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNVDIPLGADHFRYFAGVL-------RAEEGSA 129
Cdd:cd07135 16 ATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLkkwakdeKVKDGPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 130 QVFDENTlslIIR-EPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTG 208
Cdd:cd07135 96 AFMFGKP---RIRkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 209 kGSKSGQYILDHpGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCA 288
Cdd:cd07135 173 -GVPETTALLEQ-KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 289 GSRIFVQDTIYDKFVAELSKLFDKVKVGLPwDESTQLGSLIYEAQVKKVLSYVELAKeegARVVAGGERItdgelGKGCF 368
Cdd:cd07135 251 PDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTTK---GKVVIGGEMD-----EATRF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 369 VRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN---TYN 445
Cdd:cd07135 322 IPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdtlIHV 401
|
410
....*....|....*...
gi 740282804 446 SIPAgAPFGGYKQSGIGR 463
Cdd:cd07135 402 GVDN-APFGGVGDSGYGA 418
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
70-462 |
2.61e-60 |
|
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: 204.57 E-value: 2.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 70 RADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLnVDIPLGADHFRYFAGVLRAEEGSAQVFD-----ENTLSLIIREP 144
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREGGKPLVDAK-VEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 145 IGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDhPGF 223
Cdd:cd07148 125 IGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAgLPEGWCQAVPCENAVAEKLVTD-PRV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 224 SKLAFTGSTEVGLDVykaaSERLIPAT---LELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYD 300
Cdd:cd07148 204 AFFSFIGSARVGWML----RSKLAPGTrcaLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIAD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 301 KFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERitdgeLGKGCFvRPTLIVDATND 380
Cdd:cd07148 280 DFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKR-----LSDTTY-APTVLLDPPRD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 381 MRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPAG-APFGGYKQS 459
Cdd:cd07148 354 AKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQS 433
|
...
gi 740282804 460 GIG 462
Cdd:cd07148 434 GYG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
57-463 |
7.45e-60 |
|
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: 202.89 E-value: 7.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETL--------NVDIPLGADHFRyfAGVLRAEEGS 128
Cdd:cd07095 11 AAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQtevaamagKIDISIKAYHER--TGERATPMAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 129 AQvfdentlSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVT 207
Cdd:cd07095 89 GR-------AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 208 GkGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASER--LIPAtLELGGKSANIFFDDANWKQALDGAMLGILFNQGQV 285
Cdd:cd07095 162 G-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRpgKILA-LEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 286 CCAGSRIFV-QDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGelg 364
Cdd:cd07095 240 CTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAG--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 365 kGCFVRPTLIvDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQN---LNRAIRVARAietGRM-W 440
Cdd:cd07095 317 -TAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDealFERFLARIRA---GIVnW 391
|
410 420
....*....|....*....|...
gi 740282804 441 VNTYNSIPAGAPFGGYKQSGIGR 463
Cdd:cd07095 392 NRPTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
59-463 |
1.07e-58 |
|
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: 199.76 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 59 FKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRETLNVDI-PLGAD------HFRYFAGVLRAeegSAQV 131
Cdd:cd07134 11 ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEIlPVLSEinhaikHLKKWMKPKRV---RTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 132 FDENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTGkGS 211
Cdd:cd07134 88 LLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEG-DA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 212 KSGQYILDHPgFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSR 291
Cdd:cd07134 167 EVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 292 IFVQDTIYDKFVAELSKLFDKVKVGLPWD-ESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGErITDGElgkgCFVR 370
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFYGKDAARkASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQ----RYIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 371 PTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAND-----SLYglgggVFTQNLNRAIRVARAIETGRMWVNT-- 443
Cdd:cd07134 321 PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAkpkplALY-----VFSKDKANVNKVLARTSSGGVVVNDvv 395
|
410 420
....*....|....*....|
gi 740282804 444 YNSIPAGAPFGGYKQSGIGR 463
Cdd:cd07134 396 LHFLNPNLPFGGVNNSGIGS 415
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-462 |
4.53e-56 |
|
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: 195.11 E-value: 4.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 5 IKERYGLLINNEW--VPASDGAEFN------VYNPANGEQ-LAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLL 75
Cdd:cd07125 19 LADALKAFDEKEWeaIPIINGEETEtgegapVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 76 KIADAIDAHKEHLAQVETYDNGKPIRETLnVDIPLGADHFRYFAGVLRAEEGSAQ---VFDE-NTLSLiirEPIGVVGQV 151
Cdd:cd07125 99 KAADLLEANRGELIALAAAEAGKTLADAD-AEVREAIDFCRYYAAQARELFSDPElpgPTGElNGLEL---HGRGVFVCI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 152 VPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTG 230
Cdd:cd07125 175 SPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAgVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 231 STEVGLDVYKAASER---LIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELS 307
Cdd:cd07125 255 STETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 308 KLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEgARVVaggERITDGElGKGCFVRPTLI-VDATNDMrvaRE 386
Cdd:cd07125 335 GAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLI---APAPLDD-GNGYFVAPGIIeIVGIFDL---TT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 387 EIFGPVAVVIKFHSE--DEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTyNSIpaGA-----PFGGYKQS 459
Cdd:cd07125 407 EVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-NIT--GAivgrqPFGGWGLS 483
|
...
gi 740282804 460 GIG 462
Cdd:cd07125 484 GTG 486
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
138-462 |
1.86e-55 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 192.94 E-value: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 138 SLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSS---HTSLSLLELgsiLQDILPPGVVNIVTGkGSKSG 214
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSElspHTSKLMAKL---LTKYLDPSYVRVIEG-GVEVT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 215 QYILDHPgFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFV 294
Cdd:PTZ00381 179 TELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 295 QDTIYDKFVAELSKLFDKVkVGLPWDESTQLGSLIYEAQVKKVlsyVELAKEEGARVVAGGERitdGELGKgcFVRPTLI 374
Cdd:PTZ00381 258 HRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRL---AELIKDHGGKVVYGGEV---DIENK--YVAPTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 375 VDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAND-----SLYglgggVFTQNLNRAIRVARAIETGRMWVN--TYNSI 447
Cdd:PTZ00381 329 VNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSrpkplALY-----YFGEDKRHKELVLENTSSGAVVINdcVFHLL 403
|
330
....*....|....*
gi 740282804 448 PAGAPFGGYKQSGIG 462
Cdd:PTZ00381 404 NPNLPFGGVGNSGMG 418
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
138-463 |
1.18e-54 |
|
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: 189.64 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 138 SLIIREPIGVVGQVVPWNFPFLMAawkLAP---ALAAGCTVVIKPS---SHTSlSLLElgSILQDILPPGVVNIVTGkGS 211
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSeltPNTS-KVIA--KIIEETFDEEYVAVVEG-GV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 212 KSGQYILDHPgFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSR 291
Cdd:cd07136 167 EENQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 292 IFVQDTIYDKFVAELSKLFDKVKVGLPwDESTQLGSLIYEAQVKKVLSYVelakeEGARVVAGGErITDGELgkgcFVRP 371
Cdd:cd07136 246 VLVHESVKEKFIKELKEEIKKFYGEDP-LESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGN-TDRETL----YIEP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 372 TLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQAND-----SLYglgggVFTQNLNRAIRVARAIETGRMWVNtyNS 446
Cdd:cd07136 315 TILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSrpkplALY-----LFSEDKKVEKKVLENLSFGGGCIN--DT 387
|
330 340
....*....|....*....|.
gi 740282804 447 IPAGA----PFGGYKQSGIGR 463
Cdd:cd07136 388 IMHLAnpylPFGGVGNSGMGS 408
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
10-464 |
4.05e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.87 E-value: 4.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 10 GLLINNEWvpASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLA 89
Cdd:PLN02315 22 GCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 90 QVETYDNGKPIRETLNvDIPLGADHFRYFAGVLRAEEGSAQVFDE-NTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPA 168
Cdd:PLN02315 100 RLVSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIPSERpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 169 LAAGCTVVIKPSSHTSLSLLELGSILQDIL-----PPGVVNIVTGkGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAAS 243
Cdd:PLN02315 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVLeknnlPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 244 ERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDEST 323
Cdd:PLN02315 258 ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 324 QLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITdgelGKGCFVRPTlIVDATNDMRVAREEIFGPVAVVIKFHSEDE 403
Cdd:PLN02315 338 LLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPT-IVEISPDADVVKEELFGPVLYVMKFKTLEE 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740282804 404 VIEQANDSLYGLGGGVFTQNLNRAIRV--ARAIETGRMWVNT-YNSIPAGAPFGGYKQSGIGRE 464
Cdd:PLN02315 413 AIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIpTNGAEIGGAFGGEKATGGGRE 476
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
19-462 |
1.11e-49 |
|
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: 177.41 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 19 PASDGAEFNVYNPAN-GEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNG 97
Cdd:TIGR01238 46 YKADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 98 KPIRETLNvDIPLGADHFRYFAGVLRaeegsaQVFDENTLsliirEPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVI 177
Cdd:TIGR01238 126 KTIHNAIA-EVREAVDFCRYYAKQVR------DVLGEFSV-----ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 178 KPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERL---IPATLEL 253
Cdd:TIGR01238 194 KPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAET 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 254 GGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQ 333
Cdd:TIGR01238 274 GGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 334 VKKVLSYVELAKEEGaRVVAGGERITDGELGKGCFVRPTLIvdATNDMRVAREEIFGPVAVVIKFHSE--DEVIEQANDS 411
Cdd:TIGR01238 354 KQNLLAHIEHMSQTQ-KKIAQLTLDDSRACQHGTFVAPTLF--ELDDIAELSEEVFGPVLHVVRYKARelDQIVDQINQT 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 740282804 412 LYGLGGGVFTQNLNRAIRVARAIETGRMWVN--TYNSIPAGAPFGGYKQSGIG 462
Cdd:TIGR01238 431 GYGLTMGVHSRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTG 483
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
10-460 |
2.03e-49 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 176.30 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 10 GLLINNEWVpASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLA 89
Cdd:PRK09457 2 TLWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 90 QVETYDNGKPIRETLN--------VDIPLGADHFRyfAGVLRAEEGSAQVFdentlsliIR-EPIGVVGQVVPWNFPFLM 160
Cdd:PRK09457 81 EVIARETGKPLWEAATevtaminkIAISIQAYHER--TGEKRSEMADGAAV--------LRhRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 161 AAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGkGSKSGQYILDHPGFSKLAFTGSTEVGLDVY 239
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 240 KAASER--LIPAtLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIY-DKFVAELSKLFDKVKVG 316
Cdd:PRK09457 230 RQFAGQpeKILA-LEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 317 lPWDESTQ--LGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGeLGkgcFVRPTLIvDATNDMRVAREEIFGPVAV 394
Cdd:PRK09457 309 -RWDAEPQpfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAG-TG---LLTPGII-DVTGVAELPDEEYFGPLLQ 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740282804 395 VIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRM-WVNTYNSIPAGAPFGGYKQSG 460
Cdd:PRK09457 383 VVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-488 |
3.46e-46 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 169.93 E-value: 3.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 12 LINNEWVPASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQV 91
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 92 ETYDNGKPIRETlNVDIPLGADHFRYFAGVLRAEEGSAQVFDENTL-SLIIREPIGVVGQVVPWNFPFLMAAWKLAPALA 170
Cdd:PLN02419 197 ITTEQGKTLKDS-HGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVdTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 171 AGCTVVIKPSSH---TSLSLLELGsiLQDILPPGVVNIVTGKgSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERLI 247
Cdd:PLN02419 276 CGNTFILKPSEKdpgASVILAELA--MEAGLPDGVLNIVHGT-NDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 248 PATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRI-FVQD--TIYDKFVAELSKLfdKVKVGLPWDesTQ 324
Cdd:PLN02419 353 RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVvFVGDakSWEDKLVERAKAL--KVTCGSEPD--AD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 325 LGSLIYEAQVKKVLSYVELAKEEGARVVAGGERITDGELGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEV 404
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 405 IEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTynSIPAGAP---FGGYKQSGIGRETH--KVILEHYTQMKNI 479
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPffsFTGNKASFAGDLNFygKAGVDFFTQIKLV 586
|
....*....
gi 740282804 480 IVNLSDKPS 488
Cdd:PLN02419 587 TQKQKDIHS 595
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
11-460 |
3.56e-46 |
|
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: 168.15 E-value: 3.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 11 LLINNEWVpaSDGAEFNVYNPAN-GEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAhkehla 89
Cdd:cd07123 35 LVIGGKEV--RTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSG------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 90 qvetydngkPIRETLNVDIPLG----------------ADHFR---YFAGVLRAEEGSAQvfDENTLSLIIREPI-GVVG 149
Cdd:cd07123 107 ---------KYRYELNAATMLGqgknvwqaeidaacelIDFLRfnvKYAEELYAQQPLSS--PAGVWNRLEYRPLeGFVY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 150 QVVPWNFPFLMAAWKLAPALAaGCTVVIKPSSHTSLS-------LLELGsilqdiLPPGVVNIVTGKGSKSGQYILDHPG 222
Cdd:cd07123 176 AVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSnylvykiLEEAG------LPPGVINFVPGDGPVVGDTVLASPH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 223 FSKLAFTGSTEVGLDVYKAASERL-----IPATL-ELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQD 296
Cdd:cd07123 249 LAGLHFTGSTPTFKSLWKQIGENLdryrtYPRIVgETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 297 TIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEE-GARVVAGGEriTDGElgKGCFVRPTLIV 375
Cdd:cd07123 329 SLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK--CDDS--VGYFVEPTVIE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 376 dATN-DMRVAREEIFGPVAVVIKFHSED--EVIEQAND-SLYGLGGGVFTQNlNRAIRVARAI---ETGRMWVNTYnsiP 448
Cdd:cd07123 405 -TTDpKHKLMTEEIFGPVLTVYVYPDSDfeETLELVDTtSPYALTGAIFAQD-RKAIREATDAlrnAAGNFYINDK---P 479
|
490
....*....|....*..
gi 740282804 449 AGA-----PFGGYKQSG 460
Cdd:cd07123 480 TGAvvgqqPFGGARASG 496
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
20-462 |
3.75e-46 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 172.82 E-value: 3.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 20 ASDGAEFNVYNPANGEQLA-VCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKE---HLAQVE--- 92
Cdd:COG4230 566 AASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAelmALLVREagk 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 93 TYDNG-KPIRETlnVDiplgadhF-RYFAGvlRAEegsaQVFDENTLsliiREPIGVVGQVVPWNFP---FL--MAAwkl 165
Cdd:COG4230 646 TLPDAiAEVREA--VD-------FcRYYAA--QAR----RLFAAPTV----LRGRGVFVCISPWNFPlaiFTgqVAA--- 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 166 apALAAGCTVVIKPSSHTSLS-------LLELGsilqdiLPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDV 238
Cdd:COG4230 704 --ALAAGNTVLAKPAEQTPLIaaravrlLHEAG------VPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 239 YKAASERL-IPATL--ELGGKSANIF-----------------FDDAnwkqaldgamlgilfnqGQVCCAgSRI-FVQDT 297
Cdd:COG4230 776 NRTLAARDgPIVPLiaETGGQNAMIVdssalpeqvvddvlasaFDSA-----------------GQRCSA-LRVlCVQED 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 298 IYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGaRVVAGGERitDGELGKGCFVRPTLI-VD 376
Cdd:COG4230 838 IADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVHQLPL--PEECANGTFVAPTLIeID 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 377 ATNDMrvaREEIFGPVAVVIKFHSE--DEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGrmwvNTY---NSIpaGA 451
Cdd:COG4230 915 SISDL---EREVFGPVLHVVRYKADelDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYvnrNII--GA 985
|
490
....*....|....*.
gi 740282804 452 -----PFGGYKQSGIG 462
Cdd:COG4230 986 vvgvqPFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
20-462 |
1.09e-44 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 168.50 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 20 ASDGAEFNVYNPAN-GEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGK 98
Cdd:PRK11905 563 DVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGK 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 99 P-------IRETlnVDiplgadhF-RYFAgvlraeegsAQVfdENTLSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALA 170
Cdd:PRK11905 643 TlanaiaeVREA--VD-------FlRYYA---------AQA--RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALV 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 171 AGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERL--- 246
Cdd:PRK11905 703 AGNTVLAKPAEQTPLIAARAVRLLHEAgVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSgpp 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 247 IPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLG 326
Cdd:PRK11905 783 VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVG 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 327 SLIYEAQVKKVLSYVELAKEEGARVvaggERIT-DGELGKGCFVRPTLI-VDATNDMrvaREEIFGPVAVVIKFHSE--D 402
Cdd:PRK11905 863 PVIDAEAQANIEAHIEAMRAAGRLV----HQLPlPAETEKGTFVAPTLIeIDSISDL---EREVFGPVLHVVRFKADelD 935
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740282804 403 EVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTyNSIpaGA-----PFGGYKQSGIG 462
Cdd:PRK11905 936 RVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR-NII--GAvvgvqPFGGEGLSGTG 997
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
18-462 |
2.64e-44 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 167.30 E-value: 2.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 18 VPASDGAEFNVYNPANGEQ-LAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKE---HLAQVET 93
Cdd:PRK11904 556 IINGEGEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAeliALCVREA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 94 ydnGKPI-------REtlnvdiplGADHFRYFAGVLRAEEGSAQVF-----DENTLSLiirEPIGVVGQVVPWNFP---F 158
Cdd:PRK11904 636 ---GKTLqdaiaevRE--------AVDFCRYYAAQARRLFGAPEKLpgptgESNELRL---HGRGVFVCISPWNFPlaiF 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 159 L--MAAwklapALAAGCTVVIKPSSHTSLS-------LLELGsilqdiLPPGVVNIVTGKGSKSGQYILDHPGFSKLAFT 229
Cdd:PRK11904 702 LgqVAA-----ALAAGNTVIAKPAEQTPLIaaeavklLHEAG------IPKDVLQLLPGDGATVGAALTADPRIAGVAFT 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 230 GSTEVGLDVYKAASER---LIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIFVQDTIYDKFVAEL 306
Cdd:PRK11904 771 GSTETARIINRTLAARdgpIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEML 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 307 SKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEgARVVAGGERitDGELGKGCFVRPTLI-VDATNDMrvaR 385
Cdd:PRK11904 851 KGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPL--PAGTENGHFVAPTAFeIDSISQL---E 924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 386 EEIFGPVAVVIKFHSE--DEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTyNSIpaGA-----PFGGYKQ 458
Cdd:PRK11904 925 REVFGPILHVIRYKASdlDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNR-NQI--GAvvgvqPFGGQGL 1001
|
....
gi 740282804 459 SGIG 462
Cdd:PRK11904 1002 SGTG 1005
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
140-481 |
6.76e-39 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 146.40 E-value: 6.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 140 IIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTGkGSKSGQYILD 219
Cdd:cd07137 97 IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEG-GVPETTALLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 220 HPgFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGIL-FNQGQVCCAGSRIFVQD-- 296
Cdd:cd07137 176 QK-WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEEsf 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 297 --TIYDKFVAELSKLFDKVKVglpwdeSTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERiTDGELgkgcFVRPTLI 374
Cdd:cd07137 255 apTLIDALKNTLEKFFGENPK------ESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGER-DEKNL----YIEPTIL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 375 VDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVN--TYNSIPAGAP 452
Cdd:cd07137 324 LDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtVVQYAIDTLP 403
|
330 340
....*....|....*....|....*....
gi 740282804 453 FGGYKQSGIGRETHKVILEHYTQMKNIIV 481
Cdd:cd07137 404 FGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
19-462 |
1.29e-37 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 147.43 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 19 PASDGAEFNVYNPAN-GEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNG 97
Cdd:PRK11809 654 PVAAGEMSPVINPADpRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAG 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 98 KP-------IRETLnvdiplgaDHFRYFAGVLRAEegsaqvFDENTlsliiREPIGVVGQVVPWNFPFLMAAWKLAPALA 170
Cdd:PRK11809 734 KTfsnaiaeVREAV--------DFLRYYAGQVRDD------FDNDT-----HRPLGPVVCISPWNFPLAIFTGQVAAALA 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 171 AGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERL--- 246
Cdd:PRK11809 795 AGNSVLAKPAEQTPLIAAQAVRILLEAgVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpq 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 247 ---IPATLELGGKSANIFFDDANWKQ--------ALDGAmlgilfnqGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKV 315
Cdd:PRK11809 875 grpIPLIAETGGQNAMIVDSSALTEQvvadvlasAFDSA--------GQRCSALRVLCLQDDVADRTLKMLRGAMAECRM 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 316 GLPWDESTQLGSLIYEAQVKKVLSYVELAKEEGaRVVAGGERITDGELGKGCFVRPTLI-VDATNDMrvaREEIFGPVAV 394
Cdd:PRK11809 947 GNPDRLSTDIGPVIDAEAKANIERHIQAMRAKG-RPVFQAARENSEDWQSGTFVPPTLIeLDSFDEL---KREVFGPVLH 1022
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740282804 395 VIKFHSE--DEVIEQANDSLYGLGGGVFTQnLNRAI-RVARAIETGRMWVNTyNSIpaGA-----PFGGYKQSGIG 462
Cdd:PRK11809 1023 VVRYNRNqlDELIEQINASGYGLTLGVHTR-IDETIaQVTGSAHVGNLYVNR-NMV--GAvvgvqPFGGEGLSGTG 1094
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
57-463 |
5.45e-37 |
|
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: 141.59 E-value: 5.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPIRET-------LNVDIPLGADHFRYFAGVLRAEEGSA 129
Cdd:cd07132 9 EAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvlseillVKNEIKYAISNLPEWMKPEPVKKNLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 130 QVFDEntlSLIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPS---SHTSlsllelgSILQDILP----PGV 202
Cdd:cd07132 89 TLLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSevsPATA-------KLLAELIPkyldKEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 203 VNIVTGkGSKSGQYILDHPgFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQ 282
Cdd:cd07132 159 YPVVLG-GVEETTELLKQR-FDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 283 GQVCCAGSRIFVQDTIYDKFVAELSKLFDKVkVGLPWDESTQLGSLIYEAQVKKVLSYVelakeEGARVVAGGEriTDge 362
Cdd:cd07132 237 GQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQ--TD-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 363 lGKGCFVRPTLIVDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDS-----LYglgggVFTQNLNRAIRVARAIETG 437
Cdd:cd07132 307 -EKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSRekplaLY-----VFSNNKKVINKILSNTSSG 380
|
410 420
....*....|....*....|....*...
gi 740282804 438 RMWVN--TYNSIPAGAPFGGYKQSGIGR 463
Cdd:cd07132 381 GVCVNdtIMHYTLDSLPFGGVGNSGMGA 408
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
55-442 |
3.87e-33 |
|
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: 130.74 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 55 ATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHL---AQVETydnGKPIREtLNVDIPLGADHFRYFAGVLRaeEGS--- 128
Cdd:cd07129 8 AAAAFESYRALSPARRAAFLEAIADEIEALGDELvarAHAET---GLPEAR-LQGELGRTTGQLRLFADLVR--EGSwld 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 129 AQVFDEN-----------TLSLIirePIGVVGQVVPWNFP--FLMAAWKLAPALAAGCTVVIKP-SSHTSLSLLELGSIL 194
Cdd:cd07129 82 ARIDPADpdrqplprpdlRRMLV---PLGPVAVFGASNFPlaFSVAGGDTASALAAGCPVVVKAhPAHPGTSELVARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 195 QDI----LPPGVVNIVTGKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASERL--IPATLELGgkSAN-IFFDDANW 267
Cdd:cd07129 159 AALratgLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPepIPFYAELG--SVNpVFILPGAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 268 KQalDGAMLG------ILFNQGQVC-CAGSRIFVQDTIYDKFVAELSKLFDKVKVGlpwdesTQLGSLIYEAQVKKVlsy 340
Cdd:cd07129 237 AE--RGEAIAqgfvgsLTLGAGQFCtNPGLVLVPAGPAGDAFIAALAEALAAAPAQ------TMLTPGIAEAYRQGV--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 341 VELAKEEGARVVAGGeritdGELGKGCFVRPTLI-VDATNDMR--VAREEIFGPVAVVIKFHSEDEVIEQAND------- 410
Cdd:cd07129 306 EALAAAPGVRVLAGG-----AAAEGGNQAAPTLFkVDAAAFLAdpALQEEVFGPASLVVRYDDAAELLAVAEAlegqlta 380
|
410 420 430
....*....|....*....|....*....|....
gi 740282804 411 SLYGLgggvfTQNLNRAIRVARAIE--TGRMWVN 442
Cdd:cd07129 381 TIHGE-----EDDLALARELLPVLErkAGRLLFN 409
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
57-404 |
1.31e-31 |
|
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: 126.20 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 57 EAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVETYDNGKPirETLNVDIPLGADHFRYFAGVLRAEEGSAQVFDE-- 134
Cdd:cd07084 10 ISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG--WMFAENICGDQVQLRARAFVIYSYRIPHEPGNHlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 135 NTLSLIIRE---PIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQD--ILPPGVVNIVTGK 209
Cdd:cd07084 88 QGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 210 GsKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASErlIPATLELGGKSANIFFDDANWKQAL-DGAMLGILFNQGQVCCA 288
Cdd:cd07084 168 G-KTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQAVDYVaWQCVQDMTACSGQKCTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 289 GSRIFVQDTiydkfvAELSKLFDKVKVGLpwDESTQLGSLIYEAQVKKVLSYVELAKEEGARVVAGGERI---TDGELGK 365
Cdd:cd07084 245 QSMLFVPEN------WSKTPLVEKLKALL--ARRKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFSGKElknHSIPSIY 316
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 740282804 366 GCFVRPTLIVDATNDMRVAR---EEIFGPVAVVIKFHSEDEV 404
Cdd:cd07084 317 GACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLA 358
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
140-480 |
2.09e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 120.54 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 140 IIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTGKGSKSGQyiLD 219
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTA--LL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 220 HPGFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGIL-FNQGQVCCAGSRIFVQD-- 296
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKey 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 297 --TIYDKFVAELSKLFDKVKVglpwdESTQLGSLIYEAQVKKvLSYVELAKEEGARVVAGGERitDGELGKgcfVRPTLI 374
Cdd:PLN02174 266 apKVIDAMKKELETFYGKNPM-----ESKDMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGEK--DRENLK---IAPTIL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 375 VDATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMWVNTYNSIPA--GAP 452
Cdd:PLN02174 335 LDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLP 414
|
330 340
....*....|....*....|....*...
gi 740282804 453 FGGYKQSGIGRETHKVILEHYTQMKNII 480
Cdd:PLN02174 415 FGGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
13-442 |
1.92e-28 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 118.14 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 13 INNEWVpASDGAEFNVYNPANGEQLAVCAEATQADVDKAVAAATEAFKTWKTVSQVDRADYLLKIADAIDAHKEHLAQVe 92
Cdd:cd07128 5 VAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYAL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 93 TYDNGKPIRETLnVDIPLGADHFRYFAGVLRAE--------EGSAQVFDENtLSLI---IREPI-GVVGQVVPWNFPflm 160
Cdd:cd07128 83 SAATGATRRDSW-IDIDGGIGTLFAYASLGRRElpnahflvEGDVEPLSKD-GTFVgqhILTPRrGVAVHINAFNFP--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 161 aAW----KLAPALAAGCTVVIKPSSHTSLSLLELGSILQD--ILPPGVVNIVTGkgskSGQYILDH-PGFSKLAFTGSTE 233
Cdd:cd07128 158 -VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICG----SVGDLLDHlGEQDVVAFTGSAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 234 VG--LDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQ-----GQVCCAGSRIFVQDTIYDKFVAEL 306
Cdd:cd07128 233 TAakLRAHPNIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREmtvkaGQKCTAIRRAFVPEARVDAVIEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 307 SKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEgARVVAGG---ERITDGELGKGCFVRPTLIV--DATNDM 381
Cdd:cd07128 313 KARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrFEVVGADAEKGAFFPPTLLLcdDPDAAT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740282804 382 RVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIET--GRMWVN 442
Cdd:cd07128 392 AVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVL 454
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
70-408 |
6.68e-28 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 116.73 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 70 RADYLLKIADAIDAHKEHLAQVETyDNGKPIRETLNVDIPLGADHFRYFAGvLRAEEGSAQVFDENTLSLIIREPI---- 145
Cdd:PRK11903 65 RAALLAAIVKVLQANRDAYYDIAT-ANSGTTRNDSAVDIDGGIFTLGYYAK-LGAALGDARLLRDGEAVQLGKDPAfqgq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 146 -------GVVGQVVPWNFPflmaAW----KLAPALAAGCTVVIKPSSHTSLSLLELGSILQD--ILPPGVVNIVTGkgsk 212
Cdd:PRK11903 143 hvlvptrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAagILPAGALSVVCG---- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 213 SGQYILDH-PGFSKLAFTGSTEVgldvykAASERLIPATLELGGKSaNIFFDdanwkqALDGAMLG-------------- 277
Cdd:PRK11903 215 SSAGLLDHlQPFDVVSFTGSAET------AAVLRSHPAVVQRSVRV-NVEAD------SLNSALLGpdaapgseafdlfv 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 278 ------ILFNQGQVCCAGSRIFVQDTIYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVELAKEEgARV 351
Cdd:PRK11903 282 kevvreMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEV 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740282804 352 VAGGER--ITDGELGKGCFVRPTLIV--DATNDMRVAREEIFGPVAVVIKFHSEDEVIEQA 408
Cdd:PRK11903 361 LFDGGGfaLVDADPAVAACVGPTLLGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
140-480 |
2.33e-27 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 114.82 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 140 IIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNIVTGkGSKSGQYILD 219
Cdd:PLN02203 104 VVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEG-GPAVGEQLLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 220 HPgFSKLAFTGSTEVGLDVYKAASERLIPATLELGGKSANIF--FDDANWKQALDGAMLGILFN--QGQVCCAGSRIFVQ 295
Cdd:PLN02203 183 HK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSRDTKVAVNRIVGGKWGscAGQACIAIDYVLVE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 296 DTiYDKFVAELSKLFDKVKVGLPWDESTQLGSLIYEAQVKKVLSYVElAKEEGARVVAGGeritdGELGKGCFVRPTLIV 375
Cdd:PLN02203 262 ER-FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLK-DPRVAASIVHGG-----SIDEKKLFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 376 DATNDMRVAREEIFGPVAVVIKFHSEDEVIEQANDSLYGLGGGVFTQNLNRAIRVARAIETGRMwvnTYNS--IPAGA-- 451
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDaiIQYACds 411
|
330 340 350
....*....|....*....|....*....|
gi 740282804 452 -PFGGYKQSGIGRETHKVILEHYTQMKNII 480
Cdd:PLN02203 412 lPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
63-457 |
4.17e-11 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 64.98 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 63 KTVSQVDRAdyLLKIADAIDAHKEHLAQVETYDNGKPIretlnVDIPLGADHF--RYFAGVLRAEEgSAQVF--DENTLS 138
Cdd:cd07081 18 KSQEMVDLI--FRAAAEAAEDARIDLAKLAVSETGMGR-----VEDKVIKNHFaaEYIYNVYKDEK-TCGVLtgDENGGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 139 LIIREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTS-LSLLELGSILQDIL----PPGVVNIVTGKGSKS 213
Cdd:cd07081 90 LIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKkVTQRAATLLLQAAVaagaPENLIGWIDNPSIEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 214 GQYILDHPGFSKLAFTGstevGLDVYKAASERLIPATLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCCAGSRIF 293
Cdd:cd07081 170 AQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 294 VQDTIYDkfvaELSKLFdkvkvglpwdeSTQLGSLIYEAQVKKVLSyVELAKEEGARVVAGGERITDGELGkGCFVRPT- 372
Cdd:cd07081 246 VVDSVYD----EVMRLF-----------EGQGAYKLTAEELQQVQP-VILKNGDVNRDIVGQDAYKIAAAA-GLKVPQEt 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 373 --LIVDATNdmrVAREEIFG-----PVAVVIKFHSEDEVIEQAnDSLYGLGG-----GVFTQNLN---RAIRVARAIETG 437
Cdd:cd07081 309 riLIGEVTS---LAEHEPFAheklsPVLAMYRAANFADADAKA-LALKLEGGcghtsAMYSDNIKaieNMNQFANAMKTS 384
|
410 420
....*....|....*....|
gi 740282804 438 RMWVNTYNSIPAGAPFGGYK 457
Cdd:cd07081 385 RFVKNGPCSQGGLGDLYNFR 404
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
142-480 |
1.16e-09 |
|
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: 60.59 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 142 REPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-LPPGVVNIVTGKGSKSGQYILDh 220
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCgMPATDVDLIHSDGPTMNKILLE- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 221 PGFSKLAFTGSTEVgldvykaaSERLipaTLELGGKsanIFFDDA--NWK----QALDGAMLGILFNQ------GQVCCA 288
Cdd:cd07126 219 ANPRMTLFTGSSKV--------AERL---ALELHGK---VKLEDAgfDWKilgpDVSDVDYVAWQCDQdayacsGQKCSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 289 GSRIF-----VQDTIYDKF--VAELSKLFDkVKVG--LPWDEstqlgsliyeaqvKKVLSYVE-LAKEEGARVVAGGERI 358
Cdd:cd07126 285 QSILFahenwVQAGILDKLkaLAEQRKLED-LTIGpvLTWTT-------------ERILDHVDkLLAIPGAKVLFGGKPL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 359 TDGELgKGCF--VRPTLI------VDATNDMRVAREEIFGPVAVVIKFHSEDE--VIEQANDSLYGLGGGVFTQNLNRAI 428
Cdd:cd07126 351 TNHSI-PSIYgaYEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQ 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740282804 429 RVARAIETGrmwvNTYNSI--------------PAGAPFGGykqsGIGreTHKVILEHYTQMKNII 480
Cdd:cd07126 430 EVLANTVNG----TTYAGIrarttgapqnhwfgPAGDPRGA----GIG--TPEAIRLVWSCHREII 485
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
154-442 |
1.93e-07 |
|
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: 53.64 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 154 WN-FPFLMAAwklapaLAAGCTVVIKPSSHTSLSLLELGSILQDILP-----PGVVNIVT-GKGSKSGQYILDHPGFSKL 226
Cdd:cd07127 208 WNgYPGLFAS------LATGNPVIVKPHPAAILPLAITVQVAREVLAeagfdPNLVTLAAdTPEEPIAQTLATRPEVRII 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 227 AFTGSTEVGLDVYKAASER------------LIPATLELGGKSANIFFDDAnwkqaldgamlgiLFNqGQVCCAGSRIFV 294
Cdd:cd07127 282 DFTGSNAFGDWLEANARQAqvytekagvntvVVDSTDDLKAMLRNLAFSLS-------------LYS-GQMCTTPQNIYV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 295 -QDTI--------YDKFVAELSKLFDKVkVGLPWDESTQLGSLIYEAqvkkVLSYVELAKEeGARVVAGGERITDGELGK 365
Cdd:cd07127 348 pRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQSPD----TLARIAEARQ-LGEVLLASEAVAHPEFPD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 366 GCFVRPTLI-VDATNDMRVArEEIFGPVAVVIKFHSEDEVIEQANDSLYGLGG---GVFT---------QNLNRAIRVAR 432
Cdd:cd07127 422 ARVRTPLLLkLDASDEAAYA-EERFGPIAFVVATDSTDHSIELARESVREHGAmtvGVYStdpevvervQEAALDAGVAL 500
|
330
....*....|.
gi 740282804 433 AIE-TGRMWVN 442
Cdd:cd07127 501 SINlTGGVFVN 511
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
141-455 |
4.56e-07 |
|
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: 52.11 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 141 IREPIGVVGQVVPWNFPFLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDI-----LPPGVVNIVTGKGSKSGQ 215
Cdd:cd07122 92 IAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaagAPEGLIQWIEEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 216 YILDHPGFSKLAFTGSTEVgldVyKAASERLIPAtleLGGKSAN--IFFD-DANWKQALDGAMLGILFNQGQVCCAGSRI 292
Cdd:cd07122 172 ELMKHPDVDLILATGGPGM---V-KAAYSSGKPA---IGVGPGNvpAYIDeTADIKRAVKDIILSKTFDNGTICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 293 FVQDTIYDKFVAELSKLfdkvkvG---LPWDESTQLGSLIYEAQVKKVLSYV-----ELAKEEGARVVAGgeritdgelg 364
Cdd:cd07122 245 IVDDEIYDEVRAELKRR------GayfLNEEEKEKLEKALFDDGGTLNPDIVgksaqKIAELAGIEVPED---------- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 365 kgcfvRPTLIVDATNdmrVAREEIF-----GPVAVVIKFHSEDEVIEQANdSLYGLGG-----GVFTQNLNRAIRVARAI 434
Cdd:cd07122 309 -----TKVLVAEETG---VGPEEPLsreklSPVLAFYRAEDFEEALEKAR-ELLEYGGaghtaVIHSNDEEVIEEFALRM 379
|
330 340
....*....|....*....|.
gi 740282804 435 ETGRMWVNTynsipaGAPFGG 455
Cdd:cd07122 380 PVSRILVNT------PSSLGG 394
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
63-344 |
1.56e-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: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 63 KTVSQVDRAdyLLKIADAIDAHKEHLAQVETYDNGKPIRETL-NVDIPLG---------ADHFRYFAGvlrAEEGSAQVF 132
Cdd:cd07077 13 NHDEQRDLI--INAIANALYDTRQRLASEAVSERGAYIRSLIaNWIAMMGcsesklyknIDTERGITA---SVGHIQDVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 133 DENTLSLIIR-EPIGVVGQVVPWNFPfLMAAWKLAPALAAGCTVVIKPSSHTSLSLLELGSILQDILPPGVVNI----VT 207
Cdd:cd07077 88 LPDNGETYVRaFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKIlvlyVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740282804 208 GKGSKSGQYILDHPGFSKLAFTGSTEVGLDVYKAASErlIPAtLELGGKSANIFFDDANWKQALDGAMLGILFNQGQVCC 287
Cdd:cd07077 167 HPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPH--IPV-IGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740282804 288 AGSRIFVQDTIYD--------KFVAELSKLFD--KVKVGLPWDES-----TQLGSLIYEAQVKKVLSYVELA 344
Cdd:cd07077 244 SEQNLYVVDDVLDplyeefklKLVVEGLKVPQetKPLSKETTPSFddealESMTPLECQFRVLDVISAVENA 315
|
|
| |
