|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
19-244 |
5.85e-155 |
|
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: 439.09 E-value: 5.85e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELL 98
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 99 AVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPA 178
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 179 LAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTV 226
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
19-244 |
4.01e-154 |
|
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: 436.88 E-value: 4.01e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELL 98
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 99 AVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPA 178
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 179 LAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTT 226
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
16-244 |
1.90e-101 |
|
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: 302.82 E-value: 1.90e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 16 KPRYENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNL 95
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 96 ELLAVAETWDNGKAVRETiAADIPLCVDHFRYFAGCLRSQEGSMAELD-EHTVSYHLHEPLGVVGQIIPWNFPLLMAAWK 174
Cdd:COG1012 83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712421913 175 LGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAV 232
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
19-244 |
1.46e-95 |
|
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: 287.81 E-value: 1.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELL 98
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 99 AVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPA 178
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 179 LAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEV 226
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
22-244 |
1.34e-92 |
|
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: 280.25 E-value: 1.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLA 99
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 180 AAGNCVVLKPAEQTPASILVLIELIGD-LLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07091 167 AAGNTVVLKPAEQTPLSALYLAELIKEaGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAV 232
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
27-244 |
5.96e-91 |
|
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: 275.56 E-value: 5.96e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 27 WVAPvEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDN 106
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 107 GKAVRETiAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVV 186
Cdd:pfam00171 80 GKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1712421913 187 LKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAV 217
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
19-244 |
2.17e-85 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 261.77 E-value: 2.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVApVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELL 98
Cdd:PRK13473 3 TKLLINGELVA-GEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 99 AVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAE--LDEHTvSYHLHEPLGVVGQIIPWNFPLLMAAWKLG 176
Cdd:PRK13473 82 ARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGeyLEGHT-SMIRRDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712421913 177 PALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIAT 228
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
22-244 |
4.81e-84 |
|
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: 258.49 E-value: 4.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA-KTAWGKTAAAERANVLLRIADRMEQNLELLAV 100
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 101 AETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALA 180
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712421913 181 AGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
39-244 |
3.20e-80 |
|
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: 247.63 E-value: 3.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAADI 118
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAGCLRSQEGSMA-ELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASI 197
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAgEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1712421913 198 LVLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07092 162 LLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRT 208
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-244 |
2.70e-79 |
|
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: 246.29 E-value: 2.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA-KTAWG-KTAAAERANVLLRIADRMEQNLELLA 99
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 180 AAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLV 235
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
22-244 |
2.03e-78 |
|
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: 244.14 E-value: 2.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLA 99
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETiAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 180 AAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTAT 225
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
38-243 |
4.81e-78 |
|
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: 242.09 E-value: 4.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 38 NISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAAD 117
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 118 IPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASI 197
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1712421913 198 LVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTA 243
Cdd:cd07093 161 WLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETA 207
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
33-244 |
1.31e-77 |
|
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: 241.35 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 33 GDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAV 110
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 111 RETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPA 190
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1712421913 191 EQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07112 161 EQSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEV 215
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
22-244 |
1.55e-76 |
|
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: 239.17 E-value: 1.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA---KTAWGKTAAAERANVLLRIADRMEQNLELL 98
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 99 AVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPA 178
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 179 LAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
22-244 |
4.45e-76 |
|
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: 237.78 E-value: 4.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLA 99
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 180 AAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEV 232
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-244 |
2.26e-75 |
|
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: 234.80 E-value: 2.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 61 ALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAADIPLCVDHFRYFAGCLRSQEGSMA 140
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA-LGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 141 -ELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGD-LLPAGVLNIVNG 218
Cdd:cd07078 82 pSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEaGLPPGVLNVVTG 161
|
170 180
....*....|....*....|....*.
gi 1712421913 219 IGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAV 187
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-244 |
2.80e-74 |
|
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: 232.44 E-value: 2.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIA- 115
Cdd:cd07114 2 INPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 116 -ADIPlcvDHFRYFAGCLRSQEGSMAELDEHTV-SYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQT 193
Cdd:cd07114 82 vRYLA---EWYRYYAGLADKIEGAVIPVDKGDYlNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1712421913 194 PASILVLIELI---GdlLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07114 159 PASTLELAKLAeeaG--FPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTET 210
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
12-244 |
1.55e-73 |
|
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: 231.52 E-value: 1.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 12 LVNFKPRYENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRM 91
Cdd:cd07111 15 LDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 92 EQNLELLAVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAEldehtvsyhlHEPLGVVGQIIPWNFPLLMA 171
Cdd:cd07111 95 QKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAG----------WKPVGVVGQIVPWNFPLLML 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712421913 172 AWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGeEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07111 165 AWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEV 237
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-244 |
1.96e-72 |
|
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: 227.71 E-value: 1.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 38 NISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAAD 117
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 118 IPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASI 197
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1712421913 198 LVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07115 161 LRIAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAV 208
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
63-244 |
6.24e-69 |
|
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: 216.33 E-value: 6.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 63 DAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAADIPLCVDHFRYFAGCLRSQEGSM-AE 141
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPElPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 142 LDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGD-LLPAGVLNIVNGIG 220
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEaGLPPGVVNVVPGGG 159
|
170 180
....*....|....*....|....
gi 1712421913 221 EEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAV 183
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
19-244 |
7.89e-68 |
|
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: 216.35 E-value: 7.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVAPVEGDymENISPV-TGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLEL 97
Cdd:cd07097 1 YRNYIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 98 LAVAETWDNGKAVRETI-----AADIplcvdhFRYFAG-CLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMA 171
Cdd:cd07097 79 LARLLTREEGKTLPEARgevtrAGQI------FRYYAGeALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712421913 172 AWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07097 153 AWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAV 226
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
39-244 |
8.17e-66 |
|
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: 210.46 E-value: 8.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAADI 118
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAGCLRSQEgsMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASIL 198
Cdd:cd07106 81 GGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1712421913 199 VLIELIGDLLPAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07106 159 KLGELAQEVLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTAT 203
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
22-244 |
1.44e-65 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 212.36 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLA 99
Cdd:PLN02466 61 LINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELD-EHTVSYhLHEPLGVVGQIIPWNFPLLMAAWKLGPA 178
Cdd:PLN02466 141 ALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADgPHHVQT-LHEPIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 179 LAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PLN02466 220 LACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDT 286
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
18-243 |
3.57e-64 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 206.77 E-value: 3.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 18 RYENFIGGEWVAPvEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLEL 97
Cdd:TIGR03374 1 QHKLLINGELVSG-EGEKQPVYNPATGEVILEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENAQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 98 LAVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMA--ELDEHTvSYHLHEPLGVVGQIIPWNFPLLMAAWKL 175
Cdd:TIGR03374 80 FAELESRNCGKPLHSVFNDEIPAIVDVFRFFAGAARCLSGLAAgeYLEGHT-SMIRRDPLGVVASIAPWNYPLMMAAWKL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712421913 176 GPALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTA 243
Cdd:TIGR03374 159 APALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGKTVGDPLTGHEKVRMVSLTGSIA 226
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
39-244 |
4.01e-64 |
|
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: 206.13 E-value: 4.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAaDI 118
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG-EV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAGCLRSQEGSMAELDEHTVSYH-LHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASI 197
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILvIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1712421913 198 LVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07103 161 LALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAV 208
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
39-244 |
9.38e-64 |
|
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: 205.16 E-value: 9.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAA-KTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAaD 117
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 118 IPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASI 197
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1712421913 198 LVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07109 161 LRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVET 208
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
39-244 |
1.41e-63 |
|
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: 204.90 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAADI 118
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASIL 198
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1712421913 199 VLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07108 162 LLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEV 207
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-244 |
1.11e-62 |
|
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: 202.58 E-value: 1.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAADI 118
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAGC---LRSQEGSMAELDEHTVSYH-LHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTP 194
Cdd:cd07110 81 DDVAGCFEYYADLaeqLDAKAERAVPLPSEDFKARvRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1712421913 195 ASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07110 161 LTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTAT 211
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-242 |
2.01e-62 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 202.82 E-value: 2.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLA 99
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712421913 180 AAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGST 242
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGST 246
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
17-243 |
7.57e-62 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 201.50 E-value: 7.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 17 PRYENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTA-----WGKTAAAERANVLLRIADRM 91
Cdd:PLN02467 6 PRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 92 EQNLELLAVAETWDNGKAVRETI--AADIPLCVDHFRYFAGCLRSQEGSMAEL-DEHTVSYHLHEPLGVVGQIIPWNFPL 168
Cdd:PLN02467 86 TERKSELAKLETLDCGKPLDEAAwdMDDVAGCFEYYADLAEALDAKQKAPVSLpMETFKGYVLKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 169 LMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTA 243
Cdd:PLN02467 166 LMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTA 241
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
21-244 |
1.21e-61 |
|
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: 200.04 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 21 NFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAV 100
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 101 AETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEgsmaeLDEHTVSYHL-HEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDFE-----FEERRGNSLVvREPIGVCGLITPWNWPLNQIVLKVAPAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 180 AAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA 221
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
17-243 |
1.39e-59 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 195.48 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 17 PRYENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRM-EQNL 95
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILrERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 96 ELlAVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKL 175
Cdd:PRK13252 85 EL-AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712421913 176 GPALAAGNCVVLKPAEQTPASILVLIE-LIGDLLPAGVLNIVNGIGeEAGQALASSNRIAKIAFTGSTA 243
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEiYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVP 231
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
22-243 |
5.38e-59 |
|
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: 193.25 E-value: 5.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVA 101
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 102 ETWDNGKAVRETiAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLH-EPLGVVGQIIPWNFPLLMAAWKLGPALA 180
Cdd:cd07088 81 IVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFkVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712421913 181 AGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTA 243
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTE 223
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
22-244 |
1.09e-58 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 193.50 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLA 99
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712421913 180 AAGNCVVLKPAEQTPASILV---LIELIGdlLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFyahLAKLAG--VPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEV 249
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-243 |
1.43e-57 |
|
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: 189.51 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAaDI 118
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASIL 198
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1712421913 199 VLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTA 243
Cdd:cd07107 161 RLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVP 205
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
38-244 |
3.27e-57 |
|
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: 188.28 E-value: 3.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 38 NISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVrETIAAD 117
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 118 IPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASI 197
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1712421913 198 LVLIELIGDL-LPAGVLNIVNGIGeEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07090 160 LLLAEILTEAgLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPT 206
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-244 |
1.15e-56 |
|
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: 187.40 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLA 99
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSqegsMAELDEHTVSYH-----LHEPLGVVGQIIPWNFPLLMAAWK 174
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARD----FPFEERRPGSGGghvlvRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712421913 175 LGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAA 227
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
19-244 |
1.86e-56 |
|
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: 187.32 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLE 96
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 97 LLAVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELDE----HTVSYHLHEPLGVVGQIIPWNFPLLMAA 172
Cdd:cd07140 86 ELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQarpnRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712421913 173 WKLGPALAAGNCVVLKPAEQTPASILVLIEL-IGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPI 238
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
21-244 |
2.30e-55 |
|
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: 184.09 E-value: 2.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 21 NFIGGEWVAPVEGDYMENISPVTG-EAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLA 99
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 100 VAETWDNGKAVRETiAADIPLCVDHFRYFAGCLRSQEG-----SMAELDEHTVsyhlHEPLGVVGQIIPWNFPLLMAAWK 174
Cdd:cd07131 81 RLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGetvpsELPNKDAMTR----RQPIGVVALITPWNFPVAIPSWK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712421913 175 LGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07131 156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEV 226
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
38-244 |
7.53e-55 |
|
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: 182.44 E-value: 7.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 38 NISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWgKTAAAERANVLLRIADRMEQNLELLA---VAETwdnGKAVRE 112
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAfdTGDW-STDAEERARCLRQLHEALEARKEELRallVAEV---GAPVMT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 113 TIAADIPLCVDHFRYFAGCLRSQEGS--------MAELDEHTVSyhlHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNC 184
Cdd:cd07089 77 ARAMQVDGPIGHLRYFADLADSFPWEfdlpvpalRGGPGRRVVR---REPVGVVAAITPWNFPFFLNLAKLAPALAAGNT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712421913 185 VVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07089 154 VVLKPAPDTPLSALLLGEIIAETdLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAV 214
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
39-244 |
2.58e-52 |
|
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: 175.61 E-value: 2.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWgKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAA 116
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 117 DIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPAS 196
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1712421913 197 ILVLIELIGDL--LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07120 160 NAAIIRILAEIpsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTAT 209
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
39-244 |
5.43e-52 |
|
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: 174.83 E-value: 5.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAA--KTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAA 116
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 117 DIPLCVDHFRYFAGCLRSQEG-SMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPA 195
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGdSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1712421913 196 SILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07118 161 TTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRV 210
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-243 |
5.45e-52 |
|
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: 175.32 E-value: 5.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAA-KTAWGKTAAAERANVLLRIADRMEQNLELLAV 100
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 101 AETWDNGKAVRETIAADIPLCVDHFRYFAGCLRSQEG--------SMAEldEHTVSYHLHEPLGVVGQIIPWNFPLLMAA 172
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGetlapsipSMQG--ERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712421913 173 WKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGeEAGQALASSNRIAKIAFTGSTA 243
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVA 231
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
18-244 |
2.86e-49 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 168.33 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 18 RYENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLEL 97
Cdd:PLN02278 24 RTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 98 LAVAETWDNGKAVRETIaADIPLCVDHFRYFAGCLRSQEGSMAEL-DEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLG 176
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVG 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712421913 177 PALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PLN02278 183 PALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAV 251
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
36-244 |
6.08e-49 |
|
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: 166.62 E-value: 6.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 36 MENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIA 115
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 116 aDIPLCVDHFRYFAGCLRSQEGSMAELD-----EHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPA 190
Cdd:cd07149 81 -EVDRAIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1712421913 191 EQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07149 160 SQTPLSALKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAV 214
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
36-244 |
5.60e-48 |
|
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: 164.04 E-value: 5.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 36 MENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNG----KAVR 111
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGstygKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 112 ETIAAdiplcVDHFRYFAGCLRSQEGSMAELD-EHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPA 190
Cdd:cd07150 81 ETTFT-----PELLRAAAGECRRVRGETLPSDsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1712421913 191 EQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07150 156 EETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAV 210
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-244 |
6.62e-48 |
|
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: 165.09 E-value: 6.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVapVEGDYMENISPV-TGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLEL 97
Cdd:cd07124 33 YPLVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 98 LAVAETWDNGKAVRETIAaDIPLCVDHFRYFAGCLRSQEGSMAEL--DEHTVSYHlhEPLGVVGQIIPWNFPLLMAAWKL 175
Cdd:cd07124 111 LAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVEMvpGEDNRYVY--RPLGVGAVISPWNFPLAILAGMT 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 176 GPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07124 188 TAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREV 257
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
21-244 |
1.49e-47 |
|
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: 163.50 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 21 NFIGGEWVAPvEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAV 100
Cdd:cd07086 1 GVIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 101 AETWDNGKAVRETIAaDIPLCVDHFRYFAGCLRSQEGSM--AELDEHtVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPA 178
Cdd:cd07086 80 LVSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTipSERPGH-RLMEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712421913 179 LAAGNCVVLKPAEQTPASILVLIELIGDLL-----PAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVLeknglPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEV 227
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-244 |
1.06e-46 |
|
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: 161.15 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 21 NFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAV 100
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 101 AETWDNGKAVRETI------------AADIPlcvdhfRYFAGclRSQEGSMAELDEHTVsyhlHEPLGVVGQIIPWNFPL 168
Cdd:cd07085 83 LITLEHGKTLADARgdvlrglevvefACSIP------HLLKG--EYLENVARGIDTYSY----RQPLGVVAGITPFNFPA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 169 LMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07085 151 MIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPV 226
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
39-243 |
1.36e-44 |
|
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: 155.07 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAvRETIAADI 118
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAG----CLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTP 194
Cdd:cd07099 80 LLALEAIDWAARnaprVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1712421913 195 ASILVLIELIGDL-LPAGVLNIVNGIGeEAGQALASSnRIAKIAFTGSTA 243
Cdd:cd07099 160 LVGELLAEAWAAAgPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVA 207
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
36-244 |
1.83e-44 |
|
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: 154.81 E-value: 1.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 36 MENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIA 115
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 116 aDIPLCVDHFRYFAGCLRSQEGSMAELD-----EHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPA 190
Cdd:cd07145 81 -EVERTIRLFKLAAEEAKVLRGETIPVDayeynERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1712421913 191 EQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07145 160 SNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAV 214
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
57-244 |
1.01e-43 |
|
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: 152.30 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 57 DIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQN---LELLAVAETwdnG----KAVRETIAAdiplcVDHFRYFA 129
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERrdeIADWLIRES---GstrpKAAFEVGAA-----IAILREAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 130 G-CLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLI----ELI 204
Cdd:cd07104 73 GlPRRPEGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaeifEEA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1712421913 205 GdlLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07104 153 G--LPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAV 190
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
28-243 |
8.58e-42 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 148.87 E-value: 8.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 28 VAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNG 107
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 108 K----AVRETiaADIPLCVDHF-RYFAGCLRSQE--GSMAELDEHTVSYHlhePLGVVGQIIPWNFPLLMAAWKLGPALA 180
Cdd:PRK09407 106 KarrhAFEEV--LDVALTARYYaRRAPKLLAPRRraGALPVLTKTTELRQ---PKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712421913 181 AGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALAssNRIAKIAFTGSTA 243
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTA 242
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
53-244 |
1.11e-41 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 151.24 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 53 SGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNL-EL--LAVAE---TWDNGKA-VRETiaadiplcVDHF 125
Cdd:COG4230 590 ATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRaELmaLLVREagkTLPDAIAeVREA--------VDFC 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 126 RYFAgclrsqegsmAELDEHTVSYHLHEPLGVVGQIIPWNFPLL-----MAAwklgpALAAGNCVVLKPAEQTPasilvl 200
Cdd:COG4230 662 RYYA----------AQARRLFAAPTVLRGRGVFVCISPWNFPLAiftgqVAA-----ALAAGNTVLAKPAEQTP------ 720
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1712421913 201 ieLIG----DLL-----PAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:COG4230 721 --LIAaravRLLheagvPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTET 771
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
39-243 |
5.26e-41 |
|
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: 145.53 E-value: 5.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETI--AA 116
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFeeVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 117 DIPLCVDHFRYFAGCL---RSQEGSMAELDEHTVSYHlhePLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQT 193
Cdd:cd07101 81 DVAIVARYYARRAERLlkpRRRRGAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1712421913 194 PASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALAssNRIAKIAFTGSTA 243
Cdd:cd07101 158 ALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTA 206
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
19-244 |
4.22e-40 |
|
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: 143.48 E-value: 4.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVAPvEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAA-AERANVLLRIADRMEQNLEL 97
Cdd:cd07082 2 FKYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 98 LAVAETWDNGK----AVRETIAAdiplcVDHFRYFAGCLRSQEGSMAELDEH-----TVSYHLHEPLGVVGQIIPWNFPL 168
Cdd:cd07082 81 VANLLMWEIGKtlkdALKEVDRT-----IDYIRDTIEELKRLDGDSLPGDWFpgtkgKIAQVRREPLGVVLAIGPFNYPL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 169 LMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07082 156 NLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEV 232
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
39-244 |
6.23e-40 |
|
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: 143.88 E-value: 6.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEA-FCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNL-EL--LAVAETwdnGKAVRETI 114
Cdd:cd07125 51 IDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRgELiaLAAAEA---GKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 115 aADIPLCVDHFRYFAGCLR--SQEGSMAELDEHTVSYHLHePLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQ 192
Cdd:cd07125 128 -AEVREAIDFCRYYAAQARelFSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQ 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1712421913 193 TPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07125 206 TPLIAARAVELLHEAgVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTET 258
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
36-244 |
9.80e-40 |
|
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: 142.19 E-value: 9.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 36 MENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIA 115
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 116 aDIPLCVDHFRYFAGCLRSQEGSMAELDEHTVS-----YHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPA 190
Cdd:cd07094 81 -EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSdnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1712421913 191 EQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07094 160 SKTPLSALELAKILVEAgVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAV 214
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
18-244 |
3.58e-39 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 141.20 E-value: 3.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 18 RYENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLEL 97
Cdd:PRK11241 10 RQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 98 LAVAETWDNGKAVRETiAADIPLCVDHFRYFAgclrsQEGSMAELDehTVSYH--------LHEPLGVVGQIIPWNFPLL 169
Cdd:PRK11241 90 LARLMTLEQGKPLAEA-KGEISYAASFIEWFA-----EEGKRIYGD--TIPGHqadkrlivIKQPIGVTAAITPWNFPAA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 170 MAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PRK11241 162 MITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEI 237
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
11-244 |
1.40e-38 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 142.26 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 11 ALVNFKPRYENFIGGEWVAP----VEGDYMENISPV-TGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLL 85
Cdd:PRK11904 535 ELEPLAAAIAAFLEKQWQAGpiinGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILE 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 86 RIADRMEQNL-ELLA--VAE---TWDNGKA-VRETiaadiplcVDHFRYFAGCLRSQEGSMAEL---DEHTVSYHLHePL 155
Cdd:PRK11904 615 RAADLLEANRaELIAlcVREagkTLQDAIAeVREA--------VDFCRYYAAQARRLFGAPEKLpgpTGESNELRLH-GR 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 156 GVVGQIIPWNFPLlmaAWKLGP---ALAAGNCVVLKPAEQTPasilvlieLIGDL---------LPAGVLNIVNGIGEEA 223
Cdd:PRK11904 686 GVFVCISPWNFPL---AIFLGQvaaALAAGNTVIAKPAEQTP--------LIAAEavkllheagIPKDVLQLLPGDGATV 754
|
250 260
....*....|....*....|.
gi 1712421913 224 GQALASSNRIAKIAFTGSTAV 244
Cdd:PRK11904 755 GAALTADPRIAGVAFTGSTET 775
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
55-244 |
5.45e-38 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 140.77 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 55 AADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNL-ELLAVA-----ETWDNGKA-VRETiaadiplcVDHFRY 127
Cdd:PRK11905 589 AEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMpELFALAvreagKTLANAIAeVREA--------VDFLRY 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 128 FAgclrsQEGsmaeldEHTVSYHLHEPLGVVGQIIPWNFPLLM-----AAwklgpALAAGNCVVLKPAEQTPASILVLIE 202
Cdd:PRK11905 661 YA-----AQA------RRLLNGPGHKPLGPVVCISPWNFPLAIftgqiAA-----ALVAGNTVLAKPAEQTPLIAARAVR 724
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1712421913 203 LIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PRK11905 725 LLHEAgVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEV 767
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-244 |
3.78e-37 |
|
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: 135.51 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 25 GEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLEL---LAVA 101
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEiveWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 102 ET----------WDNGKAV-REtiAADIPLCVdhfryfagclrsqEG----SMAELDEHTVsyhLHEPLGVVGQIIPWNF 166
Cdd:cd07151 81 ESgstrikanieWGAAMAItRE--AATFPLRM-------------EGrilpSDVPGKENRV---YREPLGVVGVISPWNF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 167 PLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLI----ELIGdlLPAGVLNIVNGIGEEAGQALAsSNRIAK-IAFTGS 241
Cdd:cd07151 143 PLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLakifEEAG--LPKGVLNVVVGAGSEIGDAFV-EHPVPRlISFTGS 219
|
...
gi 1712421913 242 TAV 244
Cdd:cd07151 220 TPV 222
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
44-244 |
9.62e-37 |
|
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: 133.96 E-value: 9.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 44 GEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQN---LELLAVAETwdngKAVRETIAADIPL 120
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHadeIADWIVRES----GSIRPKAGFEVGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 121 CVDHFRYFAGCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVL 200
Cdd:cd07152 77 AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1712421913 201 IELIGDL--LPAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07152 157 IARLFEEagLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAV 201
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
23-244 |
1.10e-36 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 135.06 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 23 IGGEWVApvEGDYMENISPV-TGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRM-EQNLELLAV 100
Cdd:PRK03137 41 IGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIrRRKHEFSAW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 101 aETWDNGKAVRETiAADIPLCVDHFRYFA-GCLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:PRK03137 119 -LVKEAGKPWAEA-DADTAEAIDFLEYYArQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAI 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 180 AAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PRK03137 197 VAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREV 262
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
39-244 |
1.23e-36 |
|
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: 133.91 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAADI 118
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAGCLRSQEGSMAELDEHTVS-----YHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQT 193
Cdd:cd07147 83 ARAIDTFRIAAEEATRIYGEVLPLDISARGegrqgLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1712421913 194 PASILVLIELIGD-LLPAGVLNIVNgIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07147 163 PLSALILGEVLAEtGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAV 213
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
49-244 |
1.72e-35 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 133.56 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 49 EVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELL--------------AVAEtwdngkaVRETi 114
Cdd:PRK11809 675 YVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLmgllvreagktfsnAIAE-------VREA- 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 115 aadiplcVDHFRYFAGCLRsqegsmAELDEHTvsyhlHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTP 194
Cdd:PRK11809 747 -------VDFLRYYAGQVR------DDFDNDT-----HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTP 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1712421913 195 asiLVLIELIGDLL----PAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PRK11809 809 ---LIAAQAVRILLeagvPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEV 859
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
22-244 |
2.97e-35 |
|
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: 131.16 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVApvEGDYMENISPV-TGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAV 100
Cdd:cd07083 22 VIGGEWVD--TKERMVSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 101 AETWDNGKAVRETIAaDIPLCVDHFRYFAGCLRSQEGSMAELDEHTVSYH--LHEPLGVVGQIIPWNFPLLMAAWKLGPA 178
Cdd:cd07083 100 TLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNesFYVGLGAGVVISPWNFPVAIFTGMIVAP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 179 LAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07083 179 VAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLET 245
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
41-244 |
5.53e-34 |
|
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: 126.70 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 41 PVTGEAFCEVPRSGAADIELALDAAHAAKtawGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAaDIPL 120
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAASYR---STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY-EVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 121 CVDHFRYFAGCLRSQEGSMAELDEHT-----VSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPA 195
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1712421913 196 SILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07146 162 SAIYLADLLYEAgLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAV 211
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
39-243 |
7.66e-33 |
|
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: 123.90 E-value: 7.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAADI 118
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYF----AGCLRSQEGsmaELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTP 194
Cdd:cd07102 80 RGMLERARYMisiaEEALADIRV---PEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1712421913 195 asilvlieLIGD---------LLPAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTA 243
Cdd:cd07102 157 --------LCGErfaaafaeaGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVA 205
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-241 |
3.29e-32 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 122.37 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPvEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVA 101
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 102 ETWDNGKAVRET------IAADIPLCVDHFRYFAGclrSQEGSMAEldehTVSYHLHEPLGVVGQIIPWNFPLLMAAWKL 175
Cdd:PRK09457 83 IARETGKPLWEAatevtaMINKIAISIQAYHERTG---EKRSEMAD----GAAVLRHRPHGVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 176 GPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGiGEEAGQALASSNRIAKIAFTGS 241
Cdd:PRK09457 156 VPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGS 221
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
50-244 |
4.36e-32 |
|
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: 122.33 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 50 VPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAaDIPLCVDHFRYFA 129
Cdd:TIGR01238 68 VFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIA-EVREAVDFCRYYA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 130 GCLRsqegsmaeldeHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-L 208
Cdd:TIGR01238 147 KQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgF 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 1712421913 209 PAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:TIGR01238 216 PAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEV 251
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
58-243 |
7.70e-32 |
|
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: 120.64 E-value: 7.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 58 IELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIaADIPLCVDHFRYFA----GCLR 133
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEAR-AEVEKCAWICRYYAenaeAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 134 SQEgsmAELDEHTvSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGV 212
Cdd:cd07100 80 DEP---IETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPEGV 155
|
170 180 190
....*....|....*....|....*....|.
gi 1712421913 213 LNIVNGIGEEAGQALASSnRIAKIAFTGSTA 243
Cdd:cd07100 156 FQNLLIDSDQVEAIIADP-RVRGVTLTGSER 185
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
17-241 |
6.61e-31 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 119.85 E-value: 6.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 17 PRYENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLE 96
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 97 LLAVAETWDNGKAVRETiAADIPLCVDHFRYFAGCLRSQEGS-MAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKL 175
Cdd:PLN02419 192 KLAMNITTEQGKTLKDS-HGDIFRGLEVVEHACGMATLQMGEyLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMF 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 176 GPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAgQALASSNRIAKIAFTGS 241
Cdd:PLN02419 271 PVAVTCGNTFILKPSEKDPGASVILAELAMEAgLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGS 336
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-244 |
8.37e-30 |
|
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: 115.37 E-value: 8.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 57 DIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGkAVRETIAADIPLCVDHFRYFAGCL-RSQ 135
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-ATAAWAGFNVDLAAGMLREAASLItQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 136 EGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLN 214
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLN 159
|
170 180 190
....*....|....*....|....*....|...
gi 1712421913 215 IVNGIGEEAGQ---ALASSNRIAKIAFTGSTAV 244
Cdd:cd07105 160 VVTHSPEDAPEvveALIAHPAVRKVNFTGSTRV 192
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
24-244 |
1.11e-29 |
|
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: 115.38 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 24 GGEWVAPveGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAET 103
Cdd:cd07130 4 DGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 104 WDNGKA-------VRETIaaDIplCvdhfRYFAGCLRSQEGSM--AELDEHtvsyHLHE---PLGVVGQIIPWNFPLLMA 171
Cdd:cd07130 82 LEMGKIlpeglgeVQEMI--DI--C----DFAVGLSRQLYGLTipSERPGH----RMMEqwnPLGVVGVITAFNFPVAVW 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712421913 172 AWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDLL-----PAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07130 150 GWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLeknglPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAV 226
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
84-243 |
4.54e-29 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 112.91 E-value: 4.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 84 LLRIADRMEQNLELLAVAETWDNGKaVRETIAADIPLCVDHFRYFAGCLRSQEGSMAELD---EHTVSYHLhePLGVVGQ 160
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK-IQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 161 IIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSNRIAKIAFT 239
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
....
gi 1712421913 240 GSTA 243
Cdd:PRK10090 158 GSVS 161
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
19-244 |
1.14e-28 |
|
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: 113.04 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVApVEGdYMENISPV-TGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLEL 97
Cdd:TIGR01237 33 YPLVINGERVE-TEN-KIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 98 LAVAETWDNGKAVRETiAADIPLCVDHFRYFAGCLRSQEGSMAELD-EHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLG 176
Cdd:TIGR01237 111 FSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGKPVNSrEGETNQYVYTPTGVTVVISPWNFPFAIMVGMTV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712421913 177 PALAAGNCVVLKPAEQTPASILVLIE-LIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:TIGR01237 190 APIVTGNCVVLKPAEAAPVIAAKFVEiLEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREV 258
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
57-244 |
4.21e-28 |
|
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: 110.44 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 57 DIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRET------IAADIPLCVDHFRYFAG 130
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAqtevaaMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 131 clrSQEGSMAELDEHTVsyhlHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LP 209
Cdd:cd07095 81 ---ERATPMAQGRAVLR----HRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLP 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1712421913 210 AGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07095 154 PGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAAT 187
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-244 |
5.11e-27 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 108.04 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVA 101
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 102 ETWDNGKAVRET---IAADIPLcVDHFRYFAGCLRSQegSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPA 178
Cdd:TIGR01722 84 ITAEHGKTHSDAlgdVARGLEV-VEHACGVNSLLKGE--TSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 179 LAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPI 226
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
41-244 |
1.12e-26 |
|
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: 107.00 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 41 PVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAADIPL 120
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 121 CVDHFRYFAG----CLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAawkLGPALAA---GNCVVLKPAEQT 193
Cdd:cd07098 83 TCEKIRWTLKhgekALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNL---LGPIIAAlfaGNAIVVKVSEQV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 194 PASILVLIELIGDLL-----PAGVLNIVNGIGeEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07098 160 AWSSGFFLSIIRECLaacghDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPV 214
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
56-244 |
3.47e-24 |
|
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: 99.60 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 56 ADIELALDAAHAAKTAwGKTAA-AERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLR- 133
Cdd:cd07135 5 DEIDSIHSRLRATFRS-GKTKDlEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 134 -----SQEGSMAELDEHTVSYHlHEPLGVVGQIIPWNFPLLMAawkLGP---ALAAGNCVVLKPAEQTPASILVLIELIG 205
Cdd:cd07135 84 wakdeKVKDGPLAFMFGKPRIR-KEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAELVP 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1712421913 206 DLLPAGVLNIVNGIGEEAGQALASsnRIAKIAFTGSTAV 244
Cdd:cd07135 160 KYLDPDAFQVVQGGVPETTALLEQ--KFDKIFYTGSGRV 196
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
22-244 |
8.09e-24 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 99.14 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 22 FIGGEWVApvEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVA 101
Cdd:PLN02315 24 YVGGEWRA--NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 102 ETWDNGKAVRETIAaDIPLCVDHFRYFAGCLRSQEGSM--AELDEHTVsYHLHEPLGVVGQIIPWNFPLLMAAWKLGPAL 179
Cdd:PLN02315 102 VSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIipSERPNHMM-MEVWNPLGIVGVITAFNFPCAVLGWNACIAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 180 AAGNCVVLKPAEQTPASILVLIELIGDL-----LPAGVLNIVNGiGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:PLN02315 180 VCGNCVVWKGAPTTPLITIAMTKLVAEVleknnLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKV 248
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
62-244 |
5.04e-23 |
|
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: 96.40 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 62 LDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWD-NGKAVRETIAADIPLCVDHFRYfagCLRSQEGSMA 140
Cdd:cd07133 4 LERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADfGHRSRHETLLAEILPSIAGIKH---ARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 141 ELDEHT-------VSYHLHEPLGVVGQIIPWNFPLLMAawkLGP---ALAAGNCVVLKPAEQTPASILVLIELIGDLLPA 210
Cdd:cd07133 81 PSRRHVgllflpaKAEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 1712421913 211 GVLNIVNGiGEEAGQALaSSNRIAKIAFTGSTAV 244
Cdd:cd07133 158 DEVAVVTG-GADVAAAF-SSLPFDHLLFTGSTAV 189
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
148-244 |
6.23e-23 |
|
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: 96.06 E-value: 6.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 148 SYHLHEPLGVVGQIIPWNFPLLMAawkLGP---ALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAG 224
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVEGGVEVAT 170
|
90 100
....*....|....*....|
gi 1712421913 225 QALAssNRIAKIAFTGSTAV 244
Cdd:cd07087 171 ALLA--EPFDHIFFTGSPAV 188
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
19-240 |
6.24e-21 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 90.97 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 19 YENFIGGEWVAPVEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELL 98
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 99 AVAETWDNGKAVRETIAaDIPLCVDHFRYFA--GCLRSQEGSM--------AELDEHTVSYHLhePLGVVGQIIPWNFPL 168
Cdd:PLN00412 96 AECLVKEIAKPAKDAVT-EVVRSGDLISYTAeeGVRILGEGKFlvsdsfpgNERNKYCLTSKI--PLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712421913 169 LMAAWKLGPALAAGNCVVLKPAEQTPASILVLIE---LIGdlLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTG 240
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHcfhLAG--FPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG 245
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
59-244 |
3.33e-20 |
|
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: 88.45 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 59 ELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAADIPLCVDHFRYFAG-CLRSQEG 137
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIySYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 138 SMAEL--DEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGD--LLPAGVL 213
Cdd:cd07084 82 PGNHLgqGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDV 161
|
170 180 190
....*....|....*....|....*....|.
gi 1712421913 214 NIVNGIGeEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07084 162 TLINGDG-KTMQALLLHPNPKMVLFTGSSRV 191
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-241 |
9.97e-20 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 87.22 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 38 NISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAV---RETI 114
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPInqaRAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 115 AADIPLCvDHFRYFAGCLRSQEGSMAELDEHTVSYhlhEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTP 194
Cdd:PRK13968 91 AKSANLC-DWYAEHGPAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1712421913 195 ASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALaSSNRIAKIAFTGS 241
Cdd:PRK13968 167 GCAQLIAQVFKDAgIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGS 213
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
39-241 |
1.53e-19 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 86.72 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 39 ISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETiAADI 118
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-KAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 119 PLCVDHFRYFAG---CLRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPA 195
Cdd:PRK09406 85 LKCAKGFRYYAEhaeALLADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1712421913 196 SILVLIELIGDL-LPAGVLNIVNgIGEEAGQALASSNRIAKIAFTGS 241
Cdd:PRK09406 165 TALYLADLFRRAgFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGS 210
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
148-244 |
3.25e-19 |
|
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: 85.63 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 148 SYHLHEPLGVVGQIIPWNFPLLMAawkLGP---ALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAg 224
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVEGGVEEN- 169
|
90 100
....*....|....*....|
gi 1712421913 225 QALASSnRIAKIAFTGSTAV 244
Cdd:cd07136 170 QELLDQ-KFDYIFFTGSVRV 188
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
36-244 |
3.71e-19 |
|
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: 85.55 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 36 MENISPVTGEAFCEVPRSGAADIELALDAAHAA-KTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGK----AV 110
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALfLDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKplvdAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 111 RETIAA--DIPLCVDHFRYFAGclRSQEGSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLK 188
Cdd:cd07148 81 VEVTRAidGVELAADELGQLGG--REIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1712421913 189 PAEQTPASILVLIELIGDL-LPAGVLNIVnGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAgLPEGWCQAV-PCENAVAEKLVTDPRVAFFSFIGSARV 214
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
61-244 |
5.83e-18 |
|
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: 82.27 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 61 ALDAAHAAktAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRS----QE 136
Cdd:cd07134 5 AAQQAHAL--ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKwmkpKR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 137 GSMAELDEHTVSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIV 216
Cdd:cd07134 83 VRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVF 162
|
170 180
....*....|....*....|....*...
gi 1712421913 217 NGiGEEAGQALASSnRIAKIAFTGSTAV 244
Cdd:cd07134 163 EG-DAEVAQALLEL-PFDHIFFTGSPAV 188
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
148-244 |
7.51e-17 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 78.92 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 148 SYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGiGEEAGQAL 227
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEG-GVEVTTEL 181
|
90
....*....|....*..
gi 1712421913 228 ASSnRIAKIAFTGSTAV 244
Cdd:PTZ00381 182 LKE-PFDHIFFTGSPRV 197
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
23-244 |
1.99e-16 |
|
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: 78.01 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 23 IGGEWVAPVEGDYMENISPvTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNL--ELLAv 100
Cdd:cd07123 37 IGGKEVRTGNTGKQVMPHD-HAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYryELNA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 101 AETWDNGKAVRET-IAADIPLCvDHFR---YFAGCL------RSQEGSMAELDehtvsyhlHEPL-GVVGQIIPWNFPLL 169
Cdd:cd07123 115 ATMLGQGKNVWQAeIDAACELI-DFLRfnvKYAEELyaqqplSSPAGVWNRLE--------YRPLeGFVYAVSPFNFTAI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712421913 170 MAAWKLGPALAaGNCVVLKPAE-QTPASILVLIELIGDLLPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07123 186 GGNLAGAPALM-GNVVLWKPSDtAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPT 260
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
58-244 |
1.67e-15 |
|
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: 74.89 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 58 IELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNL-ELLAVAEtwdngkavRET------IAADIPLCVDHFRYFAG 130
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGdELVARAH--------AETglpearLQGELGRTTGQLRLFAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 131 CLRSQEGSMAELDE-----------HTVSYHLhePLGVVGQIIPWNFPLLM-------AAwklgpALAAGNCVVLKPAEQ 192
Cdd:cd07129 73 LVREGSWLDARIDPadpdrqplprpDLRRMLV--PLGPVAVFGASNFPLAFsvaggdtAS-----ALAAGCPVVVKAHPA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712421913 193 TPAsilvLIELIGDL---------LPAGVLNIVNGIGEEAGQALASSNRIAKIAFTGSTAV 244
Cdd:cd07129 146 HPG----TSELVARAiraalratgLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRG 202
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
63-244 |
7.20e-15 |
|
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: 73.02 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 63 DAAHAAKTAW--GKTAAAE-RANVLLRIADRMEQNLELLAVAETWDNGKAVRETIAADIPLCVDHFRYFAGCLRS----- 134
Cdd:cd07132 2 EAVRRAREAFssGKTRPLEfRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEwmkpe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 135 --QEGSMAELDEhtvSYHLHEPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGV 212
Cdd:cd07132 82 pvKKNLATLLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKEC 158
|
170 180 190
....*....|....*....|....*....|..
gi 1712421913 213 LNIVNGIGEEAGQALAssNRIAKIAFTGSTAV 244
Cdd:cd07132 159 YPVVLGGVEETTELLK--QRFDYIFYTGSTSV 188
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
153-244 |
3.24e-14 |
|
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: 71.29 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 153 EPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAGQALasSNR 232
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVPETTALL--EQK 177
|
90
....*....|..
gi 1712421913 233 IAKIAFTGSTAV 244
Cdd:cd07137 178 WDKIFFTGSPRV 189
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
153-244 |
8.22e-13 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 67.06 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 153 EPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGiGEEAGQALAsSNR 232
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEG-GPAVGEQLL-QHK 184
|
90
....*....|..
gi 1712421913 233 IAKIAFTGSTAV 244
Cdd:PLN02203 185 WDKIFFTGSPRV 196
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
153-244 |
3.99e-11 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 62.37 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 153 EPLGVVGQIIPWNFPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDLLPAGVLNIVNGIGEEAGQALasSNR 232
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90
....*....|..
gi 1712421913 233 IAKIAFTGSTAV 244
Cdd:PLN02174 189 WDKIFYTGSSKI 200
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
20-244 |
5.55e-10 |
|
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: 58.82 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 20 ENFIGGEWVAPvEGDYMENISPVTGEAFCEVpRSGAADIELALdaAHAAKTAWGKTAA---AERANVLLRIADR-MEQNL 95
Cdd:cd07128 2 QSYVAGQWHAG-TGDGRTLHDAVTGEVVARV-SSEGLDFAAAV--AYAREKGGPALRAltfHERAAMLKALAKYlMERKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 96 ELLAVAETwdNGkAVRETIAADIPLCVDHFRYFAGCLRSQ--------EGSMAEL--DEHTVSYHLHEPL-GVVGQIIPW 164
Cdd:cd07128 78 DLYALSAA--TG-ATRRDSWIDIDGGIGTLFAYASLGRRElpnahflvEGDVEPLskDGTFVGQHILTPRrGVAVHINAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 165 NFPllmaAW----KLGPALAAGNCVVLKPAEQTPASILVLIELIGD--LLPAGVLNIVNGigeEAGQALASSNRIAKIAF 238
Cdd:cd07128 155 NFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICG---SVGDLLDHLGEQDVVAF 227
|
....*.
gi 1712421913 239 TGSTAV 244
Cdd:cd07128 228 TGSAAT 233
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
18-241 |
1.52e-07 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 51.63 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 18 RYENFIGGEWVAPvEGDYMENISPVTGEAFCEVPRSG---AADIELALDAAHAAKTAWGktaAAERANVLLRIADRMEQN 94
Cdd:PRK11903 4 LLANYVAGRWQAG-SGAGTPLFDPVTGEELVRVSATGldlAAAFAFAREQGGAALRALT---YAQRAALLAAIVKVLQAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 95 LE-LLAVAETwdNGKAVRETIAADIPLCVDHFRYFAGCLRS-------QEGSMAEL--DEHTVSYHLHEPL-GVVGQIIP 163
Cdd:PRK11903 80 RDaYYDIATA--NSGTTRNDSAVDIDGGIFTLGYYAKLGAAlgdarllRDGEAVQLgkDPAFQGQHVLVPTrGVALFINA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 164 WNFPllmaAW----KLGPALAAGNCVVLKPAEQTPASILVLIELIGD--LLPAGVLNIVNGigeEAGQALASSNRIAKIA 237
Cdd:PRK11903 158 FNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAagILPAGALSVVCG---SSAGLLDHLQPFDVVS 230
|
....
gi 1712421913 238 FTGS 241
Cdd:PRK11903 231 FTGS 234
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
33-243 |
1.64e-06 |
|
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: 48.24 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 33 GDYMENISPVTGEAFCEVPRsgaADIELALDAAHAAKTAWGKTAAAERANVLLRIADRMEQNLELLAVAETWDNGKAVRE 112
Cdd:cd07127 64 GWVGGEVSPYGVELGVTYPQ---CDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 113 TIAADIPLCVDhfryfagclRSQEG------SMAELDEHTVsYHL----HEPLGV----------VGQII------PWN- 165
Cdd:cd07127 141 AFQAGGPHAQD---------RGLEAvayawrEMSRIPPTAE-WEKpqgkHDPLAMektftvvprgVALVIgcstfpTWNg 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 166 FPLLMAAwklgpaLAAGNCVVLKPAeqtPASIL-----------VLIELIGDllPAGVLNIVNGIGEEAGQALASSNRIA 234
Cdd:cd07127 211 YPGLFAS------LATGNPVIVKPH---PAAILplaitvqvareVLAEAGFD--PNLVTLAADTPEEPIAQTLATRPEVR 279
|
....*....
gi 1712421913 235 KIAFTGSTA 243
Cdd:cd07127 280 IIDFTGSNA 288
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
21-244 |
7.49e-05 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 43.25 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 21 NFIGGEWVApvEGDYMENISPVTGEAFCEVPRSGAADIELALDAAHAAKTAWGKTA--AAERANVLLRIADRMEQNLELL 98
Cdd:cd07126 1 NLVAGKWKG--ASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPlkNPERYLLYGDVSHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 99 AVAE------------TWDNGKA-VRETIAADIPLCVDHFRYFAgclRSQEGSMAELDEHTVSYHLhePLGVVGQIIPWN 165
Cdd:cd07126 79 EVEDffarliqrvapkSDAQALGeVVVTRKFLENFAGDQVRFLA---RSFNVPGDHQGQQSSGYRW--PYGPVAIITPFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712421913 166 FPLLMAAWKLGPALAAGNCVVLKPAEQTPASILVLIELIGDL-LPAGVLNIVNGIGEEAGQALASSN-RIakIAFTGSTA 243
Cdd:cd07126 154 FPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCgMPATDVDLIHSDGPTMNKILLEANpRM--TLFTGSSK 231
|
.
gi 1712421913 244 V 244
Cdd:cd07126 232 V 232
|
|
| |
