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Conserved domains on  [gi|20071875|gb|AAH26667|]
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Aldh1a3 protein, partial [Mus musculus]

Protein Classification

aldehyde dehydrogenase family protein( domain architecture ID 34081)

aldehyde dehydrogenase family protein is an NAD(P)(+)-dependent enzyme that may oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and may play an important role in detoxification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ALDH-SF super family cl11961
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 1-198 1.38e-144

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


The actual alignment was detected with superfamily member cd07141:

Pssm-ID: 448367  Cd Length: 481  Bit Score: 412.51  E-value: 1.38e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   1 EEGDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRY 80
Cdd:cd07141  39 QEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRY 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  81 FAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07141 119 YAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEA 198

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07141 199 GFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
 
Name Accession Description Interval E-value
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 1-198 1.38e-144

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: 412.51  E-value: 1.38e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   1 EEGDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRY 80
Cdd:cd07141  39 QEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRY 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  81 FAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07141 119 YAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEA 198

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07141 199 GFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 2-198 2.06e-97

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: 291.36  E-value: 2.06e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYF 81
Cdd:pfam00171  25 AATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG-EVDRAIDVLRYY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:pfam00171 101 AGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAG 180

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 20071875   162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:pfam00171 181 LPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAV 217
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 2-198 1.53e-94

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: 284.71  E-value: 1.53e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYF 81
Cdd:COG1012  39 AATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG-EVDRAADFLRYY 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:COG1012 115 AGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEA 194

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:COG1012 195 GLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAV 232
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 2-198 2.09e-89

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 273.22  E-value: 2.09e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    2 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:PLN02466  91 EGDAEDVNRAVAAARKAFDEG-PWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYY 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:PLN02466 170 AGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAG 249

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 20071875  162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PLN02466 250 LPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDT 286
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 2-197 4.64e-62

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 200.81  E-value: 4.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:TIGR01804  31 AATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQETIVADMDSGADVFEFF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:TIGR01804 108 AGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAG 187

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 20071875   162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 197
Cdd:TIGR01804 188 LPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVP 223
 
Name Accession Description Interval E-value
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 1-198 1.38e-144

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: 412.51  E-value: 1.38e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   1 EEGDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRY 80
Cdd:cd07141  39 QEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRY 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  81 FAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07141 119 YAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEA 198

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07141 199 GFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 2-198 1.53e-126

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: 366.15  E-value: 1.53e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07091  37 EADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAKGDVALSIKCLRYY 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07091 116 AGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAG 195

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07091 196 FPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAV 232
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
 4-198 8.99e-103

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: 305.87  E-value: 8.99e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFQrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAG 83
Cdd:cd07144  43 GEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAG 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  84 WADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFP 163
Cdd:cd07144 121 WADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFP 200

                       170       180       190
                ....*....|....*....|....*....|....*
gi 20071875 164 PGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07144 201 PGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 2-198 2.06e-97

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: 291.36  E-value: 2.06e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYF 81
Cdd:pfam00171  25 AATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG-EVDRAIDVLRYY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:pfam00171 101 AGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAG 180

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 20071875   162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:pfam00171 181 LPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAV 217
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
 2-198 2.91e-97

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: 291.71  E-value: 2.91e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07142  37 EGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARYAEVPLAARLFRYY 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07142 116 AGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAG 195

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07142 196 LPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEV 232
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
 2-198 3.35e-97

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: 291.74  E-value: 3.35e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQrgSPWRR-LDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRY 80
Cdd:cd07143  40 EATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRY 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  81 FAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07143 118 YGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEA 197

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07143 198 GFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLV 235
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 2-198 1.53e-94

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: 284.71  E-value: 1.53e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYF 81
Cdd:COG1012  39 AATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG-EVDRAADFLRYY 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:COG1012 115 AGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEA 194

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:COG1012 195 GLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAV 232
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
 2-198 2.06e-93

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: 280.98  E-value: 2.06e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFqRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYF 81
Cdd:cd07114  15 EASAADVDRAVAAARAAF-EGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL-IRETRAQVRYLAEWYRYY 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07114  93 AGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEA 172

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07114 173 GFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTET 210
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 2-198 2.09e-89

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 273.22  E-value: 2.09e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    2 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:PLN02466  91 EGDAEDVNRAVAAARKAFDEG-PWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYY 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:PLN02466 170 AGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAG 249

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 20071875  162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PLN02466 250 LPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDT 286
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 2-198 6.02e-88

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: 268.02  E-value: 6.02e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYF 81
Cdd:cd07119  31 EGTAEDAKRAIAAARRAFDSG-EWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEI-DIDDVANCFRYY 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07119 109 AGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAG 188

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07119 189 LPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTAT 225
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
 2-198 8.44e-88

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: 266.78  E-value: 8.44e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07112  20 ACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDVPSAANTFRWY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07112  99 AEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAG 178

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07112 179 LPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEV 215
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
 9-198 7.41e-87

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: 263.69  E-value: 7.41e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   9 DKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKI 88
Cdd:cd07078   1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  89 QGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVV 167
Cdd:cd07078  77 HGEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 20071875 168 NIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAV 187
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
 2-198 4.55e-86

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: 262.38  E-value: 4.55e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07115  15 QASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPRAADTFRYY 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07115  92 AGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAG 171

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07115 172 FPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAV 208
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 7-198 4.17e-84

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: 258.19  E-value: 4.17e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWAD 86
Cdd:cd07140  44 DVDRAVAAAKEAFENG-EWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCD 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQGRTIPTD----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGF 162
Cdd:cd07140 123 KIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGF 202

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20071875 163 PPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07140 203 PKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPI 238
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 13-198 7.18e-81

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: 246.37  E-value: 7.18e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  13 EAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKIQGRT 92
Cdd:cd06534   1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  93 IP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVP 171
Cdd:cd06534  77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156

                       170       180
                ....*....|....*....|....*..
gi 20071875 172 GFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAV 183
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
 2-197 6.03e-80

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: 246.71  E-value: 6.03e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07093  15 EGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRFF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07093  92 ADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAG 171

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 197
Cdd:cd07093 172 LPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETA 207
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 2-198 3.99e-79

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 245.89  E-value: 3.99e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    2 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:PLN02766  54 EGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYY 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:PLN02766 133 AGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAG 212

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 20071875  162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PLN02766 213 VPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEV 249
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
 3-198 1.06e-78

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: 243.30  E-value: 1.06e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFA 82
Cdd:cd07109  16 GGAADVDRAVQAARRAFESG--WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-ADVEAAARYFEYYG 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGF 162
Cdd:cd07109  93 GAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGL 172

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20071875 163 PPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07109 173 PAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVET 208
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 4-198 2.44e-76

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: 238.01  E-value: 2.44e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAG 83
Cdd:cd07559  36 TAEDVDLAVDAAHEAFKT---WGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAADIPLAIDHFRYFAG 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  84 WADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFP 163
Cdd:cd07559 113 VIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LP 191

                       170       180       190
                ....*....|....*....|....*....|....*
gi 20071875 164 PGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07559 192 KGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTV 226
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
 3-198 2.27e-71

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: 224.23  E-value: 2.27e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFA 82
Cdd:cd07103  16 AGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEVDYAASFLEWFA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07103  92 EEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAG 171

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07103 172 LPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAV 208
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 3-198 5.24e-70

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: 221.07  E-value: 5.24e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFA 82
Cdd:cd07110  16 ATAEDVDAAVRAARRAFPR---WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEAAWDVDDVAGCFEYYA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKI---QGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 158
Cdd:cd07110  92 DLAEQLdakAERAVPLPSEdFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAA 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20071875 159 EVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07110 172 EAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTAT 211
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
7-198 1.10e-69

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 220.55  E-value: 1.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWAD 86
Cdd:PRK13473  40 QVDAAVAAADAAFPE---WSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAAR 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   87 KIQGRTipTDDNVVCFT---RHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFP 163
Cdd:PRK13473 117 CLEGKA--AGEYLEGHTsmiRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LP 193

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 20071875  164 PGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PRK13473 194 PGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIAT 228
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
 3-198 6.37e-69

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 219.38  E-value: 6.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    3 GDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFA 82
Cdd:PRK09847  54 GKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   83 GWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGF 162
Cdd:PRK09847 133 EAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGL 212

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 20071875  163 PPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PRK09847 213 PDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRT 248
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
 2-198 2.87e-68

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: 216.42  E-value: 2.87e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07092  15 DASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRT----IPtddNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 157
Cdd:cd07092  92 AGAARTLEGPAageyLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELA 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20071875 158 KEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07092 169 AEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRT 208
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
 2-198 9.41e-68

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: 215.09  E-value: 9.41e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYF 81
Cdd:cd07106  15 VASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EVGGAVAWLRYT 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWAdkIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVg 161
Cdd:cd07106  91 ASLD--LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV- 167

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07106 168 LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTAT 203
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
 3-198 7.39e-67

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: 212.99  E-value: 7.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFA 82
Cdd:cd07108  16 SRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYFG 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgF 162
Cdd:cd07108  93 GLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-L 171

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20071875 163 PPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07108 172 PAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEV 207
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
 3-198 8.12e-67

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: 213.26  E-value: 8.12e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFA 82
Cdd:cd07097  34 ASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARG-EVTRAGQIFRYYA 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07097 110 GEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAG 189

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07097 190 LPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAV 226
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
 2-198 1.07e-66

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: 213.03  E-value: 1.07e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07111  55 QAEEEDVDAAVAAARTAFES---WSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHH 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQgrtipTDdnvvcFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07111 132 AGWAQLLD-----TE-----LAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAG 201

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07111 202 LPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEV 237
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
 7-198 1.60e-66

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: 212.70  E-value: 1.60e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWAD 86
Cdd:cd07117  39 DVDRAVKAAQEAFKT---WRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIR 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGV 166
Cdd:cd07117 116 AEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGV 194

                       170       180       190
                ....*....|....*....|....*....|..
gi 20071875 167 VNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07117 195 VNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEV 226
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 3-198 5.98e-66

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: 211.05  E-value: 5.98e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFA 82
Cdd:cd07131  34 STASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGR-GDVQEAIDMAQYAA 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07131 110 GEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAG 189

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07131 190 LPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEV 226
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
 1-197 1.36e-65

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: 209.81  E-value: 1.36e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   1 EEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRY 80
Cdd:cd07088  30 PAATAEDADRAVDAAEAA-QKA--WERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLAR-VEVEFTADYIDY 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  81 FAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKE 159
Cdd:cd07088 106 MAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDE 185

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 160 VGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 197
Cdd:cd07088 186 AGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTE 223
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
 7-198 1.77e-65

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: 209.47  E-value: 1.77e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWAD 86
Cdd:cd07090  20 DVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDIDSSADCLEYYAGLAP 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGV 166
Cdd:cd07090  96 TLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGV 175

                       170       180       190
                ....*....|....*....|....*....|..
gi 20071875 167 VNIVPGFGPTvGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07090 176 FNVVQGGGET-GQLLCEHPDVAKVSFTGSVPT 206
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
 4-198 2.30e-64

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: 206.92  E-value: 2.30e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAG 83
Cdd:cd07116  36 TAEDIELALDAAHAAKEA---WGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADIPLAIDHFRYFAG 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  84 WADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFP 163
Cdd:cd07116 113 CIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LP 191

                       170       180       190
                ....*....|....*....|....*....|....*
gi 20071875 164 PGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07116 192 PGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTT 226
PLN02467 PLN02467
betaine aldehyde dehydrogenase
 3-197 2.66e-63

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 204.97  E-value: 2.66e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    3 GDKPDVDKAVEAAQAAFQR--GSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF--VDLEGCiktF 78
Cdd:PLN02467  42 ATAEDVDAAVEAARKAFKRnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWdmDDVAGC---F 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   79 RYFAGWADKIQGR-----TIPtDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYL 153
Cdd:PLN02467 119 EYYADLAEALDAKqkapvSLP-METFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLEL 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20071875  154 ASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 197
Cdd:PLN02467 198 ADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTA 241
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 2-197 4.64e-62

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 200.81  E-value: 4.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:TIGR01804  31 AATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQETIVADMDSGADVFEFF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:TIGR01804 108 AGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAG 187

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 20071875   162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 197
Cdd:TIGR01804 188 LPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVP 223
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
 2-198 1.98e-61

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: 199.01  E-value: 1.98e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRGsPWRRlDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07089  15 DAGAADVDAAIAAARRAFDTG-DWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYF 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVC-----FTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASL 156
Cdd:cd07089  93 ADLADSFPWEFDLPVPALRGgpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEI 172

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20071875 157 IKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07089 173 IAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAV 214
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
 2-198 5.24e-61

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: 197.56  E-value: 5.24e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYF 81
Cdd:cd07118  15 EGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQAR-GEIEGAADLWRYA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07118  93 ASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRV 210
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
 2-198 8.00e-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: 197.34  E-value: 8.00e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07138  32 LGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAA 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVcftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07138 109 ADALKDFEFEERRGNSLVV----REPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAG 184

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07138 185 LPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA 221
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
 3-196 1.12e-60

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: 197.28  E-value: 1.12e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFA 82
Cdd:cd07113  34 ATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAFEVGQSANFLRYFA 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTI------PTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASL 156
Cdd:cd07113 112 GWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAEL 191

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20071875 157 IKEVGFPPGVVNIVPGFGpTVGAAISSHPQINKIAFTGST 196
Cdd:cd07113 192 AKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSV 230
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
 4-198 1.27e-60

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: 196.80  E-value: 1.27e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAG 83
Cdd:cd07145  19 SREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR-VEVERTIRLFKLAAE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  84 WADKIQGRTIPTDD-----NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 158
Cdd:cd07145  95 EAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILE 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20071875 159 EVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07145 175 EAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAV 214
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 1-197 1.88e-59

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 194.33  E-value: 1.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    1 EEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLV-ERDRAiLATLETMDTGKPFLHAFFVDLEGCIKTFR 79
Cdd:PRK13252  39 QAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDE-LAALETLDTGKPIQETSVVDIVTGADVLE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   80 YFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKE 159
Cdd:PRK13252 115 YYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTE 194

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 20071875  160 VGFPPGVVNIVPGFGpTVGAAISSHPQINKIAFTGSTE 197
Cdd:PRK13252 195 AGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVP 231
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
 2-196 4.07e-59

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: 192.98  E-value: 4.07e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYF 81
Cdd:cd07107  15 AASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAMLGDVMVAAALLDYF 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVg 161
Cdd:cd07107  91 AGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV- 169

                       170       180       190
                ....*....|....*....|....*....|....*
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGST 196
Cdd:cd07107 170 LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSV 204
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
 2-198 1.71e-58

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: 191.63  E-value: 1.71e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:cd07139  32 EATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYY 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADK---IQGRTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 158
Cdd:cd07139 111 AALARDfpfEERRPGSGGGHVL--VRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAE 188

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20071875 159 EVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07139 189 EAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAA 227
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
 5-198 2.59e-56

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 186.43  E-value: 2.59e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    5 KPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF--------FVDlegcik 76
Cdd:PLN02278  61 RAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIgevaygasFLE------ 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   77 tfrYFAGWADKIQGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLAS 155
Cdd:PLN02278 132 ---YFAEEAKRVYGDIIPSPFpDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAE 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 20071875  156 LIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PLN02278 209 LALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAV 251
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
 7-198 3.25e-56

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: 185.11  E-value: 3.25e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQRGspwRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWAD 86
Cdd:cd07149  22 DVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKP-IKDARKEVDRAIETLRLSAEEAK 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:cd07149  98 RLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAG 177

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07149 178 LPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAV 214
OH_muco_semi_DH TIGR03216
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ...
 2-196 3.40e-54

2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]


Pssm-ID: 132260  Cd Length: 481  Bit Score: 180.69  E-value: 3.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAfQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:TIGR03216  32 EAGAAEVDAAVAAARAA-LKG-PWGKMTVAERADLLYAVADEIERRFDDFLAAEVADTGKPRSLASHLDIPRGAANFRVF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AgwaDKIqgRTIPTD---------DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALY 152
Cdd:TIGR03216 110 A---DVV--KNAPTEcfematpdgKGALNYAVRKPLGVVGVISPWNLPLLLMTWKVGPALACGNTVVVKPSEETPGTATL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 20071875   153 LASLIKEVGFPPGVVNIVPGFGP-TVGAAISSHPQINKIAFTGST 196
Cdd:TIGR03216 185 LGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGET 229
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
 7-204 3.56e-53

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: 177.76  E-value: 3.56e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF-----FVDLegCIktfrYF 81
Cdd:cd07086  36 DVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLgevqeMIDI--CD----YA 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07086 107 VGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEV 186

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20071875 161 ----GFPPGVVNIVPGFGPtVGAAISSHPQINKIAFTGSTEV-------------RPLCEL 204
Cdd:cd07086 187 leknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVgrrvgetvarrfgRVLLEL 246
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
 3-198 8.89e-53

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: 177.41  E-value: 8.89e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFA 82
Cdd:cd07124  66 ATKEEAEAAVQAARAAFPT---WRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYA 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGF 162
Cdd:cd07124 142 REMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGL 221

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20071875 163 PPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07124 222 PPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREV 257
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
 7-198 2.17e-50

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: 169.63  E-value: 2.17e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWAD 86
Cdd:cd07104   1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLmLAWK-LAPALCCGNTVVLKPAEQTPLT-ALYLASLIKEVGFP 163
Cdd:cd07104  77 RPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLI-LAMRsVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLP 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 20071875 164 PGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAV 190
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
 3-198 2.27e-50

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: 169.82  E-value: 2.27e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFA 82
Cdd:cd07150  18 GSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF-ETTFTPELLRAAA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLmLAWK-LAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07150  94 GECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLI-LATKkVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEA 172

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 161 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07150 173 GLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAV 210
SSADH TIGR01780
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ...
 6-198 5.92e-50

succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]


Pssm-ID: 188167  Cd Length: 448  Bit Score: 168.76  E-value: 5.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     6 PDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAffvdlEGCIKT----FRYF 81
Cdd:TIGR01780  19 DETEAAIRAAYEAFKT---WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEA-----KGEILYaasfLEWF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGWADKIQGRTIPT--DDNVVCFTRhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKE 159
Cdd:TIGR01780  91 AEEAKRVYGDTIPSpqSDKRLIVIK-QPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSALALARLAEQ 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 20071875   160 VGFPPGVVNIVPG-FGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:TIGR01780 170 AGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNV 209
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
 2-198 8.19e-50

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: 168.68  E-value: 8.19e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFqRGSPWRRlDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYF 81
Cdd:cd07120  15 DGGVAEAEAAIAAARRAF-DETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARF-EISGAISELRYY 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  82 AGWADKIQGRTI-PTDDNVVCFTRhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:cd07120  92 AGLARTEAGRMIePEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEI 170

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20071875 161 -GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07120 171 pSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTAT 209
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
 4-198 3.97e-49

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: 166.84  E-value: 3.97e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAG 83
Cdd:cd07094  19 DRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-VEVDRAIDTLRLAAE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  84 WADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 158
Cdd:cd07094  95 EAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILV 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20071875 159 EVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07094 175 EAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAV 214
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 7-198 4.95e-47

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: 161.53  E-value: 4.95e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWAD 86
Cdd:cd07085  39 EVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPH 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPG 165
Cdd:cd07085 115 LLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDG 194

                       170       180       190
                ....*....|....*....|....*....|...
gi 20071875 166 VVNIVPGFGPTVGaAISSHPQINKIAFTGSTEV 198
Cdd:cd07085 195 VLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPV 226
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
 7-198 2.29e-44

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: 153.89  E-value: 2.29e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWAD 86
Cdd:cd07105   1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF-NVDLAAGMLREAASLIT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPG 165
Cdd:cd07105  77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20071875 166 VVNIV---PGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRV 192
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
2-198 1.10e-42

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 153.94  E-value: 1.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF-----FVDLegCik 76
Cdd:COG4230  589 EATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIaevreAVDF--C-- 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   77 tfRYFAGwadkiQGRTIPTDDnvvcfTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASL 156
Cdd:COG4230  662 --RYYAA-----QARRLFAAP-----TVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRL 729

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 20071875  157 IKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:COG4230  730 LHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTET 771
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
 4-198 2.61e-42

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: 148.87  E-value: 2.61e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAfQRGSpWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPflhaffvdLEGCIKTF----- 78
Cdd:cd07082  36 SALEILEAAETAYDA-GRGW-WPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT--------LKDALKEVdrtid 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  79 --RYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTAL 151
Cdd:cd07082 106 yiRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGI 185

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20071875 152 YLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07082 186 PLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEV 232
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
 4-198 6.92e-42

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 148.54  E-value: 6.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    4 DKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFA- 82
Cdd:PRK03137  71 TKELAEKAMQAALEAFET---WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEAD-ADTAEAIDFLEYYAr 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   83 ---GWADKIQGRTIPTDDNvvcFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKE 159
Cdd:PRK03137 147 qmlKLADGKPVESRPGEHN---RYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEE 223

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 20071875  160 VGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PRK03137 224 AGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREV 262
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
 3-198 7.23e-42

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: 147.39  E-value: 7.23e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFA 82
Cdd:cd07147  18 AGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG-EVARAIDTFRIAA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 157
Cdd:cd07147  94 EEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVL 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20071875 158 KEVGFPPGVVNIVPgfGPTVGAAI-SSHPQINKIAFTGSTEV 198
Cdd:cd07147 174 AETGLPKGAFSVLP--CSRDDADLlVTDERIKLLSFTGSPAV 213
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
2-198 3.32e-40

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 146.50  E-value: 3.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLH--------AffVDLeg 73
Cdd:PRK11904  581 FADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEANRAELIALCVREAGKT-LQdaiaevreA--VDF-- 652

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    74 CiktfRYFAGWADKIQGRTI----PT-DDNVVcftRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPL 148
Cdd:PRK11904  653 C----RYYAAQARRLFGAPEklpgPTgESNEL---RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPL 725

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 20071875   149 TALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PRK11904  726 IAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTET 775
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
 2-198 3.44e-40

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: 143.90  E-value: 3.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFlHAFFVDLEGCIKTFRYF 81
Cdd:TIGR01238  70 HANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTI-HNAIAEVREAVDFCRYY 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGWADKiqgrTIPTDDnvvcftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:TIGR01238 146 AKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAG 214

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 20071875   162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:TIGR01238 215 FPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEV 251
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
 7-198 5.08e-40

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: 142.43  E-value: 5.08e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWAD 86
Cdd:cd07152  14 DVDRAAARAAAA-QRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGF-EVGAAIGELHEAAGLPT 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTA-LYLASLIKEVGFPPG 165
Cdd:cd07152  90 QPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAG 169

                       170       180       190
                ....*....|....*....|....*....|...
gi 20071875 166 VVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07152 170 VLHVLPG-GADAGEALVEDPNVAMISFTGSTAV 201
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
10-198 9.12e-40

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 142.35  E-value: 9.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   10 KAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAffvdlEGCIKTFRYFAGW----A 85
Cdd:PRK11241  52 AAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEA-----KGEISYAASFIEWfaeeG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   86 DKIQGRTIP---TDDNVVCFTrhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGF 162
Cdd:PRK11241 124 KRIYGDTIPghqADKRLIVIK--QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGI 201

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 20071875  163 PPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PRK11241 202 PAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEI 237
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
 2-198 1.33e-39

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 145.01  E-value: 1.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF-----FVDlegcik 76
Cdd:PRK11905  586 EASAEDVERALAAAQAAFPE---WSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIaevreAVD------ 656

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    77 tF-RYFAGwadkiQGRTIPTDDnvvcftRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLAS 155
Cdd:PRK11905  657 -FlRYYAA-----QARRLLNGP------GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVR 724

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 20071875   156 LIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PRK11905  725 LLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEV 767
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
 4-198 1.78e-39

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: 142.33  E-value: 1.78e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF-----FVDLegCiktf 78
Cdd:cd07125  67 DAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADaevreAIDF--C---- 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  79 RYFAGWADKIQGRTI---PTD--DNVVCftrhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYL 153
Cdd:cd07125 138 RYYAAQARELFSDPElpgPTGelNGLEL----HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARA 213

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20071875 154 ASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07125 214 VELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTET 258
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
 13-198 2.65e-39

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: 140.57  E-value: 2.65e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  13 EAAQAAFQ-RGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGR 91
Cdd:cd07146  21 EALREALAlAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVGRAADVLRFAAAEALRDDGE 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  92 TIPTDDNV-----VCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGV 166
Cdd:cd07146 100 SFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDM 179

                       170       180       190
                ....*....|....*....|....*....|..
gi 20071875 167 VNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07146 180 LSVVTGEPGEIGDELITHPDVDLVTFTGGVAV 211
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
 37-197 9.13e-39

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 138.33  E-value: 9.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   37 LHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTD---DNVVCFTRhePIGVCGA 113
Cdd:PRK10090   1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  114 ITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFT 193
Cdd:PRK10090  78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157


                 ....
gi 20071875  194 GSTE 197
Cdd:PRK10090 158 GSVS 161
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
 4-196 1.37e-38

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: 138.89  E-value: 1.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAG 83
Cdd:cd07099  16 DPAEVAAAVARARAA-QRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEVLLALEAIDWAAR 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  84 WADKI-QGRTIPTDD---NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKE 159
Cdd:cd07099  92 NAPRVlAPRKVPTGLlmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAA 171

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20071875 160 VGFPPGVVNIVPGFGPTvGAAISSHPqINKIAFTGST 196
Cdd:cd07099 172 AGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSV 206
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
 2-197 2.17e-38

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 139.24  E-value: 2.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    2 EGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF--FVDLEGCIktfR 79
Cdd:PRK09407  50 VSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFeeVLDVALTA---R 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   80 YFAGWADKI------QGrTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYL 153
Cdd:PRK09407 124 YYARRAPKLlaprrrAG-ALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAA 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20071875  154 ASLIKEVGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTE 197
Cdd:PRK09407 201 VELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTA 242
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
 4-212 2.50e-38

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: 138.87  E-value: 2.50e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAG 83
Cdd:cd07083  53 DKAEAEAALEAAWAAFKT---WKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYAR 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  84 WADKIQGR-----TIPTDDNVvcfTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 158
Cdd:cd07083 129 AALRLRYPavevvPYPGEDNE---SFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFH 205

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20071875 159 EVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV-----RPLCELLPETTTAP 212
Cdd:cd07083 206 EAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETgkkiyEAAARLAPGQTWFK 264
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
 8-196 6.87e-38

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: 136.44  E-value: 6.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   8 VDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF-VDLegCIKTFRYFAGWAD 86
Cdd:cd07100   1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEK--CAWICRYYAENAE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 K-IQGRTIPTDDNVvCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPG 165
Cdd:cd07100  76 AfLADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154

                       170       180       190
                ....*....|....*....|....*....|.
gi 20071875 166 VVNIVPGFGPTVGAAIsSHPQINKIAFTGST 196
Cdd:cd07100 155 VFQNLLIDSDQVEAII-ADPRVRGVTLTGSE 184
D1pyr5carbox2 TIGR01237
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...
 7-198 5.39e-37

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: 135.38  E-value: 5.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWAD 86
Cdd:TIGR01237  70 HAEHALQAAAKAFEA---WKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEAD-AEVAEAIDFMEYYARQMI 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    87 KIQGR----TIPTDDNVVCFTrhePIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGF 162
Cdd:TIGR01237 146 ELAKGkpvnSREGETNQYVYT---PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGL 222

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 20071875   163 PPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:TIGR01237 223 PKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREV 258
aldehy_Rv0768 TIGR04284
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ...
 2-196 1.43e-36

aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275104  Cd Length: 480  Bit Score: 133.74  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFQRgSPWRRLDALsRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYF 81
Cdd:TIGR04284  33 DATAADMDAAIAAARRAFDE-TDWSRDTAL-RVRCLRQLRDALRAHVEELRELTIAEVGAPRMLTAGAQLEGPVDDLGFA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGWADKIQGRT---------IPTDDNVvcftRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALY 152
Cdd:TIGR04284 111 ADLAESYAWTTdlgvaspmgIPTRRTL----RREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAV 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 20071875   153 LASLIKE-VGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGST 196
Cdd:TIGR04284 187 LGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGST 231
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
 3-198 1.57e-36

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: 133.58  E-value: 1.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   3 GDKPDVDKAVEAAQAAfQRgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFA 82
Cdd:cd07151  29 ASKEDVDEAYRAAAAA-QK--EWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI-EWGAAMAITREAA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 GWADKIQGRTIPTD----DNVVcftRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTA-LYLASLI 157
Cdd:cd07151 105 TFPLRMEGRILPSDvpgkENRV---YREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGgLLLAKIF 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20071875 158 KEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07151 182 EEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPV 222
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
 2-196 4.05e-35

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: 129.35  E-value: 4.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF--FVDlegCIKTFR 79
Cdd:cd07101  14 QSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFeeVLD---VAIVAR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  80 YFAGWADKI-----QGRTIPT-DDNVVCftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYL 153
Cdd:cd07101  88 YYARRAERLlkprrRRGAIPVlTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWA 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20071875 154 ASLIKEVGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGST 196
Cdd:cd07101 165 VELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGST 205
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
 7-198 5.53e-35

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 131.63  E-value: 5.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     7 DVDKAVEAAQAAfqrGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF-----FVDLegciktFRYF 81
Cdd:PRK11809  683 EVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIaevreAVDF------LRYY 753

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGwadkiQGRTIPTDDNvvcftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG 161
Cdd:PRK11809  754 AG-----QVRDDFDNDT------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAG 822

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 20071875   162 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PRK11809  823 VPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEV 859
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 7-198 1.18e-34

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: 127.77  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF--------VDLEgcIKTF 78
Cdd:cd07095   1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  79 RYFAGwadkiqGRTIPTDdNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 158
Cdd:cd07095  76 HERTG------ERATPMA-QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20071875 159 EVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07095 149 EAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAAT 187
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
 2-198 2.32e-33

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: 125.01  E-value: 2.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF-----FVDLegCik 76
Cdd:cd07130  30 QATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLgevqeMIDI--C-- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  77 tfRYFAGWADKIQGRTIPTD--DNVVCFTRHePIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLA 154
Cdd:cd07130 103 --DFAVGLSRQLYGLTIPSErpGHRMMEQWN-PLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVT 179

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20071875 155 SLIKEV----GFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07130 180 KIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAV 226
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
 4-195 1.39e-32

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: 122.74  E-value: 1.39e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQ-LADLVERDRAILATLETMdTGKPFLHAffvdlEGCIKTF---- 78
Cdd:cd07102  16 SLEAVRAALERARAA-QKG--WRAVPLEERKAIVTRaVELLAANTDEIAEELTWQ-MGRPIAQA-----GGEIRGMlera 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  79 RYFAGWADK-IQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 157
Cdd:cd07102  87 RYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAF 166

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20071875 158 KEVGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGS 195
Cdd:cd07102 167 AEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGS 203
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
 7-195 1.79e-29

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 114.67  E-value: 1.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    7 DVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAffvdlegciKTfrYFAGWAD 86
Cdd:PRK09457  38 QVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEA---------AT--EVTAMIN 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   87 KI-------QGRT----IPTDDNVVCFtRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLAS 155
Cdd:PRK09457 104 KIaisiqayHERTgekrSEMADGAAVL-RHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVK 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20071875  156 LIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGS 195
Cdd:PRK09457 183 LWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGS 221
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
 7-198 5.08e-28

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: 110.47  E-value: 5.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvdleGCIKTFryfagwAD 86
Cdd:cd07098  19 DVDEAIAAARAAQRE---WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL----GEILVT------CE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  87 KIQ-----G----RTIPTDDNVVCFTR-----HEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALY 152
Cdd:cd07098  86 KIRwtlkhGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGF 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20071875 153 LASLIKEV----GFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07098 166 FLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPV 214
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
 2-198 9.49e-28

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: 109.59  E-value: 9.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875     2 EGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYF 81
Cdd:TIGR01722  34 FASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALG-DVARGLEVVEHA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    82 AGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:TIGR01722 110 CGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEA 189

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 20071875   161 GFPPGVVNIVPGFGPTVGaAISSHPQINKIAFTGSTEV 198
Cdd:TIGR01722 190 GAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPI 226
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
 7-195 4.42e-26

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 104.82  E-value: 4.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWAD 86
Cdd:PRK09406  24 EVDAAIARAHARFRD---YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALKCAKGFRYYAEHAE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   87 KIQGRTiPTDDNVV----CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGF 162
Cdd:PRK09406 100 ALLADE-PADAAAVgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGF 178

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 20071875  163 PPGVVNIVpgfgpTVGA----AISSHPQINKIAFTGS 195
Cdd:PRK09406 179 PDGCFQTL-----LVGSgaveAILRDPRVAAATLTGS 210
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
 7-194 6.02e-25

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 102.14  E-value: 6.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    7 DVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF-----VDL------EGCi 75
Cdd:PLN00412  54 EVNKAMESAKAA-QKA--WAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTevvrsGDLisytaeEGV- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   76 ktfRYFAgwadkiQGRTIPTDD------NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLT 149
Cdd:PLN00412 130 ---RILG------EGKFLVSDSfpgnerNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVA 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 20071875  150 ALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTG 194
Cdd:PLN00412 201 ALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG 245
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
 11-195 6.05e-25

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 102.52  E-value: 6.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   11 AVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKIQG 90
Cdd:PLN02419 156 AVSAAKQAFPL---WRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMG 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   91 RTIPTDDNVV-CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNI 169
Cdd:PLN02419 232 EYLPNVSNGVdTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNI 311

                        170       180
                 ....*....|....*....|....*.
gi 20071875  170 VPGFGPTVGaAISSHPQINKIAFTGS 195
Cdd:PLN02419 312 VHGTNDTVN-AICDDEDIRAVSFVGS 336
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
 4-198 3.31e-24

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: 99.80  E-value: 3.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFQRGSPWrrLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAG 83
Cdd:cd07148  19 DWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK-VEVTRAIDGVELAAD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  84 WADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 158
Cdd:cd07148  96 ELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLH 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20071875 159 EVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07148 176 EAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARV 214
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
 11-198 2.34e-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: 96.83  E-value: 2.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  11 AVEAAQAAFQRGS----PWRR--LDALSRGqllhqladLVERDRAILATLETmDTGKPFLHAFFVDLEGCIKTFRY---- 80
Cdd:cd07087   3 LVARLRETFLTGKtrslEWRKaqLKALKRM--------LTENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGEIDHalkh 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  81 FAGWADKiqgRTIPTDDNVV---CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 157
Cdd:cd07087  74 LKKWMKP---RRVSVPLLLQpakAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20071875 158 KEVgFPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEV 198
Cdd:cd07087 151 PKY-FDPEAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAV 188
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
 2-198 2.76e-23

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: 97.27  E-value: 2.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   2 EGDKPDVDKAVEAAQAAfqRGSpWRRLDALSRGQLLHQLADLVE---RDRAILATLetMDTGKPFLHAffvdlE---GC- 74
Cdd:cd07123  65 YADAALVEKAIEAALEA--RKE-WARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKNVWQA-----EidaACe 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  75 -IKTFRYFAGWADKI-QGRTIPTDDNVVCFTRHEPI-GVCGAITPWNFPLLMLAWKLAPALCcGNTVVLKPAEQTPLTAL 151
Cdd:cd07123 135 lIDFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNY 213

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20071875 152 YLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07123 214 LVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPT 260
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
 14-198 1.55e-21

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: 91.92  E-value: 1.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  14 AAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfvDLEGCIKTFRYFA--GWADKIQGR 91
Cdd:cd07084   4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE--NICGDQVQLRARAfvIYSYRIPHE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  92 TIPTDDNVVCFTRHE---PIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG-FPPGVV 167
Cdd:cd07084  82 PGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161

                       170       180       190
                ....*....|....*....|....*....|.
gi 20071875 168 NIVPGFGPTvGAAISSHPQINKIAFTGSTEV 198
Cdd:cd07084 162 TLINGDGKT-MQALLLHPNPKMVLFTGSSRV 191
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
 7-198 2.19e-20

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: 88.82  E-value: 2.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   7 DVDKAVEAAQAAFQRGS----PWRRldalsrgQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFA 82
Cdd:cd07135   6 EIDSIHSRLRATFRSGKtkdlEYRL-------WQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHML 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 G----WA-DKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 157
Cdd:cd07135  79 KnlkkWAkDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELV 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20071875 158 KEvGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEV 198
Cdd:cd07135 159 PK-YLDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRV 196
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
 104-198 1.50e-19

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: 86.38  E-value: 1.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875 104 RHEPIGVCGAITPWNFPlLMLAwkLAP---ALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 180
Cdd:cd07133  98 EYQPLGVVGIIVPWNYP-LYLA--LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GADVAAA 172

                        90
                ....*....|....*...
gi 20071875 181 ISSHPqINKIAFTGSTEV 198
Cdd:cd07133 173 FSSLP-FDHLLFTGSTAV 189
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
 101-198 2.10e-19

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: 85.74  E-value: 2.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875 101 CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 180
Cdd:cd07134  94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQA 171

                        90
                ....*....|....*...
gi 20071875 181 ISSHPqINKIAFTGSTEV 198
Cdd:cd07134 172 LLELP-FDHIFFTGSPAV 188
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
 13-198 3.22e-19

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 85.66  E-value: 3.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   13 EAAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKpFLHAFFVDLEGCIKTFRYFAGWADKIQGRT 92
Cdd:PLN02315  60 EGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSI 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   93 IPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVV 167
Cdd:PLN02315 139 IPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIF 218

                        170       180       190
                 ....*....|....*....|....*....|.
gi 20071875  168 NIVPGfGPTVGAAISSHPQINKIAFTGSTEV 198
Cdd:PLN02315 219 TSFCG-GAEIGEAIAKDTRIPLVSFTGSSKV 248
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
 6-198 1.08e-17

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: 80.92  E-value: 1.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   6 PDVDKAVEAAQAAFQRGSPWRRldalsrgQLLHQLADLV-ERDRAILATLETmDTGKPFLHAFF----VDLEGCIKTFRY 80
Cdd:cd07137   3 RLVRELRETFRSGRTRSAEWRK-------SQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRdevsVLVSSCKLAIKE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  81 FAGWAD----KIQGRTIPTDDNVVCftrhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASL 156
Cdd:cd07137  75 LKKWMApekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20071875 157 IKEVgFPPGVVNIVPGfGPTVGAAISSHpQINKIAFTGSTEV 198
Cdd:cd07137 151 IPEY-LDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRV 189
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
 106-198 2.36e-16

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: 77.16  E-value: 2.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875 106 EPIGVCGAITPWNFPLLMLawkLAP---ALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAAIS 182
Cdd:cd07136  99 EPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELL 173

                        90
                ....*....|....*.
gi 20071875 183 SHPqINKIAFTGSTEV 198
Cdd:cd07136 174 DQK-FDYIFFTGSVRV 188
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 101-198 2.60e-16

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 76.99  E-value: 2.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  101 CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 180
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180

                         90
                 ....*....|....*...
gi 20071875  181 ISSHPqINKIAFTGSTEV 198
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRV 197
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 10-157 1.84e-14

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: 71.48  E-value: 1.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  10 KAVEAAQAAFQRGspwRRLDALSRGQLLHQLADLV-ERDRAILATLEtMDTGKPFLHAFFVDLEGCIKTFRY----FAGW 84
Cdd:cd07132   2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEW 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20071875  85 A-DKIQGRTIPT--DDnvvCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 157
Cdd:cd07132  78 MkPEPVKKNLATllDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI 150
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
 8-204 1.91e-12

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: 65.64  E-value: 1.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   8 VDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFlhaffVDLEGCI-KT---FRYFA- 82
Cdd:cd07129   1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPE-----ARLQGELgRTtgqLRLFAd 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  83 -----GWADKI------QGRTIPTDDNVVCFTRHEPIGVCGAItpwNFPLlmlAWKL-----APALCCGNTVVLKPAEQT 146
Cdd:cd07129  73 lvregSWLDARidpadpDRQPLPRPDLRRMLVPLGPVAVFGAS---NFPL---AFSVaggdtASALAAGCPVVVKAHPAH 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20071875 147 PLTALYLASLIKEV----GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV-RPLCEL 204
Cdd:cd07129 147 PGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGgRALFDA 209
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
 7-195 2.16e-12

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 65.65  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875    7 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVeRDRAI-LATLETMDTGKPFLHAffvdlEGCIKTFRYFAGWA 85
Cdd:PRK13968  30 DIENALQLAAAGFRD---WRETNIDYRAQKLRDIGKAL-RARSEeMAQMITREMGKPINQA-----RAEVAKSANLCDWY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   86 DKiQG----RTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:PRK13968 101 AE-HGpamlKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDA 179

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 20071875  161 GFPPGVVNIVPGFGPTVGAAISShPQINKIAFTGS 195
Cdd:PRK13968 180 GIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGS 213
PLN02203 PLN02203
aldehyde dehydrogenase
 106-198 1.63e-11

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 63.21  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  106 EPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAAISSHP 185
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHK 184

                         90
                 ....*....|...
gi 20071875  186 QiNKIAFTGSTEV 198
Cdd:PLN02203 185 W-DKIFFTGSPRV 196
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
14-197 2.16e-10

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 59.72  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   14 AAQAAFQR---GSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQG 90
Cdd:PRK11903  43 AAAFAFAReqgGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGD 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   91 RTIPTDDNVVCFTRHEPI----------GVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 160
Cdd:PRK11903 122 ARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAA 201

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 20071875  161 G-FPPGVVNIVPGfgptVGAAISSHPQ-INKIAFTGSTE 197
Cdd:PRK11903 202 GiLPAGALSVVCG----SSAGLLDHLQpFDVVSFTGSAE 236
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
 58-198 2.98e-10

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 59.29  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   58 DTGKPFLHAFFVD---LEGCIK-TFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALC 133
Cdd:PLN02174  59 DLGKPELESSVYEvslLRNSIKlALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAIS 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20071875  134 CGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISShpQINKIAFTGSTEV 198
Cdd:PLN02174 139 AGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ--KWDKIFYTGSSKI 200
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
 33-198 4.56e-10

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 58.77  E-value: 4.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  33 RGQLLHQLADLVERDRAILATLETMDTGKPF--LHAFFVDLEGCIK--------TFRYFAGWADKIQGRTIPtdDNVVCF 102
Cdd:cd07077  18 RDLIINAIANALYDTRQRLASEAVSERGAYIrsLIANWIAMMGCSEsklyknidTERGITASVGHIQDVLLP--DNGETY 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875 103 TRHEPIGVCGAITPWNFPLLMLAwKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV---GFPPGVVNIVPGFGPTVGA 179
Cdd:cd07077  96 VRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAE 174

                       170
                ....*....|....*....
gi 20071875 180 AISSHPQINKIAFTGSTEV 198
Cdd:cd07077 175 ELLSHPKIDLIVATGGRDA 193
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
 107-198 2.38e-06

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: 47.88  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875 107 PIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAIS-SHP 185
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANP 221

                        90
                ....*....|...
gi 20071875 186 QInkIAFTGSTEV 198
Cdd:cd07126 222 RM--TLFTGSSKV 232
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
 13-172 3.75e-05

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: 44.18  E-value: 3.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  13 EAAQAAFQRGSP-WRRLDALSRGQLLHQLAD-LVERDRAILATleTMDTGKPFLHAFfVDLEGCIKTFRYFAGwadkiQG 90
Cdd:cd07128  40 AAVAYAREKGGPaLRALTFHERAAMLKALAKyLMERKEDLYAL--SAATGATRRDSW-IDIDGGIGTLFAYAS-----LG 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  91 RTIPTDDNV-------------------VCFTRHepiGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTAL 151
Cdd:cd07128 112 RRELPNAHFlvegdveplskdgtfvgqhILTPRR---GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTE 188

                       170       180
                ....*....|....*....|..
gi 20071875 152 YLASLIKEVG-FPPGVVNIVPG 172
Cdd:cd07128 189 AVVKDIVESGlLPEGALQLICG 210
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
 4-196 1.16e-03

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: 39.38  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875   4 DKPDVDKAVEAAQAAFQRgspWRRLDALSR-GQLLHQLADLVERDRAIL-ATLETmdTGKPFLHAFFVD----LEGCIKT 77
Cdd:cd07127  82 PQCDPDALLAAARAAMPG---WRDAGARARaGVCLEILQRLNARSFEMAhAVMHT--TGQAFMMAFQAGgphaQDRGLEA 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071875  78 FRYfagwADKIQGRTIPTDDNVVCFTRHEPI-----------GV-----CGAITPWN-FPLLMlawklaPALCCGNTVVL 140
Cdd:cd07127 157 VAY----AWREMSRIPPTAEWEKPQGKHDPLamektftvvprGValvigCSTFPTWNgYPGLF------ASLATGNPVIV 226

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20071875 141 KPAeqtPLTALYLASLIK-------EVGFPPGVVNIV---PGFGptVGAAISSHPQINKIAFTGST 196
Cdd:cd07127 227 KPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSN 287
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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