mitochondrial 10-formyltetrahydrofolate dehydrogenase isoform X3 [Homo sapiens]
Protein Classification
acyl carrier protein( domain architecture ID 10171317)
acyl carrier protein may function as a carrier of the growing fatty acid chain in fatty acid biosynthesis or as the carrier of activated (amino) acid groups in polyketide synthases and non-ribosomal peptide synthases
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| FMT_core_FDH_N | cd08647 | 10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
23-225 | 5.05e-151 | ||||
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain. : Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 433.41 E-value: 5.05e-151
|
||||||||
| ALDH-SF super family | cl11961 | NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
439-621 | 1.19e-121 | ||||
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 cd07140: Pssm-ID: 448367 [Multi-domain] Cd Length: 486 Bit Score: 369.13 E-value: 1.19e-121
|
||||||||
| FDH_Hydrolase_C | cd08703 | The C-terminal subdomain of the hydrolase domain on the bi-functional protein ... |
228-327 | 1.23e-53 | ||||
The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding. : Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 178.31 E-value: 1.23e-53
|
||||||||
| PP-binding | pfam00550 | Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
346-390 | 3.02e-04 | ||||
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine. : Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 39.08 E-value: 3.02e-04
|
||||||||
| Name | Accession | Description | Interval | E-value | |||||
| FMT_core_FDH_N | cd08647 | 10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
23-225 | 5.05e-151 | |||||
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain. Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 433.41 E-value: 5.05e-151
|
|||||||||
| ALDH_F1L_FTFDH | cd07140 | 10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
439-621 | 1.19e-121 | |||||
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: 369.13 E-value: 1.19e-121
|
|||||||||
| Fmt | COG0223 | Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
23-327 | 1.86e-78 | |||||
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 251.18 E-value: 1.86e-78
|
|||||||||
| Formyl_trans_N | pfam00551 | Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
23-202 | 6.25e-55 | |||||
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function. Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 184.80 E-value: 6.25e-55
|
|||||||||
| AdhE | COG1012 | Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
438-620 | 3.36e-54 | |||||
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: 191.88 E-value: 3.36e-54
|
|||||||||
| FDH_Hydrolase_C | cd08703 | The C-terminal subdomain of the hydrolase domain on the bi-functional protein ... |
228-327 | 1.23e-53 | |||||
The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding. Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 178.31 E-value: 1.23e-53
|
|||||||||
| fmt | TIGR00460 | methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
23-330 | 9.25e-51 | |||||
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 177.98 E-value: 9.25e-51
|
|||||||||
| Aldedh | pfam00171 | Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
454-620 | 9.99e-51 | |||||
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: 181.96 E-value: 9.99e-51
|
|||||||||
| PLN02766 | PLN02766 | coniferyl-aldehyde dehydrogenase |
431-621 | 6.46e-48 | |||||
coniferyl-aldehyde dehydrogenase Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 175.39 E-value: 6.46e-48
|
|||||||||
| BADH | TIGR01804 | betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
446-621 | 9.87e-37 | |||||
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: 143.03 E-value: 9.87e-37
|
|||||||||
| PRK06988 | PRK06988 | formyltransferase; |
112-326 | 3.40e-26 | |||||
formyltransferase; Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 109.40 E-value: 3.40e-26
|
|||||||||
| Formyl_trans_C | pfam02911 | Formyl transferase, C-terminal domain; |
227-327 | 1.81e-21 | |||||
Formyl transferase, C-terminal domain; Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 89.26 E-value: 1.81e-21
|
|||||||||
| PP-binding | pfam00550 | Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
346-390 | 3.02e-04 | |||||
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine. Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 39.08 E-value: 3.02e-04
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| FMT_core_FDH_N | cd08647 | 10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
23-225 | 5.05e-151 | |||||
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain. Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 433.41 E-value: 5.05e-151
|
|||||||||
| ALDH_F1L_FTFDH | cd07140 | 10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
439-621 | 1.19e-121 | |||||
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: 369.13 E-value: 1.19e-121
|
|||||||||
| ALDH_F1-2_Ald2-like | cd07091 | ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
441-621 | 2.85e-80 | |||||
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: 261.37 E-value: 2.85e-80
|
|||||||||
| Fmt | COG0223 | Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
23-327 | 1.86e-78 | |||||
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 251.18 E-value: 1.86e-78
|
|||||||||
| ALDH_F1AB_F2_RALDH1 | cd07141 | NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
439-621 | 1.31e-57 | |||||
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: 201.42 E-value: 1.31e-57
|
|||||||||
| ALDH_ALD2-YMR170C | cd07144 | Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
439-621 | 1.48e-57 | |||||
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: 201.10 E-value: 1.48e-57
|
|||||||||
| ALDH_F2BC | cd07142 | Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
442-621 | 7.73e-56 | |||||
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: 196.56 E-value: 7.73e-56
|
|||||||||
| Formyl_trans_N | pfam00551 | Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
23-202 | 6.25e-55 | |||||
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function. Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 184.80 E-value: 6.25e-55
|
|||||||||
| AdhE | COG1012 | Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
438-620 | 3.36e-54 | |||||
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: 191.88 E-value: 3.36e-54
|
|||||||||
| FDH_Hydrolase_C | cd08703 | The C-terminal subdomain of the hydrolase domain on the bi-functional protein ... |
228-327 | 1.23e-53 | |||||
The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding. Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 178.31 E-value: 1.23e-53
|
|||||||||
| fmt | TIGR00460 | methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
23-330 | 9.25e-51 | |||||
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 177.98 E-value: 9.25e-51
|
|||||||||
| Aldedh | pfam00171 | Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
454-620 | 9.99e-51 | |||||
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: 181.96 E-value: 9.99e-51
|
|||||||||
| ALDH_AldA_AN0554 | cd07143 | Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
439-621 | 1.08e-50 | |||||
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: 182.34 E-value: 1.08e-50
|
|||||||||
| ALDH_BADH-GbsA | cd07119 | Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
446-621 | 2.21e-50 | |||||
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: 181.74 E-value: 2.21e-50
|
|||||||||
| ALDH_DhaS | cd07114 | Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
462-622 | 6.39e-50 | |||||
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: 179.67 E-value: 6.39e-50
|
|||||||||
| FMT_core | cd08369 | Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
25-204 | 8.30e-49 | |||||
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis. Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 167.85 E-value: 8.30e-49
|
|||||||||
| PLN02766 | PLN02766 | coniferyl-aldehyde dehydrogenase |
431-621 | 6.46e-48 | |||||
coniferyl-aldehyde dehydrogenase Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 175.39 E-value: 6.46e-48
|
|||||||||
| PLN02466 | PLN02466 | aldehyde dehydrogenase family 2 member |
439-621 | 3.27e-47 | |||||
aldehyde dehydrogenase family 2 member Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 174.23 E-value: 3.27e-47
|
|||||||||
| FMT_core_Met-tRNA-FMT_N | cd08646 | Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
23-222 | 8.91e-46 | |||||
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 160.69 E-value: 8.91e-46
|
|||||||||
| ALDH_HMSADH_HapE | cd07115 | Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
462-621 | 2.30e-45 | |||||
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: 167.23 E-value: 2.30e-45
|
|||||||||
| FMT_core_like_2 | cd08822 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
23-223 | 4.54e-45 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 158.39 E-value: 4.54e-45
|
|||||||||
| ALDH_GABALDH-PuuC | cd07112 | Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
457-622 | 1.78e-43 | |||||
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: 162.00 E-value: 1.78e-43
|
|||||||||
| ALDH | cd07078 | NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
497-621 | 9.72e-42 | |||||
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: 156.60 E-value: 9.72e-42
|
|||||||||
| ALDH-SF | cd06534 | NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
497-621 | 1.22e-39 | |||||
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: 148.92 E-value: 1.22e-39
|
|||||||||
| ALDH_ACDHII_AcoD-like | cd07559 | Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
443-620 | 9.80e-39 | |||||
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: 149.03 E-value: 9.80e-39
|
|||||||||
| ALDH_PADH_NahF | cd07113 | Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
446-621 | 5.47e-38 | |||||
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: 146.82 E-value: 5.47e-38
|
|||||||||
| PRK13473 | PRK13473 | aminobutyraldehyde dehydrogenase; |
441-620 | 1.22e-37 | |||||
aminobutyraldehyde dehydrogenase; Pssm-ID: 237391 Cd Length: 475 Bit Score: 145.82 E-value: 1.22e-37
|
|||||||||
| BADH | TIGR01804 | betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
446-621 | 9.87e-37 | |||||
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: 143.03 E-value: 9.87e-37
|
|||||||||
| PRK13252 | PRK13252 | betaine aldehyde dehydrogenase; Provisional |
438-621 | 4.82e-36 | |||||
betaine aldehyde dehydrogenase; Provisional Pssm-ID: 183918 Cd Length: 488 Bit Score: 141.56 E-value: 4.82e-36
|
|||||||||
| ALDH_F8_HMSADH | cd07093 | Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
462-620 | 2.78e-35 | |||||
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: 138.85 E-value: 2.78e-35
|
|||||||||
| ALDH_F9_TMBADH | cd07090 | NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
462-621 | 1.43e-34 | |||||
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: 136.67 E-value: 1.43e-34
|
|||||||||
| ALDH_AAS00426 | cd07109 | Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
463-622 | 3.00e-34 | |||||
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: 135.82 E-value: 3.00e-34
|
|||||||||
| ALDH_MGR_2402 | cd07108 | Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
462-622 | 5.35e-34 | |||||
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: 135.18 E-value: 5.35e-34
|
|||||||||
| ALDH_AldA-Rv0768 | cd07139 | Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
446-620 | 5.46e-34 | |||||
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: 135.40 E-value: 5.46e-34
|
|||||||||
| ALDH_StaphAldA1 | cd07117 | Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
443-620 | 6.76e-34 | |||||
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: 134.89 E-value: 6.76e-34
|
|||||||||
| PRK09847 | PRK09847 | gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
446-621 | 1.98e-33 | |||||
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 133.87 E-value: 1.98e-33
|
|||||||||
| ALDH_F16 | cd07111 | Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
446-620 | 2.74e-33 | |||||
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: 133.29 E-value: 2.74e-33
|
|||||||||
| ALDH_F5_SSADH_GabD | cd07103 | Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
463-620 | 3.06e-33 | |||||
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: 132.56 E-value: 3.06e-33
|
|||||||||
| ALDH_LactADH-AldA | cd07088 | Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
446-622 | 3.13e-33 | |||||
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: 133.16 E-value: 3.13e-33
|
|||||||||
| ALDH_ACDHII-AcoD | cd07116 | Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
443-621 | 6.66e-33 | |||||
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: 132.19 E-value: 6.66e-33
|
|||||||||
| ALDH_ABALDH-YdcW | cd07092 | Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
463-620 | 2.06e-32 | |||||
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: 130.14 E-value: 2.06e-32
|
|||||||||
| ALDH_KGSADH-YcbD | cd07097 | Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
446-622 | 1.03e-31 | |||||
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: 128.52 E-value: 1.03e-31
|
|||||||||
| ALDH_PhdK-like | cd07107 | Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
462-620 | 4.96e-30 | |||||
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: 123.25 E-value: 4.96e-30
|
|||||||||
| PLN02278 | PLN02278 | succinic semialdehyde dehydrogenase |
444-621 | 1.79e-28 | |||||
succinic semialdehyde dehydrogenase Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 119.41 E-value: 1.79e-28
|
|||||||||
| ALDH_AldH-CAJ73105 | cd07131 | Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
446-622 | 7.81e-27 | |||||
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: 114.37 E-value: 7.81e-27
|
|||||||||
| PRK06988 | PRK06988 | formyltransferase; |
112-326 | 3.40e-26 | |||||
formyltransferase; Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 109.40 E-value: 3.40e-26
|
|||||||||
| FMT_core_like_4 | cd08651 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
24-205 | 8.22e-26 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 104.66 E-value: 8.22e-26
|
|||||||||
| ALDH_CddD-AldA-like | cd07089 | Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
463-622 | 1.06e-25 | |||||
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: 110.41 E-value: 1.06e-25
|
|||||||||
| PLN02467 | PLN02467 | betaine aldehyde dehydrogenase |
444-621 | 1.44e-25 | |||||
betaine aldehyde dehydrogenase Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 110.59 E-value: 1.44e-25
|
|||||||||
| ALDH_F7_AASADH-like | cd07086 | NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
445-622 | 1.81e-24 | |||||
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: 106.88 E-value: 1.81e-24
|
|||||||||
| ALDH_CddD_SSP0762 | cd07138 | Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
446-621 | 1.91e-24 | |||||
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: 106.82 E-value: 1.91e-24
|
|||||||||
| ALDH_F10_BADH | cd07110 | Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
462-621 | 3.26e-24 | |||||
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: 105.90 E-value: 3.26e-24
|
|||||||||
| gabD | PRK11241 | NADP-dependent succinate-semialdehyde dehydrogenase I; |
444-620 | 1.67e-23 | |||||
NADP-dependent succinate-semialdehyde dehydrogenase I; Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 104.22 E-value: 1.67e-23
|
|||||||||
| ALDH_F6_MMSDH | cd07085 | Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
446-620 | 2.06e-23 | |||||
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: 103.75 E-value: 2.06e-23
|
|||||||||
| ALDH_SNDH | cd07118 | Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
493-621 | 3.42e-23 | |||||
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: 102.80 E-value: 3.42e-23
|
|||||||||
| PLN02285 | PLN02285 | methionyl-tRNA formyltransferase |
48-326 | 4.44e-23 | |||||
methionyl-tRNA formyltransferase Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 100.54 E-value: 4.44e-23
|
|||||||||
| ALDH_BenzADH-like | cd07104 | ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
497-622 | 2.23e-22 | |||||
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: 100.30 E-value: 2.23e-22
|
|||||||||
| ALDH_PsfA-ACA09737 | cd07120 | Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
462-620 | 5.13e-22 | |||||
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: 99.34 E-value: 5.13e-22
|
|||||||||
| ALDH_LactADH_F420-Bios | cd07145 | Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
461-619 | 1.74e-21 | |||||
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: 97.80 E-value: 1.74e-21
|
|||||||||
| Formyl_trans_C | pfam02911 | Formyl transferase, C-terminal domain; |
227-327 | 1.81e-21 | |||||
Formyl transferase, C-terminal domain; Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 89.26 E-value: 1.81e-21
|
|||||||||
| ALDH_F21_LactADH-like | cd07094 | ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
461-620 | 5.39e-21 | |||||
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: 96.35 E-value: 5.39e-21
|
|||||||||
| PRK08125 | PRK08125 | bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
115-325 | 6.64e-21 | |||||
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA; Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 96.98 E-value: 6.64e-21
|
|||||||||
| ALDH_y4uC | cd07149 | Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
460-620 | 6.94e-21 | |||||
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: 95.74 E-value: 6.94e-21
|
|||||||||
| ALDH_VaniDH_like | cd07150 | Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
460-620 | 8.19e-21 | |||||
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: 95.47 E-value: 8.19e-21
|
|||||||||
| FMT_core_ArnA_N | cd08644 | ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
39-224 | 1.24e-20 | |||||
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle. Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 90.48 E-value: 1.24e-20
|
|||||||||
| ALDH_AldA-AAD23400 | cd07106 | Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
498-620 | 7.79e-20 | |||||
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: 92.59 E-value: 7.79e-20
|
|||||||||
| PurN | COG0299 | Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
47-209 | 1.67e-19 | |||||
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 87.01 E-value: 1.67e-19
|
|||||||||
| ALDH_PutA-P5CDH-RocA | cd07124 | Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
443-622 | 3.07e-19 | |||||
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: 91.13 E-value: 3.07e-19
|
|||||||||
| ALDH_HBenzADH | cd07151 | NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
449-622 | 1.87e-18 | |||||
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: 88.52 E-value: 1.87e-18
|
|||||||||
| ALDH_F21_RNP123 | cd07147 | Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
460-620 | 9.22e-18 | |||||
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: 86.15 E-value: 9.22e-18
|
|||||||||
| ALDH_SaliADH | cd07105 | Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
497-618 | 5.37e-17 | |||||
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: 83.78 E-value: 5.37e-17
|
|||||||||
| Met_tRNA_FMT_C | cd08704 | C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ... |
229-323 | 1.39e-16 | |||||
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding. Pssm-ID: 187732 [Multi-domain] Cd Length: 87 Bit Score: 74.87 E-value: 1.39e-16
|
|||||||||
| ALDH_PutA-P5CDH | cd07125 | Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
445-620 | 1.54e-16 | |||||
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: 82.63 E-value: 1.54e-16
|
|||||||||
| ALDH_F11_NP-GAPDH | cd07082 | NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
443-620 | 1.62e-16 | |||||
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: 82.62 E-value: 1.62e-16
|
|||||||||
| ALDH_BenzADH | cd07152 | NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
497-619 | 2.41e-16 | |||||
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: 81.96 E-value: 2.41e-16
|
|||||||||
| ALDH_DDALDH | cd07099 | Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
497-621 | 2.24e-15 | |||||
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: 78.80 E-value: 2.24e-15
|
|||||||||
| ALDH_PhpJ | cd07146 | Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
499-621 | 4.62e-15 | |||||
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: 77.78 E-value: 4.62e-15
|
|||||||||
| FMT_core_like_3 | cd08653 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
90-202 | 9.35e-15 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 71.86 E-value: 9.35e-15
|
|||||||||
| ALDH_P5CDH | cd07083 | ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
443-622 | 4.18e-14 | |||||
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: 74.92 E-value: 4.18e-14
|
|||||||||
| ALDH_SSADH1_GabD1 | cd07100 | Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
497-620 | 6.56e-14 | |||||
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: 74.03 E-value: 6.56e-14
|
|||||||||
| FMT_core_GART | cd08645 | Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
128-198 | 7.54e-14 | |||||
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities. Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 70.11 E-value: 7.54e-14
|
|||||||||
| PRK10090 | PRK10090 | aldehyde dehydrogenase A; Provisional |
510-622 | 8.49e-14 | |||||
aldehyde dehydrogenase A; Provisional Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 73.62 E-value: 8.49e-14
|
|||||||||
| ALDH_F7_AASADH | cd07130 | NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
457-620 | 1.92e-13 | |||||
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: 73.01 E-value: 1.92e-13
|
|||||||||
| ALDH_F15-22 | cd07098 | Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
497-621 | 3.89e-13 | |||||
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: 71.95 E-value: 3.89e-13
|
|||||||||
| PRK03137 | PRK03137 | 1-pyrroline-5-carboxylate dehydrogenase; Provisional |
443-622 | 6.57e-13 | |||||
1-pyrroline-5-carboxylate dehydrogenase; Provisional Pssm-ID: 179543 Cd Length: 514 Bit Score: 71.50 E-value: 6.57e-13
|
|||||||||
| FMT_core_NRPS_like | cd08649 | N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
40-181 | 9.07e-13 | |||||
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins. Pssm-ID: 187718 [Multi-domain] Cd Length: 166 Bit Score: 66.51 E-value: 9.07e-13
|
|||||||||
| ALDH_SSADH2_GabD2 | cd07101 | Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
497-619 | 1.36e-12 | |||||
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: 70.03 E-value: 1.36e-12
|
|||||||||
| FMT_core_HypX_N | cd08650 | HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ... |
35-206 | 2.66e-12 | |||||
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain. Pssm-ID: 187719 [Multi-domain] Cd Length: 151 Bit Score: 64.95 E-value: 2.66e-12
|
|||||||||
| FMT_core_like_5 | cd08823 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
106-206 | 2.70e-12 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 65.54 E-value: 2.70e-12
|
|||||||||
| D1pyr5carbox3 | TIGR01238 | delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
415-621 | 6.10e-12 | |||||
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: 68.40 E-value: 6.10e-12
|
|||||||||
| PLN02419 | PLN02419 | methylmalonate-semialdehyde dehydrogenase [acylating] |
446-621 | 1.33e-11 | |||||
methylmalonate-semialdehyde dehydrogenase [acylating] Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 67.46 E-value: 1.33e-11
|
|||||||||
| PurN | TIGR00639 | phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
128-208 | 1.36e-11 | |||||
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 63.93 E-value: 1.36e-11
|
|||||||||
| gabD2 | PRK09407 | succinic semialdehyde dehydrogenase; Reviewed |
497-619 | 1.71e-11 | |||||
succinic semialdehyde dehydrogenase; Reviewed Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 66.83 E-value: 1.71e-11
|
|||||||||
| ALDH_EDX86601 | cd07102 | Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
463-620 | 2.04e-11 | |||||
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: 66.50 E-value: 2.04e-11
|
|||||||||
| PRK11905 | PRK11905 | bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
453-621 | 6.97e-11 | |||||
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 65.66 E-value: 6.97e-11
|
|||||||||
| gabD1 | PRK09406 | succinic semialdehyde dehydrogenase; Reviewed |
462-620 | 1.33e-10 | |||||
succinic semialdehyde dehydrogenase; Reviewed Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 63.99 E-value: 1.33e-10
|
|||||||||
| ALDH_F3-13-14_CALDH-like | cd07087 | ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
512-619 | 1.58e-10 | |||||
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: 63.31 E-value: 1.58e-10
|
|||||||||
| PutA2 | COG4230 | Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
498-620 | 4.00e-10 | |||||
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 63.03 E-value: 4.00e-10
|
|||||||||
| ALDH_RL0313 | cd07148 | Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
461-622 | 1.18e-09 | |||||
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: 60.90 E-value: 1.18e-09
|
|||||||||
| PRK11904 | PRK11904 | bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
446-620 | 1.19e-09 | |||||
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 61.37 E-value: 1.19e-09
|
|||||||||
| ALDH_F14-YMR110C | cd07135 | Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
578-619 | 6.61e-09 | |||||
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: 58.39 E-value: 6.61e-09
|
|||||||||
| putA | PRK11809 | trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
505-621 | 7.71e-09 | |||||
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 58.83 E-value: 7.71e-09
|
|||||||||
| PTZ00381 | PTZ00381 | aldehyde dehydrogenase family protein; Provisional |
578-619 | 1.59e-08 | |||||
aldehyde dehydrogenase family protein; Provisional Pssm-ID: 240392 Cd Length: 493 Bit Score: 57.35 E-value: 1.59e-08
|
|||||||||
| PRK07579 | PRK07579 | dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
108-256 | 2.06e-08 | |||||
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 55.29 E-value: 2.06e-08
|
|||||||||
| ALDH_F3AB | cd07132 | Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
572-619 | 3.70e-08 | |||||
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: 56.08 E-value: 3.70e-08
|
|||||||||
| FMT_core_like_6 | cd08820 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
107-203 | 4.84e-08 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 53.21 E-value: 4.84e-08
|
|||||||||
| ALDH_YwdH-P39616 | cd07136 | Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
579-619 | 5.27e-08 | |||||
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: 55.59 E-value: 5.27e-08
|
|||||||||
| PLN02315 | PLN02315 | aldehyde dehydrogenase family 7 member |
445-620 | 5.33e-08 | |||||
aldehyde dehydrogenase family 7 member Pssm-ID: 177949 Cd Length: 508 Bit Score: 55.61 E-value: 5.33e-08
|
|||||||||
| ALDH_AlkH-like | cd07134 | Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
583-619 | 1.03e-07 | |||||
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: 54.54 E-value: 1.03e-07
|
|||||||||
| ALDH_KGSADH-like | cd07084 | ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
496-621 | 1.76e-07 | |||||
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: 53.78 E-value: 1.76e-07
|
|||||||||
| ALDH_CALDH_CalB | cd07133 | Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
503-619 | 4.17e-07 | |||||
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: 52.87 E-value: 4.17e-07
|
|||||||||
| PLN02331 | PLN02331 | phosphoribosylglycinamide formyltransferase |
68-200 | 7.75e-07 | |||||
phosphoribosylglycinamide formyltransferase Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 50.08 E-value: 7.75e-07
|
|||||||||
| Arna_FMT_C | cd08702 | C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ... |
229-320 | 1.06e-06 | |||||
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex. Pssm-ID: 187730 Cd Length: 92 Bit Score: 47.23 E-value: 1.06e-06
|
|||||||||
| ALDH_SGSD_AstD | cd07095 | N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
497-619 | 1.07e-06 | |||||
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: 51.50 E-value: 1.07e-06
|
|||||||||
| PLN00412 | PLN00412 | NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
443-619 | 1.64e-06 | |||||
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 50.91 E-value: 1.64e-06
|
|||||||||
| PRK13968 | PRK13968 | putative succinate semialdehyde dehydrogenase; Provisional |
462-620 | 3.15e-05 | |||||
putative succinate semialdehyde dehydrogenase; Provisional Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 46.78 E-value: 3.15e-05
|
|||||||||
| ALDH_F3FHI | cd07137 | Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
583-621 | 5.14e-05 | |||||
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: 45.86 E-value: 5.14e-05
|
|||||||||
| astD | PRK09457 | succinylglutamic semialdehyde dehydrogenase; Reviewed |
446-619 | 1.91e-04 | |||||
succinylglutamic semialdehyde dehydrogenase; Reviewed Pssm-ID: 181873 Cd Length: 487 Bit Score: 44.18 E-value: 1.91e-04
|
|||||||||
| FMT_core_like_1 | cd08821 | Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
106-247 | 2.58e-04 | |||||
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme. Pssm-ID: 187723 [Multi-domain] Cd Length: 211 Bit Score: 42.69 E-value: 2.58e-04
|
|||||||||
| PP-binding | pfam00550 | Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
346-390 | 3.02e-04 | |||||
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine. Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 39.08 E-value: 3.02e-04
|
|||||||||
| PLN02174 | PLN02174 | aldehyde dehydrogenase family 3 member H1 |
583-621 | 1.79e-03 | |||||
aldehyde dehydrogenase family 3 member H1 Pssm-ID: 177831 Cd Length: 484 Bit Score: 41.18 E-value: 1.79e-03
|
|||||||||
| PLN02203 | PLN02203 | aldehyde dehydrogenase |
583-621 | 3.21e-03 | |||||
aldehyde dehydrogenase Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 40.48 E-value: 3.21e-03
|
|||||||||
| Blast search parameters | ||||
|
