acetaldehyde dehydrogenase (acetylating); Members of this protein family are acetaldehyde ...
3-308
0e+00
acetaldehyde dehydrogenase (acetylating); Members of this protein family are acetaldehyde dehydrogenase (acetylating), EC 1.2.1.10. This enzyme oxidizes acetaldehyde, using NAD(+), and attaches coenzyme A (CoA), yielding acetyl-CoA. It occurs as a late step in the meta-cleavage pathways of a variety of compounds, including catechol, biphenyl, toluene, salicylate, etc.
Pssm-ID: 132259 [Multi-domain] Cd Length: 285 Bit Score: 500.69 E-value: 0e+00
Prokaryotic acetaldehyde dehydrogenase, dimerization; Members of this family are found in ...
131-284
4.14e-83
Prokaryotic acetaldehyde dehydrogenase, dimerization; Members of this family are found in prokaryotic acetaldehyde dehydrogenase (acylating), and adopt a structure consisting of an alpha-beta-alpha-beta(3) core. They mediate dimerization of the protein.
Pssm-ID: 430505 Cd Length: 138 Bit Score: 247.06 E-value: 4.14e-83
C-terminal catalytic domain of acetaldehyde dehydrogenase (ALDH) and similar proteins; ...
131-281
1.64e-63
C-terminal catalytic domain of acetaldehyde dehydrogenase (ALDH) and similar proteins; Acetaldehyde dehydrogenase (ALDH; EC 1.2.1.10), also called acetaldehyde dehydrogenase (acetylating), acylating acetaldehyde dehydrogenase, or aldehyde dehydrogenase (acylating), catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. It can also act on propanal and butanal to form propanoyl-CoA and butanoyl-CoA, respectively. ALDH is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols. NADP(+) can replace NAD(+) but the rate of reaction is much slower. ALDH contains two domains, an N-terminal Rossmann fold NAD+-binding domain and a C-terminal dimerization domain, which mediates dimerisation of the protein. The C-terminal dimerization domain is homologs to C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain. ALDHs are members of the GAPDH superfamily of proteins.
Pssm-ID: 467682 Cd Length: 135 Bit Score: 197.08 E-value: 1.64e-63
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
5-119
2.85e-16
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.
Pssm-ID: 214863 [Multi-domain] Cd Length: 123 Bit Score: 73.74 E-value: 2.85e-16
acetaldehyde dehydrogenase (acetylating); Members of this protein family are acetaldehyde ...
3-308
0e+00
acetaldehyde dehydrogenase (acetylating); Members of this protein family are acetaldehyde dehydrogenase (acetylating), EC 1.2.1.10. This enzyme oxidizes acetaldehyde, using NAD(+), and attaches coenzyme A (CoA), yielding acetyl-CoA. It occurs as a late step in the meta-cleavage pathways of a variety of compounds, including catechol, biphenyl, toluene, salicylate, etc.
Pssm-ID: 132259 [Multi-domain] Cd Length: 285 Bit Score: 500.69 E-value: 0e+00
Prokaryotic acetaldehyde dehydrogenase, dimerization; Members of this family are found in ...
131-284
4.14e-83
Prokaryotic acetaldehyde dehydrogenase, dimerization; Members of this family are found in prokaryotic acetaldehyde dehydrogenase (acylating), and adopt a structure consisting of an alpha-beta-alpha-beta(3) core. They mediate dimerization of the protein.
Pssm-ID: 430505 Cd Length: 138 Bit Score: 247.06 E-value: 4.14e-83
C-terminal catalytic domain of acetaldehyde dehydrogenase (ALDH) and similar proteins; ...
131-281
1.64e-63
C-terminal catalytic domain of acetaldehyde dehydrogenase (ALDH) and similar proteins; Acetaldehyde dehydrogenase (ALDH; EC 1.2.1.10), also called acetaldehyde dehydrogenase (acetylating), acylating acetaldehyde dehydrogenase, or aldehyde dehydrogenase (acylating), catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. It can also act on propanal and butanal to form propanoyl-CoA and butanoyl-CoA, respectively. ALDH is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols. NADP(+) can replace NAD(+) but the rate of reaction is much slower. ALDH contains two domains, an N-terminal Rossmann fold NAD+-binding domain and a C-terminal dimerization domain, which mediates dimerisation of the protein. The C-terminal dimerization domain is homologs to C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain. ALDHs are members of the GAPDH superfamily of proteins.
Pssm-ID: 467682 Cd Length: 135 Bit Score: 197.08 E-value: 1.64e-63
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
131-254
5.36e-21
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.
Pssm-ID: 467672 [Multi-domain] Cd Length: 166 Bit Score: 87.96 E-value: 5.36e-21
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
5-119
5.12e-18
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase
Pssm-ID: 426059 [Multi-domain] Cd Length: 121 Bit Score: 78.33 E-value: 5.12e-18
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
5-119
2.85e-16
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.
Pssm-ID: 214863 [Multi-domain] Cd Length: 123 Bit Score: 73.74 E-value: 2.85e-16
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
4-83
3.98e-04
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Pssm-ID: 426248 [Multi-domain] Cd Length: 120 Bit Score: 39.50 E-value: 3.98e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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