hydantoinase/oxoprolinase family protein may be involved in the hydrolysis of 5-membered rings via hydrolysis of their internal imide bonds, similar to the alpha and gamma subunits of Aromatoleum aromaticum acetophenone carboxylase, which catalyzes the carboxylation of acetophenone to form benzoylacetate in the anaerobic catabolism of ethylbenzene
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport ...
3-454
6.27e-41
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
The actual alignment was detected with superfamily member COG0145:
Pssm-ID: 439915 [Multi-domain] Cd Length: 678 Bit Score: 157.17 E-value: 6.27e-41
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport ...
3-454
6.27e-41
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 439915 [Multi-domain] Cd Length: 678 Bit Score: 157.17 E-value: 6.27e-41
Hydantoinase/oxoprolinase; This family includes the enzymes hydantoinase and oxoprolinase EC:3. ...
178-454
1.26e-36
Hydantoinase/oxoprolinase; This family includes the enzymes hydantoinase and oxoprolinase EC:3.5.2.9. Both reactions involve the hydrolysis of 5-membered rings via hydrolysis of their internal imide bonds.
Pssm-ID: 396517 [Multi-domain] Cd Length: 288 Bit Score: 137.80 E-value: 1.26e-36
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
2-55
1.30e-03
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 41.38 E-value: 1.30e-03
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport ...
3-454
6.27e-41
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 439915 [Multi-domain] Cd Length: 678 Bit Score: 157.17 E-value: 6.27e-41
Hydantoinase/oxoprolinase; This family includes the enzymes hydantoinase and oxoprolinase EC:3. ...
178-454
1.26e-36
Hydantoinase/oxoprolinase; This family includes the enzymes hydantoinase and oxoprolinase EC:3.5.2.9. Both reactions involve the hydrolysis of 5-membered rings via hydrolysis of their internal imide bonds.
Pssm-ID: 396517 [Multi-domain] Cd Length: 288 Bit Score: 137.80 E-value: 1.26e-36
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
2-55
1.30e-03
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 41.38 E-value: 1.30e-03
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
1-62
2.58e-03
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 40.26 E-value: 2.58e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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