dimethylarginine dimethylaminohydrolase (DdaH) family protein similar to Pseudomonas aeruginosa N(G),N(G)-dimethylarginine dimethylaminohydrolase that hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA)
N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G) ...
38-269
3.05e-15
N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G)-dimethylarginine dimethylaminohydrolases (DDAH) from eukaryotes. It also includes arginine deiminases and DDAH from prokaryotes. These enzymes are involved in arginine metabolism and belong to the amidinotransferase (AT) superfamily as they share the alpha/beta propeller fold, which includes structurally important residues (buried hydrophobic residues, buried hydrophilic residues hydrogen-bonded with mainchain groups and the hallmark of three consecutive buried Gly residues near the C-terminus, conserved among its members.
Pssm-ID: 437252 [Multi-domain] Cd Length: 288 Bit Score: 73.95 E-value: 3.05e-15
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
37-267
2.87e-07
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar proteins; This family contains amidinotransferase enzymes known to catalyze the transfer of the amidino group from a donor molecule (usually arginine) to an acceptor molecule bearing a primary amine. They are widespread in nature, occurring in essential metabolic pathways in eukaryotes as well as in biosynthetic pathways for antibiotics and virulence factors in prokaryotes. This family includes L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase, arginine-glycine amidinotransferase, or arginine-glycine transamidinase), inosamine-phosphate amidinotransferase (EC 2.1.4.2; also called inosamine amidinotransferase, inosamine-P amidinotransferase, or scyllo-inosamine-4-phosphate amidinotransferase or L-arginine:inosamine phosphate amidinotransferase), and similar proteins. L-arginine:glycine amidinotransferase (AT or AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Inosamine-phosphate amidinotransferases catalyze two nonconsecutive transamidination reactions in the biosynthesis of the streptomycin family of antibiotics. This family also includes L-arginine:inosamine-phosphate Streptomyces griseus amidinotransferase StrB1, which is structurally similar to human L-arginine:glycine amidinotransferase; AT and StrB1 share conserved residues involved in substrate binding and catalysis at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases.
Pssm-ID: 439146 Cd Length: 336 Bit Score: 50.96 E-value: 2.87e-07
N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G) ...
38-269
3.05e-15
N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G)-dimethylarginine dimethylaminohydrolases (DDAH) from eukaryotes. It also includes arginine deiminases and DDAH from prokaryotes. These enzymes are involved in arginine metabolism and belong to the amidinotransferase (AT) superfamily as they share the alpha/beta propeller fold, which includes structurally important residues (buried hydrophobic residues, buried hydrophilic residues hydrogen-bonded with mainchain groups and the hallmark of three consecutive buried Gly residues near the C-terminus, conserved among its members.
Pssm-ID: 437252 [Multi-domain] Cd Length: 288 Bit Score: 73.95 E-value: 3.05e-15
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
37-267
2.87e-07
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar proteins; This family contains amidinotransferase enzymes known to catalyze the transfer of the amidino group from a donor molecule (usually arginine) to an acceptor molecule bearing a primary amine. They are widespread in nature, occurring in essential metabolic pathways in eukaryotes as well as in biosynthetic pathways for antibiotics and virulence factors in prokaryotes. This family includes L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase, arginine-glycine amidinotransferase, or arginine-glycine transamidinase), inosamine-phosphate amidinotransferase (EC 2.1.4.2; also called inosamine amidinotransferase, inosamine-P amidinotransferase, or scyllo-inosamine-4-phosphate amidinotransferase or L-arginine:inosamine phosphate amidinotransferase), and similar proteins. L-arginine:glycine amidinotransferase (AT or AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Inosamine-phosphate amidinotransferases catalyze two nonconsecutive transamidination reactions in the biosynthesis of the streptomycin family of antibiotics. This family also includes L-arginine:inosamine-phosphate Streptomyces griseus amidinotransferase StrB1, which is structurally similar to human L-arginine:glycine amidinotransferase; AT and StrB1 share conserved residues involved in substrate binding and catalysis at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases.
Pssm-ID: 439146 Cd Length: 336 Bit Score: 50.96 E-value: 2.87e-07
Arginine deiminase; This family contains arginine deiminases, EC:3.5.3.6., enzymes that ...
125-271
3.75e-03
Arginine deiminase; This family contains arginine deiminases, EC:3.5.3.6., enzymes that catalyze the reaction: arginine + H2O <=> citrulline + NH3. These enzymes belong to the amidinotranferase (AT) superfamily, which share the alpha/beta fold including structurally important residues, i.e buried hydrophobic residues, buried hydrophilic residues hydrogen-bonded with mainchain groups and a structural hallmark of three consecutive buried Gly residues near the C-terminus, conserved among these proteins.
Pssm-ID: 426693 Cd Length: 377 Bit Score: 38.13 E-value: 3.75e-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.
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