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)
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
4-304
2.79e-46
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: 158.82 E-value: 2.79e-46
Arginine deiminase; This family contains arginine deiminases, EC:3.5.3.6., enzymes that ...
80-303
4.67e-11
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: 62.78 E-value: 4.67e-11
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
4-304
2.79e-46
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: 158.82 E-value: 2.79e-46
Arginine deiminase; This family contains arginine deiminases, EC:3.5.3.6., enzymes that ...
80-303
4.67e-11
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: 62.78 E-value: 4.67e-11
L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic ...
4-298
2.83e-05
L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase or arginine-glycine amidinotransferase or arginine-glycine transamidinase or AT or AGAT) involved in creatine biosynthesis. L-arginine:glycine amidinotransferase (AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues, and may play a role in embryonic and central nervous system development and may be involved in the response to heart failure by elevating local creatine synthesis. This subfamily also contains bacterial proteins that include the virulence-associated protein HsvA from the fire blight pathogen Erwinia amylovora shown to be a polyamine amidinotransferase, and cyanobacterial SxtG, an amidinotransferase involved in the biosynthesis of paralytic shellfish toxins. The active sites of these enzymes are located in the core of the proteins at the base of a long, narrow substrate access channel. HsvA has a novel acceptor substrate specificity, with a clear preference for linear polyamines, especially putrescine and spermidine, as the amidino acceptor substrate. SxtG has a broad substrate promiscuity, operating on a wide variety of substrates and preferring alpha-amino ketones and alpha-amino methyl esters over alpha-amino acids.
Pssm-ID: 439148 Cd Length: 352 Bit Score: 44.90 E-value: 2.83e-05
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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