L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic ...
65-415
0e+00
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: 722.85 E-value: 0e+00
L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic ...
65-415
0e+00
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: 722.85 E-value: 0e+00
L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic ...
65-415
0e+00
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: 722.85 E-value: 0e+00
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
65-415
4.19e-170
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: 479.69 E-value: 4.19e-170
L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus (StrB1) and ...
66-421
3.58e-102
L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus (StrB1) and similar proteins; This subfamily includes inosamine-phosphate amidinotransferase (EC 2.1.4.2; also called inosamine amidinotransferase or inosamine-P amidinotransferase or scyllo-inosamine-4-phosphate amidinotransferase or L-arginine:inosamine phosphate amidinotransferase) from Streptomyces griseus (StrB1), among others. Inosamine-phosphate amidinotransferase catalyzes two non-consecutive transamidination reactions; it converts scyllo-inosamine 4-phosphate into N-amidino-scyllo-inosamine 4-phosphate, and N1-amidinostreptamine 6-phosphate into streptidine 6-phosphate. L-arginine:inosamine-phosphate amidinotransferase StrB1 is structurally similar to the human L-arginine:glycine amidinotransferase (AT), with residues involved in substrate binding and catalysis conserved in AT and StrB1 at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases. This subfamily also includes putative inosamine-phosphate amidinotransferase 2 (StrB2), also called aminocyclitol amidinotransferase or inosamine-phosphate amidinotransferase II, from Streptomyces glaucescens. It is unclear if StrB2 participates in streptomycin biosynthesis as it contains an arginine residue instead of the nucleophilic cysteine that is a key residue for amidine transfer.
Pssm-ID: 439147 Cd Length: 343 Bit Score: 307.43 E-value: 3.58e-102
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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