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)
TIGR00300 family protein; All members of the family come from genome projects. A partial ...
283-695
0e+00
TIGR00300 family protein; All members of the family come from genome projects. A partial length search brings in two plant lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzymes hitting the N-terminal region of the family. [Hypothetical proteins, Conserved]
Pssm-ID: 129401 [Multi-domain] Cd Length: 407 Bit Score: 594.49 E-value: 0e+00
Saccharopine dehydrogenase N-terminal domain; SDH N-terminal domain is named due to its ...
287-401
1.35e-42
Saccharopine dehydrogenase N-terminal domain; SDH N-terminal domain is named due to its appearance at the N-terminal of SDH in eukaryotes, but can be found C-terminal of the SDH-like domain in other enzymes, such as the bifunctional lysine ketoglutarate reductase/saccharopine dehydrogenase enzyme. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of a related structure.
Pssm-ID: 213387 [Multi-domain] Cd Length: 114 Bit Score: 149.60 E-value: 1.35e-42
LOR/SDH bifunctional enzyme conserved region; Lysine-oxoglutarate reductase/Saccharopine dehydrogenase (LOR/SDH) is a bifunctional enzyme. This conserved region is commonly found immediately N-terminal to Saccharop_dh (pfam03435) in eukaryotes.
Pssm-ID: 427960 [Multi-domain] Cd Length: 93 Bit Score: 136.42 E-value: 3.96e-38
N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G) ...
36-266
7.41e-11
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: 63.55 E-value: 7.41e-11
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
30-269
2.63e-09
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: 59.44 E-value: 2.63e-09
TIGR00300 family protein; All members of the family come from genome projects. A partial ...
283-695
0e+00
TIGR00300 family protein; All members of the family come from genome projects. A partial length search brings in two plant lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzymes hitting the N-terminal region of the family. [Hypothetical proteins, Conserved]
Pssm-ID: 129401 [Multi-domain] Cd Length: 407 Bit Score: 594.49 E-value: 0e+00
Saccharopine dehydrogenase N-terminal domain; SDH N-terminal domain is named due to its ...
287-401
1.35e-42
Saccharopine dehydrogenase N-terminal domain; SDH N-terminal domain is named due to its appearance at the N-terminal of SDH in eukaryotes, but can be found C-terminal of the SDH-like domain in other enzymes, such as the bifunctional lysine ketoglutarate reductase/saccharopine dehydrogenase enzyme. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of a related structure.
Pssm-ID: 213387 [Multi-domain] Cd Length: 114 Bit Score: 149.60 E-value: 1.35e-42
LOR/SDH bifunctional enzyme conserved region; Lysine-oxoglutarate reductase/Saccharopine dehydrogenase (LOR/SDH) is a bifunctional enzyme. This conserved region is commonly found immediately N-terminal to Saccharop_dh (pfam03435) in eukaryotes.
Pssm-ID: 427960 [Multi-domain] Cd Length: 93 Bit Score: 136.42 E-value: 3.96e-38
N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G) ...
36-266
7.41e-11
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: 63.55 E-value: 7.41e-11
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
30-269
2.63e-09
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: 59.44 E-value: 2.63e-09
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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