1XVA
METHYLTRANSFERASE
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | d1xvaa_ | Alpha and beta proteins (a/b) | S-adenosyl-L-methionine-dependent methyltransferases | S-adenosyl-L-methionine-dependent methyltransferases | Glycine N-methyltransferase | Glycine N-methyltransferase | (Escherichia coli ) [TaxId: 562 ], | SCOPe (2.08) |
B | d1xvab_ | Alpha and beta proteins (a/b) | S-adenosyl-L-methionine-dependent methyltransferases | S-adenosyl-L-methionine-dependent methyltransferases | Glycine N-methyltransferase | Glycine N-methyltransferase | (Escherichia coli ) [TaxId: 562 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2 Family | Glycine N-methyltransferase | 8019898 | 4000664 | SCOP2 (2022-06-29) |
A | SCOP2 Superfamily | S-adenosyl-L-methionine-dependent methyltransferases | 8032278 | 3000118 | SCOP2 (2022-06-29) |
B | SCOP2B Superfamily | S-adenosyl-L-methionine-dependent methyltransferases | 8032278 | 3000118 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | Methyltransf_11_4 | e1xvaA1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: Methyltransf_11_4 | ECOD (1.6) |
B | Methyltransf_11_4 | e1xvaB1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: Methyltransf_11_4 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.30.46.10 | Alpha Beta | 2-Layer Sandwich | Glycine N-methyltransferase | chain A, domain 1 | CATH (4.3.0) |
A | 3.40.50.150 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Vaccinia Virus protein VP39 | CATH (4.3.0) |
B | 3.30.46.10 | Alpha Beta | 2-Layer Sandwich | Glycine N-methyltransferase | chain A, domain 1 | CATH (4.3.0) |
B | 3.40.50.150 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Vaccinia Virus protein VP39 | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF13649 | Methyltransferase domain (Methyltransf_25) | Methyltransferase domain | This family appears to be a methyltransferase domain. | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR029063 | S-adenosyl-L-methionine-dependent methyltransferase superfamily | Homologous Superfamily | |
IPR014369 | Glycine/Sarcosine N-methyltransferase | Family | |
IPR041698 | Methyltransferase domain 25 | Domain |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
glycine N-methyltransferase M-CSA #23 | Glycine N-methyltransferase (GNMT) isolated from Rattus norvegicus catalyses the transfer of a methyl group from S-adenosyl-methionine (SAM) to glycine to produce N-methylglycine (sarcosine) and S-adenosyl homocysteine (SAH). Unlike most SAM-dependent methyltransferases, GNMT is not strongly inhibited by SAH. This, coupled with no evidence of a physiological role for sarcosine, has led to the suggestion that GNMT plays a key role in modulating the SAM/SAH ratio in tissues where it is an important cofactor, and so controls methyltransferase activity. GNMT exists as a dimer of dimers. Each subunit contains a molecular basket structure and a flexible N-terminal U-loop that can block the entrance to the basket of the partner subunit of the dimer. The U-loop competes with SAM for binding at the active site and so can regulate catalytic activity. GNMT binds first to SAM, which causes a conformational change, and then to glycine. | Defined by 5 residues: TYR:A-21GLY:A-137HIS:A-142ARG:A-175TYR:A-194 | EC: 2.1.1.20 (PDB Primary Data) |