Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyGlycine N-methyltransferase8019898 4000664 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyS-adenosyl-L-methionine-dependent methyltransferases8032278 3000118 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyS-adenosyl-L-methionine-dependent methyltransferases8032278 3000118 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF13649e1xvaA1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: PF13649ECOD (1.6)
BPF13649e1xvaB1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: PF13649ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF13649Methyltransferase domain (Methyltransf_25)Methyltransferase domainThis family appears to be a methyltransferase domain.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
GLYCINE N-METHYLTRANSFERASE

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic 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
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