Reviewed, UniProtKB/Swiss-Prot Q29513 (GNMT_RABIT)

Names and origin

Protein names

Recommended name:
    Glycine N-methyltransferase
    EC=2.1.1.20

Gene names

Name:

GNMT

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	292 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine.
Catalytic activity	S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Tissue specificity	Abundant in liver.
Sequence similarities	Belongs to the glycine N-methyltransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Folate-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Gene Ontology (GO)
Biological process	S-adenosylmethionine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB methionine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	folic acid binding Inferred from electronic annotation. Source: UniProtKB-KW glycine N-methyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB glycine binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 292	›292	Glycine N-methyltransferase		PRO_0000087527
Regions
	Region	115 – 116	2	S-adenosyl-L-methionine binding By similarity
Sites
	Binding site	20	1	S-adenosyl-L-methionine By similarity
	Binding site	29	1	S-adenosyl-L-methionine By similarity
	Binding site	32	1	Substrate By similarity
	Binding site	39	1	S-adenosyl-L-methionine By similarity
	Binding site	63	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	84	1	S-adenosyl-L-methionine By similarity
	Binding site	137	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	176	1	Substrate By similarity
	Binding site	220	1	Substrate By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q29513-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CF36EF0379313CDA	FASTA	292	32,626
	10 20 30 40 50 60 DSVYRTRSLG VAAEGLPDQY ADGEAARVWQ LYIGDTRSRT SEYKTWLLGL LRQHGCRRVL 70 80 90 100 110 120 DVACGTGVDS IMLVEEGFSV TSVDASDKML KYALKERWNR RHEPAFDKWV IEEANWMTLD 130 140 150 160 170 180 KDVPQPAGGG FDAVICLGNS FAHLPDCKGD QSEHRQALKN IASMVRTGGL LVIDHRNYDH 190 200 210 220 230 240 ILSTLCAPGK NIYYKSDLTK DVTTSVLTVN NKAHMVTLDY TVQVPAAGQD GPPSLSKFRL 250 260 270 280 290 SYYPHCLAPF TEFLRAAFEG KCQHSVLGDF KPYQPGQAYV PCYFIHVLKR TA

References

[1]	"Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers." Ogawa H., Gomi T., Fujioka M. Comp. Biochem. Physiol. 106B:601-611(1993) [PubMed: 8281755] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13307 mRNA. Translation: BAA02567.1.
UniGene	Ocu.2139
3D structure databases
SMR	Q29513. Positions 1-292.
ModBase	Search...
Protein-protein interaction databases
STRING	Q29513.
Genome annotation databases
Ensembl	ENSOCUT00000003855; ENSOCUP00000003341; ENSOCUG00000003858; Oryctolagus cuniculus. [Genome view]
Phylogenomic databases
eggNOG	maNOG08489.
HOVERGEN	Q29513.
Enzyme and pathway databases
BRENDA	2.1.1.20. 255.
Family and domain databases
InterPro	IPR014369. Gly_N_MeTrfase. [Graphical view]
PIRSF	PIRSF000385. Gly_N-mtase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GNMT_RABIT

Accession

Primary (citable) accession number: Q29513

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)