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Reviewed, UniProtKB/Swiss-Prot P13255 (GNMT_RAT)

Last modified June 16, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycine N-methyltransferase
    EC=2.1.1.20
Alternative name(s):
    Folate-binding protein
Gene names
Name: Gnmt
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Enzyme regulation

Inhibited by 5-methyltetrahydrofolate pentaglutamate.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Tissue specificity

Abundant in liver.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 293292Glycine N-methyltransferase
PRO_0000087528

Amino acid modifications

Modified residue21N-acetylvaline Ref.1

Secondary structure

................................................... 293
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13255-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4E98C7512F0228A5

FASTA29332,549
        10         20         30         40         50         60 
MVDSVYRTRS LGVAAEGIPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCHR 

        70         80         90        100        110        120 
VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRKEPAFDK WVIEEANWLT 

       130        140        150        160        170        180 
LDKDVPAGDG FDAVICLGNS FAHLPDSKGD QSEHRLALKN IASMVRPGGL LVIDHRNYDY 

       190        200        210        220        230        240 
ILSTGCAPPG KNIYYKSDLT KDITTSVLTV NNKAHMVTLD YTVQVPGAGR DGAPGFSKFR 

       250        260        270        280        290 
LSYYPHCLAS FTELVQEAFG GRCQHSVLGD FKPYRPGQAY VPCYFIHVLK KTG 

« Hide

References

[1]"Rat glycine methyltransferase. Complete amino acid sequence deduced from a cDNA clone and characterization of the genomic DNA."
Ogawa H., Konishi K., Takata Y., Nakashima H., Fujioka M.
Eur. J. Biochem. 168:141-151(1987) [PubMed: 2822402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 2-7.
Strain: Sprague-Dawley.
[2]"Crystal structure of glycine N-methyltransferase from rat liver."
Fu Z., Hu Y., Konishi K., Takata Y., Ogawa H., Gomi T., Fujioka M., Takusagawa F.
Biochemistry 35:11985-11993(1996) [PubMed: 8810903] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Tissue: Liver.
[3]"Crystal structure of apo-glycine N-methyltransferase (GNMT)."
Pattanayek R., Newcomer M.E., Wagner C.
Protein Sci. 7:1326-1331(1998) [PubMed: 9655336] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]"Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes."
Huang Y., Komoto J., Konishi K., Takata Y., Ogawa H., Gomi T., Fujioka M., Takusagawa F.
J. Mol. Biol. 298:149-162(2000) [PubMed: 10756111] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

X06150 mRNA. Translation: CAA29508.1.
X07833 Genomic DNA. Translation: CAA30686.1.
IPIIPI00231648.
PIRS00112.
RefSeqNP_058780.1.
UniGeneRn.11142

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BHJX-ray2.50A/B2-293[»]
1D2CX-ray2.50A/B2-293[»]
1D2GX-ray2.50A/B2-293[»]
1D2HX-ray3.00A/B/C/D2-293[»]
1KIAX-ray2.80A/B/C/D2-292[»]
1NBHX-ray2.80A/B/C/D2-292[»]
1NBIX-ray3.00A/B/C/D2-292[»]
1XVAX-ray2.20A/B2-293[»]
2IDJX-ray2.35A/B/C/D2-292[»]
2IDKX-ray2.55A/B/C/D2-292[»]
DisProtDP00031.
ModBaseSearch...

PTM databases

PhosphoSiteP13255.

Proteomic databases

PRIDEP13255.

Genome annotation databases

EnsemblENSRNOG00000016349. Rattus norvegicus. [Contig view]
GeneID25134.
KEGGrno:25134.

Organism-specific databases

RGD2719. Gnmt.

Phylogenomic databases

HOVERGENP13255.
OMAP13255. KCQHSIL.

Enzyme and pathway databases

BRENDA2.1.1.20. 248.

Gene expression databases

ArrayExpressP13255.
GermOnlineENSRNOG00000016349. Rattus norvegicus.

Family and domain databases

InterProIPR014369. Gly_N_MeTrfase.
IPR013217. Methyltransf_12.
[Graphical view]
PfamPF08242. Methyltransf_12. 1 hit.
[Graphical view]
PIRSFPIRSF000385. Gly_N-mtase. 1 hit.
ProtoNetSearch...

Other Resources

NextBio605549.

Entry information

Entry nameGNMT_RAT
AccessionPrimary (citable) accession number: P13255
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents